{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,23]],"date-time":"2026-09-23T01:37:48Z","timestamp":1790127468842,"version":"4.0.1"},"reference-count":131,"publisher":"Springer Science and Business Media LLC","issue":"3","license":[{"start":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T00:00:00Z","timestamp":1740096000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T00:00:00Z","timestamp":1740096000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Cell Biol"],"published-print":{"date-parts":[[2025,3]]},"DOI":"10.1038\/s41556-025-01616-x","type":"journal-article","created":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T05:11:19Z","timestamp":1740114679000},"page":"449-463","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":25,"title":["Growth factor-triggered de-sialylation controls glycolipid-lectin-driven endocytosis"],"prefix":"10.1038","volume":"27","author":[{"given":"Ewan","family":"MacDonald","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3352-9173","authenticated-orcid":false,"given":"Alison","family":"Forrester","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1786-8207","authenticated-orcid":false,"given":"Cesar A.","family":"Valades-Cruz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas D.","family":"Madsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joseph H. R.","family":"Hetmanski","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Estelle","family":"Dransart","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yeap","family":"Ng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rashmi","family":"Godbole","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ananthan Akhil","family":"Shp","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ludovic","family":"Leconte","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Val\u00e9rie","family":"Chambon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Debarpan","family":"Ghosh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alexis","family":"Pinet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1478-6417","authenticated-orcid":false,"given":"Dhiraj","family":"Bhatia","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9044-3662","authenticated-orcid":false,"given":"B\u00e9rang\u00e8re","family":"Lombard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9111-8842","authenticated-orcid":false,"given":"Damarys","family":"Loew","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6203-0123","authenticated-orcid":false,"given":"Martin R.","family":"Larsen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4482-8945","authenticated-orcid":false,"given":"Hakon","family":"Leffler","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dirk J.","family":"Lefeber","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0915-5055","authenticated-orcid":false,"given":"Henrik","family":"Clausen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7043-0784","authenticated-orcid":false,"given":"Anne","family":"Blangy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2633-2324","authenticated-orcid":false,"given":"Patrick","family":"Caswell","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7582-8131","authenticated-orcid":false,"given":"Massiullah","family":"Shafaq-Zadah","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9842-6963","authenticated-orcid":false,"given":"Satyajit","family":"Mayor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0740-4465","authenticated-orcid":false,"given":"Roberto","family":"Weigert","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9091-0080","authenticated-orcid":false,"given":"Christian","family":"Wunder","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2168-0004","authenticated-orcid":false,"given":"Ludger","family":"Johannes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,2,21]]},"reference":[{"key":"1616_CR1","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1016\/j.cell.2010.06.011","volume":"141","author":"MA Lemmon","year":"2010","unstructured":"Lemmon, M. A. & Schlessinger, J. Cell signaling by receptor tyrosine kinases. Cell 141, 1117\u20131134 (2010).","journal-title":"Cell"},{"key":"1616_CR2","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1038\/nrm3048","volume":"12","author":"R Avraham","year":"2011","unstructured":"Avraham, R. & Yarden, Y. Feedback regulation of EGFR signalling: decision making by early and delayed loops. Nat. Rev. Mol. Cell Biol. 12, 104\u2013117 (2011).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"1616_CR3","doi-asserted-by":"crossref","first-page":"1252","DOI":"10.3390\/cells10051252","volume":"10","author":"Y Gao","year":"2021","unstructured":"Gao, Y., Luan, X., Melamed, J. & Brockhausen, I. Role of glycans on key cell surface receptors that regulate cell proliferation and cell death. Cells 10, 1252 (2021).","journal-title":"Cells"},{"key":"1616_CR4","doi-asserted-by":"crossref","first-page":"1781","DOI":"10.1042\/CS20160273","volume":"130","author":"M Takahashi","year":"2016","unstructured":"Takahashi, M., Hasegawa, Y., Gao, C., Kuroki, Y. & Taniguchi, N. N-glycans of growth factor receptors: their role in receptor function and disease implications. Clin. Sci. 130, 1781\u20131792 (2016).","journal-title":"Clin. Sci."},{"key":"1616_CR5","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1111\/j.1349-7006.2008.00839.x","volume":"99","author":"YY Zhao","year":"2008","unstructured":"Zhao, Y. Y. et al. Functional roles of N-glycans in cell signaling and cell adhesion in cancer. Cancer Sci. 99, 1304\u20131310 (2008).","journal-title":"Cancer Sci."},{"key":"1616_CR6","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/j.trecan.2018.05.009","volume":"4","author":"G Marsico","year":"2018","unstructured":"Marsico, G., Russo, L., Quondamatteo, F. & Pandit, A. Glycosylation and integrin regulation in cancer. Trends Cancer 4, 537\u2013552 (2018).","journal-title":"Trends Cancer"},{"key":"1616_CR7","doi-asserted-by":"crossref","first-page":"2587","DOI":"10.1016\/j.cellsig.2013.08.008","volume":"25","author":"AM Gilmour","year":"2013","unstructured":"Gilmour, A. M. et al. A novel epidermal growth factor receptor-signaling platform and its targeted translation in pancreatic cancer. Cell Signal. 25, 2587\u20132603 (2013).","journal-title":"Cell Signal."},{"key":"1616_CR8","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1007\/978-1-61779-148-2_21","volume":"753","author":"G Palmisano","year":"2011","unstructured":"Palmisano, G., Lendal, S. E. & Larsen, M. R. Titanium dioxide enrichment of sialic acid-containing glycopeptides. Methods Mol. Biol. 753, 309\u2013322 (2011).","journal-title":"Methods Mol. Biol."},{"key":"1616_CR9","doi-asserted-by":"crossref","first-page":"a005199","DOI":"10.1101\/cshperspect.a005199","volume":"3","author":"P Stanley","year":"2011","unstructured":"Stanley, P. Golgi glycosylation. Cold Spring Harb. Perspect. Biol. 3, a005199 (2011).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"1616_CR10","doi-asserted-by":"crossref","first-page":"392","DOI":"10.1016\/j.ceb.2004.06.001","volume":"16","author":"A Sorkin","year":"2004","unstructured":"Sorkin, A. Cargo recognition during clathrin-mediated endocytosis: a team effort. Curr. Opin. Cell Biol. 16, 392\u2013399 (2004).","journal-title":"Curr. Opin. Cell Biol."},{"key":"1616_CR11","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1038\/nrm3151","volume":"12","author":"HT McMahon","year":"2011","unstructured":"McMahon, H. T. & Boucrot, E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 12, 517\u2013533 (2011).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"1616_CR12","doi-asserted-by":"crossref","first-page":"a016725","DOI":"10.1101\/cshperspect.a016725","volume":"6","author":"T Kirchhausen","year":"2014","unstructured":"Kirchhausen, T., Owen, D. & Harrison, S. C. Molecular structure, function, and dynamics of clathrin-mediated membrane traffic. Cold Spring Harb. Perspect. Biol. 6, a016725 (2014).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"1616_CR13","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/nrm.2017.132","volume":"19","author":"M Kaksonen","year":"2018","unstructured":"Kaksonen, M. & Roux, A. Mechanisms of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 19, 313\u2013326 (2018).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"1616_CR14","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1146\/annurev.biochem.78.081307.110540","volume":"78","author":"GJ Doherty","year":"2009","unstructured":"Doherty, G. J. & McMahon, H. T. Mechanisms of endocytosis. Annu. Rev. Biochem. 78, 857\u2013902 (2009).","journal-title":"Annu. Rev. Biochem."},{"key":"1616_CR15","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/nrm3968","volume":"16","author":"L Johannes","year":"2015","unstructured":"Johannes, L., Parton, R. G., Bassereau, P. & Mayor, S. Building endocytic pits without clathrin. Nat. Rev. Mol. Cell Biol. 16, 311\u2013321 (2015).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"1616_CR16","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1007\/s00418-018-1678-5","volume":"150","author":"K Sandvig","year":"2018","unstructured":"Sandvig, K., Kavaliauskiene, S. & Skotland, T. Clathrin-independent endocytosis: an increasing degree of complexity. Histochem. Cell. Biol. 150, 107\u2013118 (2018).","journal-title":"Histochem. Cell. Biol."},{"key":"1616_CR17","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1016\/j.ceb.2021.03.001","volume":"71","author":"HF Renard","year":"2021","unstructured":"Renard, H. F. & Boucrot, E. Unconventional endocytic mechanisms. Curr. Opin. Cell Biol. 71, 120\u2013129 (2021).","journal-title":"Curr. Opin. Cell Biol."},{"key":"1616_CR18","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1038\/s41580-021-00375-5","volume":"22","author":"S Sigismund","year":"2021","unstructured":"Sigismund, S., Lanzetti, L., Scita, G. & Di Fiore, P. P. Endocytosis in the context-dependent regulation of individual and collective cell properties. Nat. Rev. Mol. Cell Biol. 22, 625\u2013643 (2021).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"1616_CR19","unstructured":"Cummings, R. D., Liu, F. T., Rabinovich, G. A., Stowell, S. R. & Vasta, G. R. in Essentials of Glycobiology (eds Varki, A. et al.) 491\u2013504 (Cold Spring Harbor Laboratory Press, 2022)."},{"key":"1616_CR20","doi-asserted-by":"crossref","first-page":"jcs208884","DOI":"10.1242\/jcs.208884","volume":"131","author":"L Johannes","year":"2018","unstructured":"Johannes, L., Jacob, R. & Leffler, H. Galectins at a glance. J. Cell Sci. 131, jcs208884 (2018).","journal-title":"J. Cell Sci."},{"key":"1616_CR21","doi-asserted-by":"crossref","first-page":"10119","DOI":"10.1016\/S0021-9258(18)67499-X","volume":"261","author":"H Leffler","year":"1986","unstructured":"Leffler, H. & Barondes, S. H. Specificity of binding of three soluble rat lung lectins to substituted and unsubstituted mammalian \u03b2-galactosides. J. Biol. Chem. 261, 10119\u201310126 (1986).","journal-title":"J. Biol. Chem."},{"key":"1616_CR22","doi-asserted-by":"crossref","first-page":"10109","DOI":"10.1074\/jbc.M709545200","volume":"283","author":"SR Stowell","year":"2008","unstructured":"Stowell, S. R. et al. Galectin-1, -2, and -3 exhibit differential recognition of sialylated glycans and blood group antigens. J. Biol. Chem. 283, 10109\u201310123 (2008).","journal-title":"J. Biol. Chem."},{"key":"1616_CR23","doi-asserted-by":"crossref","first-page":"5935","DOI":"10.1074\/jbc.R110.191429","volume":"286","author":"Y Zhuo","year":"2011","unstructured":"Zhuo, Y. & Bellis, S. L. Emerging role of \u03b12,6-sialic acid as a negative regulator of galectin binding and function. J. Biol. Chem. 286, 5935\u20135941 (2011).","journal-title":"J. Biol. Chem."},{"key":"1616_CR24","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1111\/j.1749-6632.2012.06517.x","volume":"1253","author":"A Varki","year":"2012","unstructured":"Varki, A. & Gagneux, P. Multifarious roles of sialic acids in immunity. Ann. N. Y. Acad. Sci. 1253, 16\u201336 (2012).","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"1616_CR25","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1007\/s00018-019-03288-x","volume":"77","author":"H L\u00e4ubli","year":"2020","unstructured":"L\u00e4ubli, H. & Varki, A. Sialic acid-binding immunoglobulin-like lectins (Siglecs) detect self-associated molecular patterns to regulate immune responses. Cell. Mol. Life Sci. 77, 593\u2013605 (2020).","journal-title":"Cell. Mol. Life Sci."},{"key":"1616_CR26","doi-asserted-by":"crossref","first-page":"120","DOI":"10.1126\/science.1102109","volume":"306","author":"EA Partridge","year":"2004","unstructured":"Partridge, E. A. et al. Regulation of cytokine receptors by Golgi N-glycan processing and endocytosis. Science 306, 120\u2013124 (2004).","journal-title":"Science"},{"key":"1616_CR27","doi-asserted-by":"crossref","first-page":"2213","DOI":"10.1242\/jcs.151159","volume":"128","author":"IR Nabi","year":"2015","unstructured":"Nabi, I. R., Shankar, J. & Dennis, J. W. The galectin lattice at a glance. J. Cell Sci. 128, 2213\u20132219 (2015).","journal-title":"J. Cell Sci."},{"key":"1616_CR28","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1016\/j.sbi.2007.09.002","volume":"17","author":"GA Rabinovich","year":"2007","unstructured":"Rabinovich, G. A., Toscano, M. A., Jackson, S. S. & Vasta, G. R. Functions of cell surface galectin\u2013glycoprotein lattices. Curr. Opin. Struct. Biol. 17, 513\u2013520 (2007).","journal-title":"Curr. Opin. Struct. Biol."},{"key":"1616_CR29","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1038\/ncb2970","volume":"16","author":"R Lakshminarayan","year":"2014","unstructured":"Lakshminarayan, R. et al. Galectin-3 drives glycosphingolipid-dependent biogenesis of clathrin-independent carriers. Nat. Cell Biol. 16, 595\u2013606 (2014).","journal-title":"Nat. Cell Biol."},{"key":"1616_CR30","doi-asserted-by":"crossref","first-page":"4792","DOI":"10.1016\/j.jmb.2016.10.027","volume":"428","author":"L Johannes","year":"2016","unstructured":"Johannes, L., Wunder, C. & Shafaq-Zadah, M. Glycolipids and lectins in endocytic uptake processes. J. Mol. Biol. 428, 4792\u20134818 (2016).","journal-title":"J. Mol. Biol."},{"key":"1616_CR31","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-020-15303-y","volume":"11","author":"HF Renard","year":"2020","unstructured":"Renard, H. F. et al. Endophilin-A3 and galectin-8 control the clathrin-independent endocytosis of CD166. Nat. Commun. 11, 1457 (2020).","journal-title":"Nat. Commun."},{"key":"1616_CR32","doi-asserted-by":"crossref","first-page":"7222","DOI":"10.1074\/jbc.RA118.001802","volume":"293","author":"MP Mathew","year":"2018","unstructured":"Mathew, M. P. & Donaldson, J. G. Distinct cargo-specific response landscapes underpin the complex and nuanced role of galectin-glycan interactions in clathrin-independent endocytosis. J. Biol. Chem. 293, 7222\u20137237 (2018).","journal-title":"J. Biol. Chem."},{"key":"1616_CR33","doi-asserted-by":"crossref","first-page":"105416","DOI":"10.1016\/j.jbc.2023.105416","volume":"299","author":"C Zhang","year":"2023","unstructured":"Zhang, C. et al. SLC3A2 N-glycosylation and Golgi remodeling regulate SLC7A amino acid exchangers and stress mitigation. J. Biol. Chem. 299, 105416 (2023).","journal-title":"J. Biol. Chem."},{"key":"1616_CR34","doi-asserted-by":"crossref","first-page":"1169","DOI":"10.3390\/biom14091169","volume":"14","author":"M Shafaq-Zadah","year":"2024","unstructured":"Shafaq-Zadah, M. et al. Exploration into galectin-3 driven endocytosis and lattices. Biomolecules 14, 1169 (2024).","journal-title":"Biomolecules"},{"key":"1616_CR35","doi-asserted-by":"crossref","first-page":"603","DOI":"10.1093\/glycob\/cwq010","volume":"20","author":"M Arabkhari","year":"2010","unstructured":"Arabkhari, M. et al. Desialylation of insulin receptors and IGF-1 receptors by neuraminidase-1 controls the net proliferative response of L6 myoblasts to insulin. Glycobiology 20, 603\u2013616 (2010).","journal-title":"Glycobiology"},{"key":"1616_CR36","doi-asserted-by":"crossref","first-page":"1197","DOI":"10.1007\/s10719-009-9239-8","volume":"26","author":"SR Amith","year":"2009","unstructured":"Amith, S. R. et al. Dependence of pathogen molecule-induced toll-like receptor activation and cell function on Neu1 sialidase. Glycoconj. J. 26, 1197\u20131212 (2009).","journal-title":"Glycoconj. J."},{"key":"1616_CR37","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1038\/s41556-018-0223-z","volume":"21","author":"P Moreno-Layseca","year":"2019","unstructured":"Moreno-Layseca, P., Icha, J., Hamidi, H. & Ivaska, J. Integrin trafficking in cells and tissues. Nat. Cell Biol. 21, 122\u2013132 (2019).","journal-title":"Nat. Cell Biol."},{"key":"1616_CR38","doi-asserted-by":"crossref","first-page":"3695","DOI":"10.1242\/jcs.095810","volume":"125","author":"RE Bridgewater","year":"2012","unstructured":"Bridgewater, R. E., Norman, J. C. & Caswell, P. T. Integrin trafficking at a glance. J. Cell Sci. 125, 3695\u20133701 (2012).","journal-title":"J. Cell Sci."},{"key":"1616_CR39","doi-asserted-by":"crossref","first-page":"491","DOI":"10.3109\/15419060009040306","volume":"7","author":"RK Pretzlaff","year":"2000","unstructured":"Pretzlaff, R. K., Xue, V. W. & Rowin, M. E. Sialidase treatment exposes the \u03b21-integrin active ligand binding site on HL60 cells and increases binding to fibronectin. Cell Adhes. Commun. 7, 491\u2013500 (2000).","journal-title":"Cell Adhes. Commun."},{"key":"1616_CR40","doi-asserted-by":"crossref","first-page":"4645","DOI":"10.1158\/0008-5472.CAN-04-3117","volume":"65","author":"EC Seales","year":"2005","unstructured":"Seales, E. C. et al. Hypersialylation of \u03b21 integrins, observed in colon adenocarcinoma, may contribute to cancer progression by up-regulating cell motility. Cancer Res. 65, 4645\u20134652 (2005).","journal-title":"Cancer Res."},{"key":"1616_CR41","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.bpj.2010.03.063","volume":"99","author":"D Pan","year":"2010","unstructured":"Pan, D. & Song, Y. Role of altered sialylation of the I-like domain of \u03b21 integrin in the binding of fibronectin to \u03b21 integrin: thermodynamics and conformational analyses. Biophys. J. 99, 208\u2013217 (2010).","journal-title":"Biophys. J."},{"key":"1616_CR42","doi-asserted-by":"crossref","first-page":"4120","DOI":"10.1096\/fj.201600665R","volume":"30","author":"S Hou","year":"2016","unstructured":"Hou, S. et al. Importance of membrane-proximal N-glycosylation on integrin \u03b21 in its activation and complex formation. FASEB J. 30, 4120\u20134131 (2016).","journal-title":"FASEB J."},{"key":"1616_CR43","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1242\/jcs.114.11.2167","volume":"114","author":"AA de Melker","year":"2001","unstructured":"de Melker, A. A., van der Horst, G., Calafat, J., Jansen, H. & Borst, J. c-Cbl ubiquitinates the EGF receptor at the plasma membrane and remains receptor associated throughout the endocytic route. J. Cell Sci. 114, 2167\u20132178 (2001).","journal-title":"J. Cell Sci."},{"key":"1616_CR44","doi-asserted-by":"crossref","first-page":"3591","DOI":"10.1091\/mbc.e04-01-0041","volume":"15","author":"E Stang","year":"2004","unstructured":"Stang, E. et al. Cbl-dependent ubiquitination is required for progression of EGF receptors into clathrin-coated pits. Mol. Biol. Cell 15, 3591\u20133604 (2004).","journal-title":"Mol. Biol. Cell"},{"key":"1616_CR45","doi-asserted-by":"crossref","first-page":"3918","DOI":"10.1073\/pnas.74.9.3918","volume":"74","author":"RM Pruss","year":"1977","unstructured":"Pruss, R. M. & Herschman, H. R. Variants of 3T3 cells lacking mitogenic response to epidermal growth factor. Proc. Natl Acad. Sci. USA 74, 3918\u20133921 (1977).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1616_CR46","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1038\/nrclinonc.2013.154","volume":"10","author":"HA Yu","year":"2013","unstructured":"Yu, H. A. & Pao, W. Targeted therapies: Afatinib\u2013new therapy option for EGFR-mutant lung cancer. Nat. Rev. Clin. Oncol. 10, 551\u2013552 (2013).","journal-title":"Nat. Rev. Clin. Oncol."},{"key":"1616_CR47","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1210\/endo-95-3-776","volume":"95","author":"RL Byyny","year":"1974","unstructured":"Byyny, R. L., Orth, D. N., Cohen, S. & Doyne, E. S. Epidermal growth factor: effects of androgens and adrenergic agents. Endocrinology 95, 776\u2013782 (1974).","journal-title":"Endocrinology"},{"key":"1616_CR48","doi-asserted-by":"crossref","first-page":"3431","DOI":"10.2147\/DDDT.S176220","volume":"12","author":"VY Glanz","year":"2018","unstructured":"Glanz, V. Y., Myasoedova, V. A., Grechko, A. V. & Orekhov, A. N. Inhibition of sialidase activity as a therapeutic approach. Drug Des. Devel. Ther. 12, 3431\u20133437 (2018).","journal-title":"Drug Des. Devel. Ther."},{"key":"1616_CR49","doi-asserted-by":"crossref","first-page":"590","DOI":"10.1021\/acschembio.1c00868","volume":"17","author":"SJ Moons","year":"2022","unstructured":"Moons, S. J. et al. Structure-activity relationship of metabolic sialic acid inhibitors and labeling reagents. ACS Chem. Biol. 17, 590\u2013597 (2022).","journal-title":"ACS Chem. Biol."},{"key":"1616_CR50","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1016\/j.ceb.2006.08.003","volume":"18","author":"MC Jones","year":"2006","unstructured":"Jones, M. C., Caswell, P. T. & Norman, J. C. Endocytic recycling pathways: emerging regulators of cell migration. Curr. Opin. Cell Biol. 18, 549\u2013557 (2006).","journal-title":"Curr. Opin. Cell Biol."},{"key":"1616_CR51","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1006\/bbrc.2001.6064","volume":"289","author":"V Furtak","year":"2001","unstructured":"Furtak, V., Hatcher, F. & Ochieng, J. Galectin-3 mediates the endocytosis of \u03b2-1 integrins by breast carcinoma cells. Biochem. Biophys. Res. Commun. 289, 845\u2013850 (2001).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"1616_CR52","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1038\/ncb3287","volume":"18","author":"M Shafaq-Zadah","year":"2016","unstructured":"Shafaq-Zadah, M. et al. Persistent cell migration and adhesion rely on retrograde transport of \u03b21 integrin. Nat. Cell Biol. 18, 54\u201364 (2016).","journal-title":"Nat. Cell Biol."},{"key":"1616_CR53","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1016\/S0065-2318(10)64007-3","volume":"64","author":"E Monti","year":"2010","unstructured":"Monti, E. et al. Sialidases in vertebrates: a family of enzymes tailored for several cell functions. Adv. Carbohydr. Chem. Biochem. 64, 403\u2013479 (2010).","journal-title":"Adv. Carbohydr. Chem. Biochem."},{"key":"1616_CR54","doi-asserted-by":"crossref","DOI":"10.1038\/srep38363","volume":"6","author":"P Maurice","year":"2016","unstructured":"Maurice, P. et al. New insights into molecular organization of human neuraminidase-1: transmembrane topology and dimerization ability. Sci Rep. 6, 38363 (2016).","journal-title":"Sci Rep."},{"key":"1616_CR55","doi-asserted-by":"crossref","first-page":"37021","DOI":"10.1074\/jbc.M404531200","volume":"279","author":"V Seyrantepe","year":"2004","unstructured":"Seyrantepe, V. et al. Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells. J. Biol. Chem. 279, 37021\u201337029 (2004).","journal-title":"J. Biol. Chem."},{"key":"1616_CR56","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1042\/BJ20070503","volume":"408","author":"G Zanchetti","year":"2007","unstructured":"Zanchetti, G. et al. Sialidase NEU3 is a peripheral membrane protein localized on the cell surface and in endosomal structures. Biochem. J. 408, 211\u2013219 (2007).","journal-title":"Biochem. J."},{"key":"1616_CR57","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1042\/bj3490343","volume":"349","author":"E Monti","year":"2000","unstructured":"Monti, E. et al. Identification and expression of NEU3, a novel human sialidase associated to the plasma membrane. Biochem. J. 349, 343\u2013351 (2000).","journal-title":"Biochem. J."},{"key":"1616_CR58","doi-asserted-by":"crossref","first-page":"1313","DOI":"10.1093\/glycob\/9.12.1313","volume":"9","author":"E Monti","year":"1999","unstructured":"Monti, E., Preti, A., Nesti, C., Ballabio, A. & Borsani, G. Expression of a novel human sialidase encoded by the NEU2 gene. Glycobiology 9, 1313\u20131321 (1999).","journal-title":"Glycobiology"},{"key":"1616_CR59","doi-asserted-by":"crossref","first-page":"3156","DOI":"10.1101\/gad.10.24.3156","volume":"10","author":"E Bonten","year":"1996","unstructured":"Bonten, E., van der Spoel, A., Fornerod, M., Grosveld, G. & d\u2019Azzo, A. Characterization of human lysosomal neuraminidase defines the molecular basis of the metabolic storage disorder sialidosis. Genes Dev. 10, 3156\u20133169 (1996).","journal-title":"Genes Dev."},{"key":"1616_CR60","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1002\/ajmg.1320010104","volume":"1","author":"J Sphranger","year":"1977","unstructured":"Sphranger, J., Gehler, J. & Cantz, M. Mucolipidosis I\u2013a sialidosis. Am. J. Med. Genet. 1, 21\u201329 (1977).","journal-title":"Am. J. Med. Genet."},{"key":"1616_CR61","doi-asserted-by":"crossref","first-page":"46172","DOI":"10.1074\/jbc.M104547200","volume":"276","author":"KE Lukong","year":"2001","unstructured":"Lukong, K. E. et al. Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail. J. Biol. Chem. 276, 46172\u201346181 (2001).","journal-title":"J. Biol. Chem."},{"key":"1616_CR62","doi-asserted-by":"crossref","first-page":"1127","DOI":"10.1093\/glycob\/cwq077","volume":"20","author":"A Albohy","year":"2010","unstructured":"Albohy, A., Li, M. D., Zheng, R. B., Zou, C. & Cairo, C. W. Insight into substrate recognition and catalysis by the human neuraminidase 3 (NEU3) through molecular modeling and site-directed mutagenesis. Glycobiology 20, 1127\u20131138 (2010).","journal-title":"Glycobiology"},{"key":"1616_CR63","doi-asserted-by":"crossref","first-page":"312","DOI":"10.1002\/jcb.240510310","volume":"51","author":"M Nunez","year":"1993","unstructured":"Nunez, M., Mayo, K. H., Starbuck, C. & Lauffenburger, D. pH sensitivity of epidermal growth factor receptor complexes. J. Cell. Biochem. 51, 312\u2013321 (1993).","journal-title":"J. Cell. Biochem."},{"key":"1616_CR64","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1126\/science.2154036","volume":"247","author":"C Sardet","year":"1990","unstructured":"Sardet, C., Counillon, L., Franchi, A. & Pouyss\u00e9gur, J. Growth factors induce phosphorylation of the Na+\/H+ antiporter, glycoprotein of 110\u2009kD. Science 247, 723\u2013726 (1990).","journal-title":"Science"},{"key":"1616_CR65","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1083\/jcb.200908086","volume":"188","author":"M Koivusalo","year":"2010","unstructured":"Koivusalo, M. et al. Amiloride inhibits macropinocytosis by lowering submembranous pH and preventing Rac1 and Cdc42 signaling. J. Cell Biol. 188, 547\u2013563 (2010).","journal-title":"J. Cell Biol."},{"key":"1616_CR66","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.semcancer.2016.12.001","volume":"43","author":"C Stock","year":"2017","unstructured":"Stock, C. & Pedersen, S. F. Roles of pH and the Na+\/H+ exchanger NHE1 in cancer: From cell biology and animal models to an emerging translational perspective? Semin. Cancer Biol. 43, 5\u201316 (2017).","journal-title":"Semin. Cancer Biol."},{"key":"1616_CR67","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1007\/s11010-020-03984-4","volume":"476","author":"L Fliegel","year":"2021","unstructured":"Fliegel, L. Role of genetic mutations of the Na+\/H+ exchanger isoform 1, in human disease and protein targeting and activity. Mol. Cell. Biochem. 476, 1221\u20131232 (2021).","journal-title":"Mol. Cell. Biochem."},{"key":"1616_CR68","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1113\/jphysiol.2007.145185","volume":"585","author":"L St\u00fcwe","year":"2007","unstructured":"St\u00fcwe, L. et al. pH dependence of melanoma cell migration: protons extruded by NHE1 dominate protons of the bulk solution. J. Physiol. 585, 351\u2013360 (2007).","journal-title":"J. Physiol."},{"key":"1616_CR69","doi-asserted-by":"crossref","first-page":"20206","DOI":"10.1074\/jbc.274.29.20206","volume":"274","author":"E Takahashi","year":"1999","unstructured":"Takahashi, E. et al. p90RSK is a serum-stimulated Na+\/H+ exchanger isoform-1 kinase. Regulatory phosphorylation of serine 703 of Na+\/H+ exchanger isoform-1. J. Biol. Chem. 274, 20206\u201320214 (1999).","journal-title":"J. Biol. Chem."},{"key":"1616_CR70","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1111\/j.1476-5381.1993.tb13607.x","volume":"109","author":"W Scholz","year":"1993","unstructured":"Scholz, W. et al. Hoe 694, a new Na+\/H+ exchange inhibitor and its effects in cardiac ischaemia. Br. J. Pharmacol. 109, 562\u2013568 (1993).","journal-title":"Br. J. Pharmacol."},{"key":"1616_CR71","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1042\/BJ20100717","volume":"432","author":"SP Lawrence","year":"2010","unstructured":"Lawrence, S. P., Holman, G. D. & Koumanov, F. Translocation of the Na+\/H+ exchanger 1 (NHE1) in cardiomyocyte responses to insulin and energy-status signalling. Biochem. J. 432, 515\u2013523 (2010).","journal-title":"Biochem. J."},{"key":"1616_CR72","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1002\/jcp.22501","volume":"226","author":"L Liu","year":"2011","unstructured":"Liu, L., Schlesinger, P. H., Slack, N. M., Friedman, P. A. & Blair, H. C. High capacity Na+\/H+ exchange activity in mineralizing osteoblasts. J. Cell. Physiol. 226, 1702\u20131712 (2011).","journal-title":"J. Cell. Physiol."},{"key":"1616_CR73","doi-asserted-by":"crossref","first-page":"2481","DOI":"10.3390\/ijms18112481","volume":"18","author":"C Iacobini","year":"2017","unstructured":"Iacobini, C., Fantauzzi, C. B., Pugliese, G. & Menini, S. Role of galectin-3 in bone cell differentiation, bone pathophysiology and vascular osteogenesis. Int. J. Mol. Sci. 18, 2481 (2017).","journal-title":"Int. J. Mol. Sci."},{"key":"1616_CR74","doi-asserted-by":"crossref","first-page":"149","DOI":"10.1016\/j.metabol.2018.02.001","volume":"83","author":"C Iacobini","year":"2018","unstructured":"Iacobini, C. et al. Galectin-3 is essential for proper bone cell differentiation and activity, bone remodeling and biomechanical competence in mice. Metabolism 83, 149\u2013158 (2018).","journal-title":"Metabolism"},{"key":"1616_CR75","doi-asserted-by":"crossref","first-page":"4899","DOI":"10.1091\/mbc.e07-04-0378","volume":"18","author":"A Chabadel","year":"2007","unstructured":"Chabadel, A. et al. CD44 and \u03b23 integrin organize two functionally distinct actin-based domains in osteoclasts. Mol. Biol. Cell 18, 4899\u20134910 (2007).","journal-title":"Mol. Biol. Cell"},{"key":"1616_CR76","doi-asserted-by":"crossref","DOI":"10.1038\/s41598-019-38497-8","volume":"9","author":"J Stegmayr","year":"2019","unstructured":"Stegmayr, J. et al. Extracellular and intracellular small-molecule galectin-3 inhibitors. Sci. Rep. 9, 2186 (2019).","journal-title":"Sci. Rep."},{"key":"1616_CR77","doi-asserted-by":"crossref","first-page":"5367","DOI":"10.1016\/j.bmc.2010.05.040","volume":"18","author":"BA Salameh","year":"2010","unstructured":"Salameh, B. A., Cumpstey, I., Sundin, A., Leffler, H. & Nilsson, U. J. 1H-1,2,3-Triazol-1-yl thiodigalactoside derivatives as high affinity galectin-3 inhibitors. Bioorg. Med. Chem. 18, 5367\u20135378 (2010).","journal-title":"Bioorg. Med. Chem."},{"key":"1616_CR78","doi-asserted-by":"crossref","first-page":"e202302348","DOI":"10.26508\/lsa.202302348","volume":"7","author":"M Roy","year":"2024","unstructured":"Roy, M. et al. Galectin-8 modulates human osteoclast activity partly through isoform-specific interactions. Life Sci. Alliance 7, e202302348 (2024).","journal-title":"Life Sci. Alliance"},{"key":"1616_CR79","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1083\/jcb.201002119","volume":"190","author":"MT Howes","year":"2010","unstructured":"Howes, M. T. et al. Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells. J. Cell Biol. 190, 675\u2013691 (2010).","journal-title":"J. Cell Biol."},{"key":"1616_CR80","doi-asserted-by":"crossref","first-page":"3418","DOI":"10.1091\/mbc.e16-03-0164","volume":"27","author":"F Aguet","year":"2016","unstructured":"Aguet, F. et al. Membrane dynamics of dividing cells imaged by lattice light-sheet microscopy. Mol. Biol. Cell 27, 3418\u20133435 (2016).","journal-title":"Mol. Biol. Cell"},{"key":"1616_CR81","doi-asserted-by":"crossref","first-page":"2044","DOI":"10.1091\/mbc.E15-01-0055","volume":"26","author":"C Kural","year":"2015","unstructured":"Kural, C. et al. Asymmetric formation of coated pits on dorsal and ventral surfaces at the leading edges of motile cells and on protrusions of immobile cells. Mol. Biol. Cell 26, 2044\u20132053 (2015).","journal-title":"Mol. Biol. Cell"},{"key":"1616_CR82","doi-asserted-by":"crossref","first-page":"757","DOI":"10.1091\/mbc.e04-08-0672","volume":"16","author":"J Sottile","year":"2005","unstructured":"Sottile, J. & Chandler, J. Fibronectin matrix turnover occurs through a caveolin-1-dependent process. Mol. Biol. Cell 16, 757\u2013768 (2005).","journal-title":"Mol. Biol. Cell"},{"key":"1616_CR83","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1038\/ncb1262","volume":"7","author":"EJ Ezratty","year":"2005","unstructured":"Ezratty, E. J., Partridge, M. A. & Gundersen, G. G. Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase. Nat. Cell Biol. 7, 581\u2013590 (2005).","journal-title":"Nat. Cell Biol."},{"key":"1616_CR84","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1016\/j.febslet.2009.03.037","volume":"583","author":"WT Chao","year":"2009","unstructured":"Chao, W. T. & Kunz, J. Focal adhesion disassembly requires clathrin-dependent endocytosis of integrins. FEBS Lett. 583, 1337\u20131343 (2009).","journal-title":"FEBS Lett."},{"key":"1616_CR85","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1083\/jcb.200904054","volume":"187","author":"EJ Ezratty","year":"2009","unstructured":"Ezratty, E. J., Bertaux, C., Marcantonio, E. E. & Gundersen, G. G. Clathrin mediates integrin endocytosis for focal adhesion disassembly in migrating cells. J. Cell Biol. 187, 733\u2013747 (2009).","journal-title":"J. Cell Biol."},{"key":"1616_CR86","doi-asserted-by":"crossref","first-page":"4039","DOI":"10.1242\/jcs.087858","volume":"124","author":"F Shi","year":"2011","unstructured":"Shi, F. & Sottile, J. MT1-MMP regulates the turnover and endocytosis of extracellular matrix fibronectin. J. Cell Sci. 124, 4039\u20134050 (2011).","journal-title":"J. Cell Sci."},{"key":"1616_CR87","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1016\/j.cell.2018.05.020","volume":"174","author":"L Almeida-Souza","year":"2018","unstructured":"Almeida-Souza, L. et al. A flat BAR protein promotes actin polymerization at the base of clathrin-coated pits. Cell 174, 325\u2013337 (2018).","journal-title":"Cell"},{"key":"1616_CR88","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1038\/s41556-021-00767-x","volume":"23","author":"P Moreno-Layseca","year":"2021","unstructured":"Moreno-Layseca, P. et al. Cargo-specific recruitment in clathrin- and dynamin-independent endocytosis. Nat. Cell Biol. 23, 1073\u20131084 (2021).","journal-title":"Nat. Cell Biol."},{"key":"1616_CR89","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1038\/nature14064","volume":"517","author":"HF Renard","year":"2015","unstructured":"Renard, H. F. et al. Endophilin-A2 functions in membrane scission in clathrin-independent endocytosis. Nature 517, 493\u2013496 (2015).","journal-title":"Nature"},{"key":"1616_CR90","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.cell.2017.05.047","volume":"170","author":"M Simunovic","year":"2017","unstructured":"Simunovic, M. et al. Friction mediates scission of tubular membranes scaffolded by BAR proteins. Cell 170, 172\u2013184 (2017).","journal-title":"Cell"},{"key":"1616_CR91","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1016\/j.ceb.2020.05.009","volume":"65","author":"M Shafaq-Zadah","year":"2020","unstructured":"Shafaq-Zadah, M., Dransart, E. & Johannes, L. Clathrin-independent endocytosis, retrograde trafficking, and cell polarity. Curr. Opin. Cell Biol. 65, 112\u2013121 (2020).","journal-title":"Curr. Opin. Cell Biol."},{"key":"1616_CR92","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/B978-0-12-417164-0.00009-4","volume":"118","author":"L Johannes","year":"2013","unstructured":"Johannes, L. & Shafaq-Zadah, M. SNAP-tagging the retrograde route. Methods Cell Biol. 118, 139\u2013155 (2013).","journal-title":"Methods Cell Biol."},{"key":"1616_CR93","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1016\/j.chembiol.2008.01.007","volume":"15","author":"A Gautier","year":"2008","unstructured":"Gautier, A. et al. An engineered protein tag for multiprotein labeling in living cells. Chem. Biol. 15, 128\u2013136 (2008).","journal-title":"Chem. Biol."},{"key":"1616_CR94","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1002\/jcp.1041240117","volume":"124","author":"J Blay","year":"1985","unstructured":"Blay, J. & Brown, K. D. Epidermal growth factor promotes the chemotactic migration of cultured rat intestinal epithelial cells. J. Cell. Physiol. 124, 107\u2013112 (1985).","journal-title":"J. Cell. Physiol."},{"key":"1616_CR95","doi-asserted-by":"crossref","first-page":"2376","DOI":"10.1038\/nprot.2017.107","volume":"12","author":"R Kaukonen","year":"2017","unstructured":"Kaukonen, R., Jacquemet, G., Hamidi, H. & Ivaska, J. Cell-derived matrices for studying cell proliferation and directional migration in a complex 3D microenvironment. Nat. Protoc. 12, 2376\u20132390 (2017).","journal-title":"Nat. Protoc."},{"key":"1616_CR96","first-page":"3591","volume":"9","author":"RF Hennigan","year":"1994","unstructured":"Hennigan, R. F., Hawker, K. L. & Ozanne, B. W. Fos-transformation activates genes associated with invasion. Oncogene 9, 3591\u20133600 (1994).","journal-title":"Oncogene"},{"key":"1616_CR97","doi-asserted-by":"crossref","first-page":"169","DOI":"10.1083\/jcb.112.1.169","volume":"112","author":"MJ Elices","year":"1991","unstructured":"Elices, M. J., Urry, L. A. & Hemler, M. E. Receptor functions for the integrin VLA-3: fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations. J. Cell Biol. 112, 169\u2013181 (1991).","journal-title":"J. Cell Biol."},{"key":"1616_CR98","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1016\/j.ccell.2022.06.011","volume":"40","author":"Y Chen","year":"2022","unstructured":"Chen, Y. et al. Oncogenic collagen I homotrimers from cancer cells bind to \u03b13\u03b21 integrin and impact tumor microbiome and immunity to promote pancreatic cancer. Cancer Cell 40, 818\u2013834 (2022).","journal-title":"Cancer Cell"},{"key":"1616_CR99","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1084\/jem.20162042","volume":"215","author":"JM Carpier","year":"2018","unstructured":"Carpier, J. M. et al. Rab6-dependent retrograde traffic of LAT controls T cell activation. J. Exp. Med. 215, 1245\u20131265 (2018).","journal-title":"J. Exp. Med."},{"key":"1616_CR100","doi-asserted-by":"crossref","first-page":"jcs244798","DOI":"10.1242\/jcs.244798","volume":"133","author":"A Blangy","year":"2020","unstructured":"Blangy, A. et al. The osteoclast cytoskeleton\u2014current understanding and therapeutic perspectives for osteoporosis. J. Cell Sci. 133, jcs244798 (2020).","journal-title":"J. Cell Sci."},{"key":"1616_CR101","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1093\/hmg\/11.12.1455","volume":"11","author":"N de Geest","year":"2002","unstructured":"de Geest, N. et al. Systemic and neurologic abnormalities distinguish the lysosomal disorders sialidosis and galactosialidosis in mice. Hum. Mol. Genet. 11, 1455\u20131464 (2002).","journal-title":"Hum. Mol. Genet."},{"key":"1616_CR102","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1158\/0008-5472.CAN-12-4031","volume":"73","author":"SR Amith","year":"2013","unstructured":"Amith, S. R. & Fliegel, L. Regulation of the Na+\/H+ exchanger (NHE1) in breast cancer metastasis. Cancer Res. 73, 1259\u20131264 (2013).","journal-title":"Cancer Res."},{"key":"1616_CR103","doi-asserted-by":"crossref","first-page":"1418","DOI":"10.1074\/mcp.RA119.001896","volume":"19","author":"I Boll","year":"2020","unstructured":"Boll, I., Jensen, P., Schw\u00e4mmle, V. & Larsen, M. R. Depolarization-dependent induction of site-specific changes in sialylation on N-linked glycoproteins in rat nerve terminals. Mol. Cell. Proteomics 19, 1418\u20131435 (2020).","journal-title":"Mol. Cell. Proteomics"},{"key":"1616_CR104","volume":"9","author":"C Abe","year":"2019","unstructured":"Abe, C., Yi, Y., Hane, M., Kitajima, K. & Sato, C. Acute stress-induced change in polysialic acid levels mediated by sialidase in mouse brain. Sci Rep. 9, 9950 (2019).","journal-title":"Sci Rep."},{"key":"1616_CR105","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/jid.1963.1","volume":"40","author":"S Cohen","year":"1963","unstructured":"Cohen, S. & Elliott, G. A. The stimulation of epidermal keratinization by a protein isolated from the submaxillary gland of the mouse. J. Invest. Dermatol. 40, 1\u20135 (1963).","journal-title":"J. Invest. Dermatol."},{"key":"1616_CR106","doi-asserted-by":"crossref","first-page":"2760","DOI":"10.1073\/pnas.0409817102","volume":"102","author":"S Sigismund","year":"2005","unstructured":"Sigismund, S. et al. Clathrin-independent endocytosis of ubiquitinated cargos. Proc. Natl Acad. Sci. USA 102, 2760\u20132765 (2005).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"1616_CR107","doi-asserted-by":"publisher","unstructured":"Shafaq-Zadah, M. et al. Spatial N-glycan rearrangement on a5b1 integrin nucleates galectin-3 oligomers to determine endocytic fate. Preprint at bioRxiv https:\/\/doi.org\/10.1101\/2023.10.27.564026 (2023).","DOI":"10.1101\/2023.10.27.564026"},{"key":"1616_CR108","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1146\/annurev-pathol-012414-040438","volume":"10","author":"SR Stowell","year":"2015","unstructured":"Stowell, S. R., Ju, T. & Cummings, R. D. Protein glycosylation in cancer. Annu. Rev. Pathol. 10, 473\u2013510 (2015).","journal-title":"Annu. Rev. Pathol."},{"key":"1616_CR109","doi-asserted-by":"crossref","first-page":"1640","DOI":"10.1016\/j.bbagen.2015.12.017","volume":"1860","author":"AP Willems","year":"2016","unstructured":"Willems, A. P., van Engelen, B. G. & Lefeber, D. J. Genetic defects in the hexosamine and sialic acid biosynthesis pathway. Biochim. Biophys. Acta 1860, 1640\u20131654 (2016).","journal-title":"Biochim. Biophys. Acta"},{"key":"1616_CR110","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1038\/s41573-020-00093-1","volume":"20","author":"BAH Smith","year":"2021","unstructured":"Smith, B. A. H. & Bertozzi, C. R. The clinical impact of glycobiology: targeting selectins, Siglecs and mammalian glycans. Nat. Rev. Drug Discov. 20, 217\u2013243 (2021).","journal-title":"Nat. Rev. Drug Discov."},{"key":"1616_CR111","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1248\/bpb1978.11.146","volume":"11","author":"T Hayashi","year":"1988","unstructured":"Hayashi, T. & Sakamoto, S. Radioimmunoassay of human epidermal growth factor\u2013hEGF levels in human body fluids. J. Pharmacobiodyn. 11, 146\u2013151 (1988).","journal-title":"J. Pharmacobiodyn."},{"key":"1616_CR112","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1677\/joe.0.0960287","volume":"96","author":"JM Beardmore","year":"1983","unstructured":"Beardmore, J. M. & Richards, R. C. Concentrations of epidermal growth factor in mouse milk throughout lactation. J. Endocrinol. 96, 287\u2013292 (1983).","journal-title":"J. Endocrinol."},{"key":"1616_CR113","doi-asserted-by":"crossref","first-page":"1854","DOI":"10.1210\/endo.135.5.7956907","volume":"135","author":"M Grau","year":"1994","unstructured":"Grau, M., Rodriguez, C., Soley, M. & Ramirez, I. Relationship between epidermal growth factor in mouse submandibular glands, plasma, and bile: effects of catecholamines and fasting. Endocrinology 135, 1854\u20131862 (1994).","journal-title":"Endocrinology"},{"key":"1616_CR114","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1002\/(SICI)1097-0045(19970901)32:4<234::AID-PROS2>3.0.CO;2-J","volume":"32","author":"PH Gann","year":"1997","unstructured":"Gann, P. H., Chatterton, R., Vogelsong, K., Grayhack, J. T. & Lee, C. Epidermal growth factor-related peptides in human prostatic fluid: sources of variability in assay results. Prostate 32, 234\u2013240 (1997).","journal-title":"Prostate"},{"key":"1616_CR115","doi-asserted-by":"crossref","first-page":"2553","DOI":"10.1002\/pmic.200600784","volume":"7","author":"P Poullet","year":"2007","unstructured":"Poullet, P., Carpentier, S. & Barillot, E. myProMS, a web server for management and validation of mass spectrometry-based proteomic data. Proteomics 7, 2553\u20132556 (2007).","journal-title":"Proteomics"},{"key":"1616_CR116","doi-asserted-by":"crossref","first-page":"1719","DOI":"10.1007\/s13361-016-1460-7","volume":"27","author":"M The","year":"2016","unstructured":"The, M., MacCoss, M. J., Noble, W. S. & K\u00e4ll, L. Fast and accurate protein false discovery rates on large-scale proteomics data sets with Percolator 3.0. J. Am. Soc. Mass Spectrom. 27, 1719\u20131727 (2016).","journal-title":"J. Am. Soc. Mass Spectrom."},{"key":"1616_CR117","doi-asserted-by":"crossref","first-page":"3572","DOI":"10.1002\/pmic.201100120","volume":"11","author":"B Valot","year":"2011","unstructured":"Valot, B., Langella, O., Nano, E. & Zivy, M. MassChroQ: a versatile tool for mass spectrometry quantification. Proteomics 11, 3572\u20133577 (2011).","journal-title":"Proteomics"},{"key":"1616_CR118","doi-asserted-by":"crossref","first-page":"e21800","DOI":"10.1371\/journal.pone.0021800","volume":"6","author":"F Supek","year":"2011","unstructured":"Supek, F., Bo\u0161njak, M., \u0160kunca, N. & \u0160muc, T. REVIGO summarizes and visualizes long lists of gene ontology terms. PLoS ONE 6, e21800 (2011).","journal-title":"PLoS ONE"},{"key":"1616_CR119","doi-asserted-by":"crossref","first-page":"D543","DOI":"10.1093\/nar\/gkab1038","volume":"50","author":"Y Perez-Riverol","year":"2022","unstructured":"Perez-Riverol, Y. et al. The PRIDE database resources in 2022: a hub for mass spectrometry-based proteomics evidences. Nucleic Acids Res. 50, D543\u2013d552 (2022).","journal-title":"Nucleic Acids Res."},{"key":"1616_CR120","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1038\/nprot.2016.165","volume":"12","author":"LA Lonowski","year":"2017","unstructured":"Lonowski, L. A. et al. Genome editing using FACS enrichment of nuclease-expressing cells and indel detection by amplicon analysis. Nat. Protoc. 12, 581\u2013603 (2017).","journal-title":"Nat. Protoc."},{"key":"1616_CR121","doi-asserted-by":"crossref","first-page":"1708","DOI":"10.1126\/science.1064829","volume":"294","author":"E Cukierman","year":"2001","unstructured":"Cukierman, E., Pankov, R., Stevens, D. R. & Yamada, K. M. Taking cell-matrix adhesions to the third dimension. Science 294, 1708\u20131712 (2001).","journal-title":"Science"},{"key":"1616_CR122","doi-asserted-by":"crossref","first-page":"1257998","DOI":"10.1126\/science.1257998","volume":"346","author":"BC Chen","year":"2014","unstructured":"Chen, B. C. et al. Lattice light-sheet microscopy: imaging molecules to embryos at high spatiotemporal resolution. Science 346, 1257998 (2014).","journal-title":"Science"},{"key":"1616_CR123","doi-asserted-by":"publisher","unstructured":"Sofroniew, N. et al. napari: A multi-dimensional image viewer for Python. Zenodo https:\/\/doi.org\/10.5281\/zenodo.3555620 (2025).","DOI":"10.5281\/zenodo.3555620"},{"key":"1616_CR124","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1038\/nmeth.1237","volume":"5","author":"K Jaqaman","year":"2008","unstructured":"Jaqaman, K. et al. Robust single-particle tracking in live-cell time-lapse sequences. Nat. Methods 5, 695\u2013702 (2008).","journal-title":"Nat. Methods"},{"key":"1616_CR125","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1109\/TMI.2009.2033991","volume":"29","author":"J Boulanger","year":"2010","unstructured":"Boulanger, J. et al. Patch-based nonlocal functional for denoising fluorescence microscopy image sequences. IEEE Trans. Med. Imaging 29, 442\u2013454 (2010).","journal-title":"IEEE Trans. Med. Imaging"},{"key":"1616_CR126","doi-asserted-by":"crossref","first-page":"1328","DOI":"10.1038\/s41592-022-01642-9","volume":"19","author":"S Prigent","year":"2022","unstructured":"Prigent, S. et al. BioImageIT: open-source framework for integration of image data management with analysis. Nat. Methods 19, 1328\u20131330 (2022).","journal-title":"Nat. Methods"},{"key":"1616_CR127","volume":"10","author":"Z Wang","year":"2019","unstructured":"Wang, Z. et al. Syngeneic animal models of tobacco-associated oral cancer reveal the activity of in situ anti-CTLA-4. Nat. Commun. 10, 5546 (2019).","journal-title":"Nat. Commun."},{"key":"1616_CR128","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1158\/1940-6207.CAPR-11-0502","volume":"5","author":"L Vitale-Cross","year":"2012","unstructured":"Vitale-Cross, L. et al. Metformin prevents the development of oral squamous cell carcinomas from carcinogen-induced premalignant lesions. Cancer Prev. Res. 5, 562\u2013573 (2012).","journal-title":"Cancer Prev. Res."},{"key":"1616_CR129","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-020-19401-9","volume":"11","author":"I Sequeira","year":"2020","unstructured":"Sequeira, I. et al. Genomic landscape and clonal architecture of mouse oral squamous cell carcinomas dictate tumour ecology. Nat. Commun. 11, 5671 (2020).","journal-title":"Nat. Commun."},{"key":"1616_CR130","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-018-05367-2","volume":"9","author":"M Padilla-Rodriguez","year":"2018","unstructured":"Padilla-Rodriguez, M. et al. The actin cytoskeletal architecture of estrogen receptor positive breast cancer cells suppresses invasion. Nat. Commun. 9, 2980 (2018).","journal-title":"Nat. Commun."},{"key":"1616_CR131","doi-asserted-by":"crossref","first-page":"778887","DOI":"10.3389\/fcell.2021.778887","volume":"9","author":"J Maurin","year":"2021","unstructured":"Maurin, J. et al. The \u03b2-tubulin isotype TUBB6 controls microtubule and actin dynamics in osteoclasts. Front. Cell. Dev. Biol. 9, 778887 (2021).","journal-title":"Front. Cell. Dev. Biol."}],"updated-by":[{"DOI":"10.1038\/s41556-025-01643-8","type":"correction","label":"Correction","source":"publisher","updated":{"date-parts":[[2025,2,25]],"date-time":"2025-02-25T00:00:00Z","timestamp":1740441600000}}],"container-title":["Nature Cell Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41556-025-01616-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41556-025-01616-x","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41556-025-01616-x.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,3,13]],"date-time":"2025-03-13T19:03:41Z","timestamp":1741892621000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41556-025-01616-x"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,2,21]]},"references-count":131,"journal-issue":{"issue":"3","published-print":{"date-parts":[[2025,3]]}},"alternative-id":["1616"],"URL":"https:\/\/doi.org\/10.1038\/s41556-025-01616-x","relation":{"has-preprint":[{"id-type":"doi","id":"10.1101\/2023.09.12.557183","asserted-by":"object"}]},"ISSN":["1465-7392","1476-4679"],"issn-type":[{"value":"1465-7392","type":"print"},{"value":"1476-4679","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,2,21]]},"assertion":[{"value":"2 January 2024","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"9 January 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"21 February 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"25 February 2025","order":4,"name":"change_date","label":"Change Date","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"Correction","order":5,"name":"change_type","label":"Change Type","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"A Correction to this paper has been published:","order":6,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"https:\/\/doi.org\/10.1038\/s41556-025-01643-8","URL":"https:\/\/doi.org\/10.1038\/s41556-025-01643-8","order":7,"name":"change_details","label":"Change Details","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"H.L. is a shareholder in Galecto Biotech AB, a company that is developing galectin inhibitors. The other authors declare no conflicts of interest.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}