{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T04:21:37Z","timestamp":1790050897891,"version":"4.0.1"},"reference-count":59,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2015,12,18]],"date-time":"2015-12-18T00:00:00Z","timestamp":1450396800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"},{"start":{"date-parts":[[2015,12,18]],"date-time":"2015-12-18T00:00:00Z","timestamp":1450396800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Kindlins are FERM-containing cytoplasmic proteins that regulate integrin-mediated cell-cell and cell-extracellular matrix (ECM) attachments. Kindlin-3 is expressed in hematopoietic cells, platelets and endothelial cells. Studies have shown that kindlin-3 stabilizes cell adhesion mediated by \u00df1, \u00df2 and \u00df3 integrins. Apart from integrin cytoplasmic tails, kindlins are known to interact with other cytoplasmic proteins. Here we demonstrate that kindlin-3 can associate with ribosome via the receptor for activated-C kinase 1 (RACK1) scaffold protein based on immunoprecipitation, ribosome binding and proximity ligation assays. We show that kindlin-3 regulates c-Myc protein expression in the human chronic myeloid leukemia cell line K562. Cell proliferation was reduced following siRNA reduction of kindlin-3 expression and a significant reduction in tumor mass was observed in xenograft experiments. Mechanistically, kindlin-3 is involved in integrin \u03b15\u00df1-Akt-mTOR-p70S6K signaling; however, its regulation of c-Myc protein expression could be independent of this signaling axis.<\/jats:p>","DOI":"10.1038\/srep18491","type":"journal-article","created":{"date-parts":[[2015,12,18]],"date-time":"2015-12-18T10:11:55Z","timestamp":1450433515000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":16,"title":["Kindlin-3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells"],"prefix":"10.1038","volume":"5","author":[{"given":"Jing","family":"Qu","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rya","family":"Ero","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chen","family":"Feng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Li-Teng","family":"Ong","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui-Foon","family":"Tan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui-Shan","family":"Lee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muhammad HB","family":"Ismail","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wen-Ting","family":"Bu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Srikanth","family":"Nama","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Prabha","family":"Sampath","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yong-Gui","family":"Gao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suet-Mien","family":"Tan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2015,12,18]]},"reference":[{"key":"BFsrep18491_CR1","doi-asserted-by":"publisher","first-page":"504","DOI":"10.1016\/j.tcb.2009.07.006","volume":"19","author":"A Meves","year":"2009","unstructured":"Meves, A., Stremmel, C., Gottschalk, K. & Fassler, R. The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol 19, 504\u2013513 (2009).","journal-title":"Trends Cell Biol"},{"key":"BFsrep18491_CR2","doi-asserted-by":"publisher","first-page":"1203","DOI":"10.1038\/embor.2008.202","volume":"9","author":"H Larjava","year":"2008","unstructured":"Larjava, H., Plow, E. F. & Wu, C. Kindlins: essential regulators of integrin signalling and cell-matrix adhesion. EMBO reports 9, 1203\u20131208 (2008).","journal-title":"EMBO reports"},{"key":"BFsrep18491_CR3","doi-asserted-by":"publisher","first-page":"6","DOI":"10.1007\/s11684-014-0317-3","volume":"8","author":"F Ye","year":"2014","unstructured":"Ye, F., Snider, A. K. & Ginsberg, M. H. Talin and kindlin: the one-two punch in integrin activation. Front Med 8, 6\u201316 (2014).","journal-title":"Front Med"},{"key":"BFsrep18491_CR4","doi-asserted-by":"publisher","first-page":"895","DOI":"10.1126\/science.1163865","volume":"324","author":"M Moser","year":"2009","unstructured":"Moser, M., Legate, K. R., Zent, R. & Fassler, R. The tail of integrins, talin and kindlins. Science 324, 895\u2013899 (2009).","journal-title":"Science"},{"key":"BFsrep18491_CR5","doi-asserted-by":"publisher","first-page":"3142","DOI":"10.1016\/j.yexcr.2006.06.030","volume":"312","author":"S Ussar","year":"2006","unstructured":"Ussar, S., Wang, H. V., Linder, S., Fassler, R. & Moser, M. The Kindlins: subcellular localization and expression during murine development. Exp Cell Res 312, 3142\u20133151 (2006).","journal-title":"Exp Cell Res"},{"key":"BFsrep18491_CR6","doi-asserted-by":"publisher","first-page":"18640","DOI":"10.1074\/jbc.M109.085746","volume":"285","author":"K Bialkowska","year":"2010","unstructured":"Bialkowska, K. et al. The integrin co-activator kindlin-3 is expressed and functional in a non-hematopoietic cell, the endothelial cell. J Biol Chem 285, 18640\u201318649 (2010).","journal-title":"J Biol Chem"},{"key":"BFsrep18491_CR7","doi-asserted-by":"publisher","first-page":"925","DOI":"10.1093\/hmg\/ddg097","volume":"12","author":"F Jobard","year":"2003","unstructured":"Jobard, F. et al. Identification of mutations in a new gene encoding a FERM family protein with a pleckstrin homology domain in Kindler syndrome. Hum Mol Genet 12, 925\u2013935 (2003).","journal-title":"Hum Mol Genet"},{"key":"BFsrep18491_CR8","doi-asserted-by":"publisher","first-page":"750","DOI":"10.1038\/embor.2012.88","volume":"13","author":"Y Yu","year":"2012","unstructured":"Yu, Y. et al. Kindlin 2 forms a transcriptional complex with b-catenin and TCF4 to enhance Wnt signalling. EMBO reports 13, 750\u2013758 (2012).","journal-title":"EMBO reports"},{"key":"BFsrep18491_CR9","doi-asserted-by":"publisher","first-page":"1325","DOI":"10.1101\/gad.469408","volume":"22","author":"E Montanez","year":"2008","unstructured":"Montanez, E. et al. Kindlin-2 controls bidirectional signaling of integrins. Genes Dev 22, 1325\u20131330 (2008).","journal-title":"Genes Dev"},{"key":"BFsrep18491_CR10","doi-asserted-by":"publisher","first-page":"300","DOI":"10.1038\/nm.1921","volume":"15","author":"M Moser","year":"2009","unstructured":"Moser, M. et al. Kindlin-3 is required for b2 integrin-mediated leukocyte adhesion to endothelial cells. Nat Med 15, 300\u2013305 (2009).","journal-title":"Nat Med"},{"key":"BFsrep18491_CR11","doi-asserted-by":"publisher","first-page":"4011","DOI":"10.1182\/blood-2009-10-239269","volume":"115","author":"NL Malinin","year":"2010","unstructured":"Malinin, N. L., Plow, E. F. & Byzova, T. V. Kindlins in FERM adhesion. Blood 115, 4011\u20134017 (2010).","journal-title":"Blood"},{"key":"BFsrep18491_CR12","doi-asserted-by":"publisher","first-page":"325","DOI":"10.1038\/nm1722","volume":"14","author":"M Moser","year":"2008","unstructured":"Moser, M., Nieswandt, B., Ussar, S., Pozgajova, M. & Fassler, R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med 14, 325\u2013330 (2008).","journal-title":"Nat Med"},{"key":"BFsrep18491_CR13","doi-asserted-by":"publisher","first-page":"24585","DOI":"10.1074\/jbc.M111.336743","volume":"287","author":"K Bledzka","year":"2012","unstructured":"Bledzka, K. et al. Spatial coordination of kindlin-2 with talin head domain in interaction with integrin \u00df cytoplasmic tails. The Journal of biological chemistry 287, 24585\u201324594 (2012).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR14","doi-asserted-by":"publisher","first-page":"2288","DOI":"10.1016\/j.cub.2013.09.050","volume":"23","author":"F Ye","year":"2013","unstructured":"Ye, F. et al. The mechanism of kindlin-mediated activation of integrin \u03b1IIb\u00df3. Current biology: CB 23, 2288\u20132295 (2013).","journal-title":"Current biology: CB"},{"key":"BFsrep18491_CR15","doi-asserted-by":"publisher","first-page":"2056","DOI":"10.1038\/ncomms3056","volume":"4","author":"H Patel","year":"2013","unstructured":"Patel, H. et al. Kindlin-1 regulates mitotic spindle formation by interacting with integrins and Plk-1. Nat Commun 4, 2056 (2013).","journal-title":"Nat Commun"},{"key":"BFsrep18491_CR16","doi-asserted-by":"publisher","first-page":"2491","DOI":"10.1182\/blood-2013-04-497669","volume":"122","author":"E Pluskota","year":"2013","unstructured":"Pluskota, E. et al. Kindlin-2 regulates hemostasis by controlling endothelial cell surface expression of ADP\/AMP catabolic enzymes via a clathrin-dependent mechanism. Blood 122, 2491\u20132499 (2013).","journal-title":"Blood"},{"key":"BFsrep18491_CR17","doi-asserted-by":"publisher","first-page":"350","DOI":"10.1038\/nm.3490","volume":"20","author":"E Rognoni","year":"2014","unstructured":"Rognoni, E. et al. Kindlin-1 controls Wnt and TGF-\u00df availability to regulate cutaneous stem cell proliferation. Nature medicine 20, 350\u2013359 (2014).","journal-title":"Nature medicine"},{"key":"BFsrep18491_CR18","doi-asserted-by":"publisher","first-page":"353","DOI":"10.1016\/j.cell.2008.05.033","volume":"134","author":"M Kruger","year":"2008","unstructured":"Kruger, M. et al. SILAC mouse for quantitative proteomics uncovers kindlin-3 as an essential factor for red blood cell function. Cell 134, 353\u2013364 (2008).","journal-title":"Cell"},{"key":"BFsrep18491_CR19","doi-asserted-by":"publisher","first-page":"791","DOI":"10.1182\/blood-2005-11-007799","volume":"108","author":"EM Pasini","year":"2006","unstructured":"Pasini, E. M. et al. In-depth analysis of the membrane and cytosolic proteome of red blood cells. Blood 108, 791\u2013801 (2006).","journal-title":"Blood"},{"key":"BFsrep18491_CR20","doi-asserted-by":"publisher","first-page":"883","DOI":"10.1083\/jcb.201007141","volume":"192","author":"S Schmidt","year":"2011","unstructured":"Schmidt, S. et al. Kindlin-3-mediated signaling from multiple integrin classes is required for osteoclast-mediated bone resorption. The Journal of cell biology 192, 883\u2013897 (2011).","journal-title":"The Journal of cell biology"},{"key":"BFsrep18491_CR21","doi-asserted-by":"publisher","first-page":"2260","DOI":"10.1096\/fj.13-244004","volume":"28","author":"K Sossey-Alaoui","year":"2014","unstructured":"Sossey-Alaoui, K. et al. Kindlin-3 enhances breast cancer progression and metastasis by activating Twist-mediated angiogenesis. FASEB journal 28, 2260\u20132271 (2014).","journal-title":"FASEB journal"},{"key":"BFsrep18491_CR22","doi-asserted-by":"publisher","first-page":"8970","DOI":"10.18632\/oncotarget.2125","volume":"5","author":"I Djaafri","year":"2014","unstructured":"Djaafri, I. et al. A novel tumor suppressor function of Kindlin-3 in solid cancer. Oncotarget 5, 8970\u20138985 (2014).","journal-title":"Oncotarget"},{"key":"BFsrep18491_CR23","doi-asserted-by":"publisher","first-page":"3156","DOI":"10.1182\/blood-2013-08-520627","volume":"123","author":"A Kasirer-Friede","year":"2014","unstructured":"Kasirer-Friede, A. et al. ADAP interactions with talin and kindlin promote platelet integrin \u03b1IIb\u00df3 activation and stable fibrinogen binding. Blood 123, 3156\u20133165 (2014).","journal-title":"Blood"},{"key":"BFsrep18491_CR24","doi-asserted-by":"publisher","first-page":"10714","DOI":"10.1074\/jbc.M111.299594","volume":"287","author":"C Feng","year":"2012","unstructured":"Feng, C. et al. Kindlin-3 mediates integrin aLb2 outside-in signaling and it interacts with scaffold protein receptor for activated-C kinase 1 (RACK1). J Biol Chem 287, 10714\u201310726 (2012).","journal-title":"J Biol Chem"},{"key":"BFsrep18491_CR25","doi-asserted-by":"publisher","first-page":"1626","DOI":"10.1128\/MCB.01718-08","volume":"29","author":"SM Coyle","year":"2009","unstructured":"Coyle, S. M., Gilbert, W. V. & Doudna, J. A. Direct link between RACK1 function and localization at the ribosome in vivo. Mol Cell Biol 29, 1626\u20131634 (2009).","journal-title":"Mol Cell Biol"},{"key":"BFsrep18491_CR26","doi-asserted-by":"publisher","first-page":"867","DOI":"10.1107\/S1744309112027480","volume":"68","author":"D Ruiz Carrillo","year":"2012","unstructured":"Ruiz Carrillo, D. et al. Structure of human Rack1 protein at a resolution of 2.45 A. Acta Crystallogr Sect F Struct Biol Cryst Commun 68, 867\u2013872 (2012).","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"BFsrep18491_CR27","doi-asserted-by":"publisher","first-page":"1261","DOI":"10.1124\/mol.62.6.1261","volume":"62","author":"A McCahill","year":"2002","unstructured":"McCahill, A., Warwicker, J., Bolger, G. B., Houslay, M. D. & Yarwood, S. J. The RACK1 scaffold protein: a dynamic cog in cell response mechanisms. Mol Pharmacol 62, 1261\u20131273 (2002).","journal-title":"Mol Pharmacol"},{"key":"BFsrep18491_CR28","doi-asserted-by":"publisher","first-page":"2787","DOI":"10.1016\/j.febslet.2012.04.048","volume":"586","author":"TJ Gibson","year":"2012","unstructured":"Gibson, T. J. RACK1 research\u2014ships passing in the night? FEBS letters 586, 2787\u20132789 (2012).","journal-title":"FEBS letters"},{"key":"BFsrep18491_CR29","doi-asserted-by":"publisher","first-page":"2379","DOI":"10.1074\/jbc.273.4.2379","volume":"273","author":"J Liliental","year":"1998","unstructured":"Liliental, J. & Chang, D. D. Rack1, a receptor for activated protein kinase C, interacts with integrin \u00df subunit. J Biol Chem 273, 2379\u20132383 (1998).","journal-title":"J Biol Chem"},{"key":"BFsrep18491_CR30","doi-asserted-by":"publisher","first-page":"4041","DOI":"10.1128\/MCB.01868-05","volume":"26","author":"PA Kiely","year":"2006","unstructured":"Kiely, P. A., O\u2019Gorman, D., Luong, K., Ron, D. & O\u2019Connor, R. Insulin-like growth factor I controls a mutually exclusive association of RACK1 with protein phosphatase 2A and \u00df1 integrin to promote cell migration. Molecular and cellular biology 26, 4041\u20134051 (2006).","journal-title":"Molecular and cellular biology"},{"key":"BFsrep18491_CR31","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1091\/mbc.e02-03-0142","volume":"14","author":"EA Cox","year":"2003","unstructured":"Cox, E. A., Bennin, D., Doan, A. T., O\u2019Toole, T. & Huttenlocher, A. RACK1 regulates integrin-mediated adhesion, protrusion and chemotactic cell migration via its Src-binding site. Mol Biol Cell 14, 658\u2013669 (2003).","journal-title":"Mol Biol Cell"},{"key":"BFsrep18491_CR32","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1016\/S0092-8674(04)00456-8","volume":"117","author":"CL De Hoog","year":"2004","unstructured":"De Hoog, C. L., Foster, L. J. & Mann, M. RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117, 649\u2013662 (2004).","journal-title":"Cell"},{"key":"BFsrep18491_CR33","doi-asserted-by":"publisher","first-page":"54","DOI":"10.4161\/sgtp.2.1.15137","volume":"2","author":"B Serrels","year":"2011","unstructured":"Serrels, B., Sandilands, E. & Frame, M. C. Signaling of the direction-sensing FAK\/RACK1\/PDE4D5 complex to the small GTPase Rap1. Small GTPases 2, 54\u201361 (2011).","journal-title":"Small GTPases"},{"key":"BFsrep18491_CR34","doi-asserted-by":"publisher","first-page":"2554","DOI":"10.1172\/JCI58488","volume":"122","author":"Y Ruan","year":"2012","unstructured":"Ruan, Y. et al. Ribosomal RACK1 promotes chemoresistance and growth in human hepatocellular carcinoma. The Journal of clinical investigation 122, 2554\u20132566 ((2012).","journal-title":"The Journal of clinical investigation"},{"key":"BFsrep18491_CR35","doi-asserted-by":"publisher","first-page":"2683","DOI":"10.1093\/nar\/gkr1083","volume":"40","author":"T Kouba","year":"2012","unstructured":"Kouba, T., Rutkai, E., Karaskova, M. & Valasek, L. The eIF3c\/NIP1 PCI domain interacts with RNA and RACK1\/ASC1 and promotes assembly of translation preinitiation complexes. Nucleic Acids Res 40, 2683\u20132699 (2012).","journal-title":"Nucleic Acids Res"},{"key":"BFsrep18491_CR36","doi-asserted-by":"publisher","first-page":"579","DOI":"10.1038\/nature02160","volume":"426","author":"M Ceci","year":"2003","unstructured":"Ceci, M. et al. Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly. Nature 426, 579\u2013584 (2003).","journal-title":"Nature"},{"key":"BFsrep18491_CR37","doi-asserted-by":"publisher","first-page":"1086","DOI":"10.1016\/j.cell.2014.10.041","volume":"159","author":"K Majzoub","year":"2014","unstructured":"Majzoub, K. et al. RACK1 Controls IRES-Mediated Translation of Viruses. Cell 159, 1086\u20131095 (2014).","journal-title":"Cell"},{"key":"BFsrep18491_CR38","doi-asserted-by":"publisher","first-page":"40012","DOI":"10.1074\/jbc.M112.380469","volume":"287","author":"Y Zhao","year":"2012","unstructured":"Zhao, Y. et al. Regulation of cell adhesion and migration by Kindlin-3 cleavage by calpain. The Journal of biological chemistry 287, 40012\u201340020 (2012).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR39","doi-asserted-by":"publisher","first-page":"1203","DOI":"10.1126\/science.1194294","volume":"330","author":"A Ben-Shem","year":"2010","unstructured":"Ben-Shem, A., Jenner, L., Yusupova, G. & Yusupov, M. Crystal structure of the eukaryotic ribosome. Science 330, 1203\u20131209 (2010).","journal-title":"Science"},{"key":"BFsrep18491_CR40","doi-asserted-by":"publisher","first-page":"1524","DOI":"10.1126\/science.1212642","volume":"334","author":"A Ben-Shem","year":"2011","unstructured":"Ben-Shem, A. et al. The structure of the eukaryotic ribosome at 3.0 A resolution. Science 334, 1524\u20131529 (2011).","journal-title":"Science"},{"key":"BFsrep18491_CR41","doi-asserted-by":"publisher","first-page":"32596","DOI":"10.1074\/jbc.M602768200","volume":"281","author":"DA Palmer","year":"2006","unstructured":"Palmer, D. A., Thompson, J. K., Li, L., Prat, A. & Wang, P. Gib2, a novel Gbeta-like\/RACK1 homolog, functions as a Gbeta subunit in cAMP signaling and is essential in Cryptococcus neoformans. The Journal of biological chemistry 281, 32596\u201332605 (2006).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR42","doi-asserted-by":"publisher","first-page":"8688","DOI":"10.1038\/srep08688","volume":"5","author":"R Ero","year":"2015","unstructured":"Ero, R. et al. Crystal structure of Gib2, a signal-transducing protein scaffold associated with ribosomes in Cryptococcus neoformans. Sci Rep 5, 8688 (2015).","journal-title":"Sci Rep"},{"key":"BFsrep18491_CR43","doi-asserted-by":"publisher","first-page":"12202","DOI":"10.1074\/jbc.M113.537183","volume":"289","author":"Y Wang","year":"2014","unstructured":"Wang, Y. et al. Noncanonical Gbeta Gib2 is a scaffolding protein promoting cAMP signaling through functions of Ras1 and Cac1 proteins in Cryptococcus neoformans. The Journal of biological chemistry 289, 12202\u201312216 (2014).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR44","doi-asserted-by":"publisher","first-page":"976","DOI":"10.1038\/nrc2231","volume":"8","author":"N Meyer","year":"2008","unstructured":"Meyer, N. & Penn, L. Z. Reflecting on 25 years with MYC. Nat Rev Cancer 8, 976\u2013990 (2008).","journal-title":"Nat Rev Cancer"},{"key":"BFsrep18491_CR45","doi-asserted-by":"crossref","first-page":"3300","DOI":"10.1016\/S0021-9258(18)61504-2","volume":"262","author":"ME Hemler","year":"1987","unstructured":"Hemler, M. E., Huang, C. & Schwarz, L. The VLA protein family. Characterization of five distinct cell surface heterodimers each with a common 130,000 molecular weight beta subunit. The Journal of biological chemistry 262, 3300\u20133309 (1987).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR46","doi-asserted-by":"publisher","first-page":"4308","DOI":"10.1242\/jcs.155879","volume":"127","author":"C Huet-Calderwood","year":"2014","unstructured":"Huet-Calderwood, C. et al. Differences in binding to the ILK complex determines kindlin isoform adhesion localization and integrin activation. Journal of cell science 127, 4308\u20134321 (2014).","journal-title":"Journal of cell science"},{"key":"BFsrep18491_CR47","doi-asserted-by":"publisher","first-page":"786","DOI":"10.1091\/mbc.E14-08-1294","volume":"26","author":"J Meller","year":"2014","unstructured":"Meller, J. et al. Emergence and subsequent functional specialization of Kindlins during evolution of cell adhesiveness. Molecular biology of the cell 26, 786\u2013796 (2014).","journal-title":"Molecular biology of the cell"},{"key":"BFsrep18491_CR48","doi-asserted-by":"publisher","first-page":"957","DOI":"10.1038\/nsmb822","volume":"11","author":"J Sengupta","year":"2004","unstructured":"Sengupta, J. et al. Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM. Nat Struct Mol Biol 11, 957\u2013962 (2004).","journal-title":"Nat Struct Mol Biol"},{"key":"BFsrep18491_CR49","doi-asserted-by":"publisher","first-page":"e56911","DOI":"10.1371\/journal.pone.0056911","volume":"8","author":"ZH Xue","year":"2013","unstructured":"Xue, Z. H., Feng, C., Liu, W. L. & Tan, S. M. A role of kindlin-3 in integrin \u03b1M\u00df2 outside-in signaling and the Syk-Vav1-Rac1\/Cdc42 signaling axis. PloS one 8, e56911 (2013).","journal-title":"PloS one"},{"key":"BFsrep18491_CR50","doi-asserted-by":"publisher","first-page":"3729","DOI":"10.1242\/jcs.00071","volume":"115","author":"DG Stupack","year":"2002","unstructured":"Stupack, D. G. & Cheresh, D. A. Get a ligand, get a life: integrins, signaling and cell survival. Journal of cell science 115, 3729\u20133738 (2002).","journal-title":"Journal of cell science"},{"key":"BFsrep18491_CR51","doi-asserted-by":"publisher","first-page":"3245","DOI":"10.1128\/MCB.18.6.3245","volume":"18","author":"BY Chang","year":"1998","unstructured":"Chang, B. Y., Conroy, K. B., Machleder, E. M. & Cartwright, C. A. RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells. Mol Cell Biol 18, 3245\u20133256 (1998).","journal-title":"Mol Cell Biol"},{"key":"BFsrep18491_CR52","doi-asserted-by":"publisher","first-page":"20346","DOI":"10.1074\/jbc.M101375200","volume":"276","author":"BY Chang","year":"2001","unstructured":"Chang, B. Y., Chiang, M. & Cartwright, C. A. The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. The Journal of biological chemistry 276, 20346\u201320356 (2001).","journal-title":"The Journal of biological chemistry"},{"key":"BFsrep18491_CR53","doi-asserted-by":"publisher","first-page":"500","DOI":"10.1016\/j.tim.2007.10.001","volume":"15","author":"PL Stewart","year":"2007","unstructured":"Stewart, P. L. & Nemerow, G. R. Cell integrins: commonly used receptors for diverse viral pathogens. Trends Microbiol 15, 500\u2013507 (2007).","journal-title":"Trends Microbiol"},{"key":"BFsrep18491_CR54","doi-asserted-by":"publisher","first-page":"3927","DOI":"10.1182\/blood-2003-05-1522","volume":"102","author":"KA Weigel-Kelley","year":"2003","unstructured":"Weigel-Kelley, K. A., Yoder, M. C. & Srivastava, A. \u03b15\u00df1 integrin as a cellular coreceptor for human parvovirus B19: requirement of functional activation of \u00df1 integrin for viral entry. Blood 102, 3927\u20133933 (2003).","journal-title":"Blood"},{"key":"BFsrep18491_CR55","doi-asserted-by":"publisher","first-page":"254","DOI":"10.1038\/nrc2824","volume":"10","author":"D Silvera","year":"2010","unstructured":"Silvera, D., Formenti, S. C. & Schneider, R. J. Translational control in cancer. Nat Rev Cancer 10, 254\u2013266 (2010).","journal-title":"Nat Rev Cancer"},{"key":"BFsrep18491_CR56","doi-asserted-by":"publisher","first-page":"313","DOI":"10.1038\/nm.1917","volume":"15","author":"NL Malinin","year":"2009","unstructured":"Malinin, N. L. et al. A point mutation in KINDLIN3 ablates activation of three integrin subfamilies in humans. Nat Med 15, 313\u2013318 (2009).","journal-title":"Nat Med"},{"key":"BFsrep18491_CR57","doi-asserted-by":"publisher","first-page":"4793","DOI":"10.4049\/jimmunol.180.7.4793","volume":"180","author":"XY Tang","year":"2008","unstructured":"Tang, X. Y., Li, Y. F. & Tan, S. M. Intercellular adhesion molecule-3 binding of integrin aLb2 requires both extension and opening of the integrin headpiece. J Immunol 180, 4793\u20134804 (2008).","journal-title":"J Immunol"},{"key":"BFsrep18491_CR58","doi-asserted-by":"publisher","first-page":"269","DOI":"10.1007\/978-1-59745-188-8_19","volume":"439","author":"B Shrestha","year":"2008","unstructured":"Shrestha, B., Smee, C. & Gileadi, O. Baculovirus expression vector system: an emerging host for high-throughput eukaryotic protein expression. Methods Mol Biol 439, 269\u2013289 (2008).","journal-title":"Methods Mol Biol"},{"key":"BFsrep18491_CR59","doi-asserted-by":"publisher","first-page":"2096","DOI":"10.1101\/gad.1450406","volume":"20","author":"AP Weng","year":"2006","unstructured":"Weng, A. P. et al. c-Myc is an important direct target of Notch1 in T-cell acute lymphoblastic leukemia\/lymphoma. Genes & development 20, 2096\u20132109 (2006).","journal-title":"Genes & development"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/srep18491","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/srep18491.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/srep18491.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,1,6]],"date-time":"2023-01-06T01:02:56Z","timestamp":1672966976000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/srep18491"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,12,18]]},"references-count":59,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2016,11,22]]}},"alternative-id":["BFsrep18491"],"URL":"https:\/\/doi.org\/10.1038\/srep18491","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2015,12,18]]},"assertion":[{"value":"20 August 2015","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"19 November 2015","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"18 December 2015","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing financial interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"18491"}}