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Here we report exocytosis as an important response mechanism to lysosomal damage, which is further potentiated when membrane repair or lysosomal degradation mechanisms are impaired. Our data reveal that Connexin43 (Cx43), a protein canonically associated with gap junctions, is recruited to damaged lysosomes to promote their secretion, thereby accelerating cell recovery. The exocytotic effects were found to be dependent on actin reorganization: Cx43 expression was associated with actin network remodelling, increased plasma membrane fluidity and decreased cell stiffness. Furthermore, we demonstrate that Cx43 interacts with the actin nucleator Arp2, the activity of which was shown to be necessary for Cx43-mediated actin rearrangement and lysosomal exocytosis following damage. These results identify a novel mechanism of lysosomal quality control whereby Cx43-mediated actin remodelling potentiates the secretion of damaged lysosomes.<\/p>","DOI":"10.21203\/rs.3.rs-2277227\/v1","type":"posted-content","created":{"date-parts":[[2022,12,21]],"date-time":"2022-12-21T21:03:51Z","timestamp":1671656631000},"source":"Crossref","is-referenced-by-count":1,"title":["Cx43 promotes exocytosis of damaged lysosomes through actin remodelling"],"prefix":"10.21203","author":[{"given":"Neuza","family":"Domingues","sequence":"first","affiliation":[{"name":"Univ Coimbra, Coimbra Institute for Clinical and Biomedical Research (iCBR), Faculty of Medicine, Coimbra, Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9644-6960","authenticated-orcid":false,"given":"Steve","family":"Catarino","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Coimbra Institute for Clinical and Biomedical Research (iCBR), Faculty of Medicine"}]},{"given":"Beatriz","family":"Cristovao","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Coimbra Institute for Clinical and Biomedical Research (iCBR), Faculty of Medicine"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9898-2409","authenticated-orcid":false,"given":"Lisa","family":"Rodrigues","sequence":"additional","affiliation":[{"name":"Faculty of Medicine, Coimbra, Portugal"}]},{"given":"Carvalho","family":"Filomena","sequence":"additional","affiliation":[{"name":"Instituto de Medicina Molecular"}]},{"given":"Maria Joao","family":"Sarmento","sequence":"additional","affiliation":[{"name":"Instituto de Medicina Molecular, Faculdade de Medicina, Universidade de Lisboa"}]},{"given":"Monica","family":"Zuzarte","sequence":"additional","affiliation":[{"name":"Coimbra Institute for Clinical and Biomedical Research (iCBR), Faculty of Medicine, University of Coimbra"}]},{"given":"Jani","family":"Almeida","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Faculty of Medicine"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9112-265X","authenticated-orcid":false,"given":"Fabio","family":"Fernandes","sequence":"additional","affiliation":[{"name":"Institute for Bioengineering and Biosciences (IBB), Instituto Superior T\u00e9cnico, Universidade de Lisboa"}]},{"given":"Paulo","family":"Rodrigues-Santos","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Faculty of Medicine"}]},{"given":"Nuno","family":"Santos","sequence":"additional","affiliation":[{"name":"University of Lisbon"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4071-592X","authenticated-orcid":false,"given":"Viktor","family":"Korolchuk","sequence":"additional","affiliation":[{"name":"Newcastle University"}]},{"given":"Teresa","family":"Gon\u00e7alves","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Center for Neurosciences and Cell Biology (CNC), Faculty of Medicine"}]},{"given":"Ira","family":"Milosevic","sequence":"additional","affiliation":[{"name":"Multidisciplinary Institute of Ageing, University of Coimbra"}]},{"given":"Nuno","family":"Raimundo","sequence":"additional","affiliation":[{"name":"Multidisciplinary Institute of Ageing, University of Coimbra"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5786-8447","authenticated-orcid":false,"given":"Henrique","family":"Girao","sequence":"additional","affiliation":[{"name":"Univ Coimbra, Coimbra Institute for Clinical and Biomedical Research (iCBR), Faculty of Medicine, Coimbra, Portugal"}]}],"member":"297","reference":[{"year":"2002","author":"Blott EJ","key":"ref1","unstructured":"Blott, E. J. & Griffiths, G. M. Secretory lysosomes. Nat. Rev. Mol. Cell Biol. 2002 32 3, 122\u2013131 (2002)."},{"key":"ref2","doi-asserted-by":"crossref","first-page":"1453","DOI":"10.1042\/BCJ20160780","article-title":"The lysosome: a crucial hub for AMPK and mTORC1 signalling","volume":"474","author":"Carroll B","year":"2017","unstructured":"Carroll, B. & Dunlop, E. A. The lysosome: a crucial hub for AMPK and mTORC1 signalling. Biochem. J. 474, 1453\u20131466 (2017).","journal-title":"Biochem. J."},{"key":"ref3","doi-asserted-by":"crossref","first-page":"847","DOI":"10.1038\/ncb0905-847","article-title":"The lysosome turns fifty","volume":"7","author":"Duve C","year":"2005","unstructured":"de Duve, C. The lysosome turns fifty. Nat. Cell Biol. 7, 847\u20139 (2005).","journal-title":"Nat. Cell Biol."},{"key":"ref4","doi-asserted-by":"crossref","first-page":"622","DOI":"10.1038\/nrm2217","article-title":"Lysosomes: fusion and function","volume":"8","author":"Luzio JP","year":"2007","unstructured":"Luzio, J. P., Pryor, P. R. & Bright, N. A. Lysosomes: fusion and function. Nat. Rev. Mol. Cell Biol. 8, 622\u2013632 (2007).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref5","doi-asserted-by":"crossref","first-page":"R315","DOI":"10.1016\/j.cub.2015.02.027","volume":"25","author":"Wartosch L","year":"2015","unstructured":"Wartosch, L., Bright, N. A. & Luzio, J. P. Lysosomes. Curr. Biol. 25, R315\u2013R316 (2015).","journal-title":"Curr. Biol."},{"key":"ref6","doi-asserted-by":"crossref","first-page":"e1006603","DOI":"10.1371\/journal.pgen.1006603","article-title":"Protecting cells by protecting their vulnerable lysosomes: Identification of a new mechanism for preserving lysosomal functional integrity upon oxidative stress","volume":"13","author":"Pascua-Maestro R","year":"2017","unstructured":"Pascua-Maestro, R., Diez-Hermano, S., Lillo, C., Ganfornina, M. D. & Sanchez, D. Protecting cells by protecting their vulnerable lysosomes: Identification of a new mechanism for preserving lysosomal functional integrity upon oxidative stress. PLOS Genet. 13, e1006603 (2017).","journal-title":"PLOS Genet."},{"key":"ref7","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1089\/ars.2008.2263","article-title":"Oxidative Stress and Autophagy in the Regulation of Lysosome-Dependent Neuron Death","volume":"11","author":"Pivtoraiko VN","year":"2009","unstructured":"Pivtoraiko, V. N., Stone, S. L., Roth, K. A. & Shacka, J. J. Oxidative Stress and Autophagy in the Regulation of Lysosome-Dependent Neuron Death. Antioxid. Redox Signal. 11, 481 (2009).","journal-title":"Antioxid. Redox Signal."},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1002\/jnr.22640","article-title":"Intraneuronal amyloid \u03b2 oligomers cause cell death via endoplasmic reticulum stress, endosomal\/lysosomal leakage, and mitochondrial dysfunction in vivo","volume":"89","author":"Umeda T","year":"2011","unstructured":"Umeda, T. et al. Intraneuronal amyloid \u03b2 oligomers cause cell death via endoplasmic reticulum stress, endosomal\/lysosomal leakage, and mitochondrial dysfunction in vivo. J. Neurosci. Res. 89, 1031\u20131042 (2011).","journal-title":"J. Neurosci. Res."},{"year":"2022","author":"Niekamp P","key":"ref9","unstructured":"Niekamp, P. et al. Ca2+-activated sphingomyelin scrambling and turnover mediate ESCRT-independent lysosomal repair. Nat. Commun. 2022 131 13, 1\u201316 (2022)."},{"key":"ref10","doi-asserted-by":"crossref","first-page":"2","DOI":"10.15252\/embj.2020106162","article-title":"LRRK 2 to the rescue of damaged endomembranes","volume":"39","author":"Radulovic M","year":"2020","unstructured":"Radulovic, M. & Stenmark, H. LRRK 2 to the rescue of damaged endomembranes. EMBO J. 39, 2\u20134 (2020).","journal-title":"EMBO J."},{"key":"ref11","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1128\/mBio.01226-18","article-title":"Candida albicans Hyphal Expansion Causes Phagosomal Membrane Damage and Luminal Alkalinization","volume":"9","author":"Westman J","year":"2018","unstructured":"Westman, J., Moran, G., Mogavero, S., Hube, B. & Grinstein, S. Candida albicans Hyphal Expansion Causes Phagosomal Membrane Damage and Luminal Alkalinization. MBio 9, 1\u201314 (2018).","journal-title":"MBio"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"2336","DOI":"10.1038\/emboj.2013.171","article-title":"Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury","volume":"32","author":"Maejima I","year":"2013","unstructured":"Maejima, I. et al. Autophagy sequesters damaged lysosomes to control lysosomal biogenesis and kidney injury. EMBO J. 32, 2336 (2013).","journal-title":"EMBO J."},{"key":"ref13","doi-asserted-by":"crossref","first-page":"6434","DOI":"10.1038\/onc.2008.310","article-title":"Lysosomal membrane permeabilization in cell death","volume":"27","author":"Boya P","year":"2008","unstructured":"Boya, P. & Kroemer, G. Lysosomal membrane permeabilization in cell death. Oncogene 27, 6434\u20136451 (2008).","journal-title":"Oncogene"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1158\/0008-5472.CAN-03-3060","article-title":"Cathepsin B Mediates Caspase-Independent Cell Death Induced by Microtubule Stabilizing Agents in Non-Small Cell Lung Cancer Cells","volume":"64","author":"Br\u00f6ker LE","year":"2004","unstructured":"Br\u00f6ker, L. E. et al. Cathepsin B Mediates Caspase-Independent Cell Death Induced by Microtubule Stabilizing Agents in Non-Small Cell Lung Cancer Cells. Cancer Res. 64, 27\u201330 (2004).","journal-title":"Cancer Res."},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15252\/embj.201899753","article-title":"ESCRT -mediated lysosome repair precedes lysophagy and promotes cell survival","volume":"37","author":"Radulovic M","year":"2018","unstructured":"Radulovic, M. et al. ESCRT -mediated lysosome repair precedes lysophagy and promotes cell survival. 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Elife 10, (2021)."},{"key":"ref31","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1023\/A:1021152709313","article-title":"The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth","volume":"242","author":"Dang X","year":"2003","unstructured":"Dang, X., Doble, B. W. & Kardami, E. The carboxy-tail of connexin-43 localizes to the nucleus and inhibits cell growth. Mol. Cell. Biochem. 242, 35\u201338 (2003).","journal-title":"Mol. Cell. Biochem."},{"key":"ref32","doi-asserted-by":"crossref","DOI":"10.3390\/biom10030473","article-title":"An alternatively translated connexin 43 isoform, gja1-11k, localizes to the nucleus and can inhibit cell cycle progression","volume":"10","author":"Epifantseva I","year":"2020","unstructured":"Epifantseva, I. et al. An alternatively translated connexin 43 isoform, gja1-11k, localizes to the nucleus and can inhibit cell cycle progression. Biomolecules 10, (2020).","journal-title":"Biomolecules"},{"key":"ref33","doi-asserted-by":"crossref","unstructured":"Agullo-Pascual, E. et al. Editor\u2019s choice: Super-resolution imaging reveals that loss of the C-terminus of connexin43 limits microtubule plus-end capture and NaV1.5 localization at the intercalated disc. Cardiovasc. Res. 104, 371 (2014).","DOI":"10.1093\/cvr\/cvu195"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1161\/CIRCRESAHA.117.311955","article-title":"GJA1-20k Arranges Actin to Guide Cx43 Delivery to Cardiac Intercalated Discs","volume":"121","author":"Basheer WA","year":"2017","unstructured":"Basheer, W. A. et al. GJA1-20k Arranges Actin to Guide Cx43 Delivery to Cardiac Intercalated Discs. Circ. Res. 121, 1069\u20131080 (2017).","journal-title":"Circ. Res."},{"key":"ref35","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.devcel.2019.10.025","article-title":"Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal","volume":"52","author":"Jia J","year":"2020","unstructured":"Jia, J. et al. Galectin-3 Coordinates a Cellular System for Lysosomal Repair and Removal. Dev. Cell 52, 69\u201387.e8 (2020).","journal-title":"Dev. Cell"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1083\/jcb.200208154","article-title":"Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells","volume":"159","author":"Jaiswal JK","year":"2002","unstructured":"Jaiswal, J. K., Andrews, N. W. & Simon, S. M. Membrane proximal lysosomes are the major vesicles responsible for calcium-dependent exocytosis in nonsecretory cells. J. Cell Biol. 159, 625\u2013635 (2002).","journal-title":"J. Cell Biol."},{"key":"ref37","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1083\/jcb.137.1.93","article-title":"Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells","volume":"137","author":"Rodr\u00edguez A","year":"1997","unstructured":"Rodr\u00edguez, A., Webster, P., Ortego, J. & Andrews, N. W. Lysosomes behave as Ca2+-regulated exocytic vesicles in fibroblasts and epithelial cells. J. Cell Biol. 137, 93\u2013104 (1997).","journal-title":"J. Cell Biol."},{"key":"ref38","doi-asserted-by":"crossref","first-page":"10850","DOI":"10.1074\/jbc.M109.080796","article-title":"Dual Role of 3-Methyladenine in Modulation of Autophagy via Different Temporal Patterns of Inhibition on Class I and III Phosphoinositide 3-Kinase","volume":"285","author":"Wu YT","year":"2010","unstructured":"Wu, Y. T. et al. Dual Role of 3-Methyladenine in Modulation of Autophagy via Different Temporal Patterns of Inhibition on Class I and III Phosphoinositide 3-Kinase. J. Biol. Chem. 285, 10850 (2010).","journal-title":"J. Biol. Chem."},{"key":"ref39","doi-asserted-by":"crossref","first-page":"C600","DOI":"10.1152\/ajpcell.00155.2015","article-title":"The connexin 43\/ZO-1 complex regulates cerebral endothelial F-actin architecture and migration","volume":"309","author":"Chen CH","year":"2015","unstructured":"Chen, C. H. et al. The connexin 43\/ZO-1 complex regulates cerebral endothelial F-actin architecture and migration. Am. J. Physiol. - Cell Physiol. 309, C600\u2013C607 (2015).","journal-title":"Am. J. Physiol. - Cell Physiol."},{"key":"ref40","doi-asserted-by":"crossref","first-page":"978","DOI":"10.1161\/CIRCRESAHA.111.257964","article-title":"Actin cytoskeleton rest stops regulate anterograde traffic of connexin 43 vesicles to the plasma membrane","volume":"110","author":"Smyth JW","year":"2012","unstructured":"Smyth, J. W. et al. Actin cytoskeleton rest stops regulate anterograde traffic of connexin 43 vesicles to the plasma membrane. Circ. Res. 110, 978\u2013989 (2012).","journal-title":"Circ. Res."},{"key":"ref41","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1016\/j.yexcr.2008.12.025","article-title":"The TSG101 protein binds to connexins and is involved in connexin degradation","volume":"315","author":"Auth T","year":"2009","unstructured":"Auth, T. et al. The TSG101 protein binds to connexins and is involved in connexin degradation. Exp. Cell Res. 315, 1053\u20131062 (2009).","journal-title":"Exp. Cell Res."},{"key":"ref42","doi-asserted-by":"crossref","first-page":"3883","DOI":"10.1242\/jcs.053801","article-title":"Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101","volume":"122","author":"Leithe E","year":"2009","unstructured":"Leithe, E. et al. Ubiquitylation of the gap junction protein connexin-43 signals its trafficking from early endosomes to lysosomes in a process mediated by Hrs and Tsg101. J. Cell Sci. 122, 3883\u20133893 (2009).","journal-title":"J. Cell Sci."},{"key":"ref43","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1042\/BJ20102059","article-title":"Ubiquitin-mediated internalization of connexin43 is independent of the canonical endocytic tyrosine-sorting signal","volume":"437","author":"Catarino S","year":"2011","unstructured":"Catarino, S., Ramalho, J. S., Marques, C., Pereira, P. & Gir\u00e3o, H. Ubiquitin-mediated internalization of connexin43 is independent of the canonical endocytic tyrosine-sorting signal. Biochem. J. 437, 255\u2013267 (2011).","journal-title":"Biochem. J."},{"key":"ref44","doi-asserted-by":"crossref","first-page":"4629","DOI":"10.1096\/fj.13-248963","article-title":"AMSH-mediated deubiquitination of Cx43 regulates internalization and degradation of gap junctions","volume":"28","author":"Ribeiro-Rodrigues TM","year":"2014","unstructured":"Ribeiro-Rodrigues, T. M. et al. AMSH-mediated deubiquitination of Cx43 regulates internalization and degradation of gap junctions. FASEB J. 28, 4629\u20134641 (2014).","journal-title":"FASEB J."},{"key":"ref45","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/j.tim.2022.03.004","article-title":"Phagolysosomal remodeling to confine Candida albicans in the macrophage","volume":"30","author":"Domingues N","year":"2022","unstructured":"Domingues, N., Gon\u00e7alves, T. & Girao, H. Phagolysosomal remodeling to confine Candida albicans in the macrophage. Trends Microbiol. 30, 519\u2013523 (2022).","journal-title":"Trends Microbiol."},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.15252\/embj.2020104494","article-title":"LRRK 2 activation controls the repair of damaged endomembranes in macrophages","volume":"39","author":"Herbst S","year":"2020","unstructured":"Herbst, S. et al. LRRK 2 activation controls the repair of damaged endomembranes in macrophages. EMBO J. 39, 1\u201314 (2020).","journal-title":"EMBO J."},{"year":"2018","author":"Miranda AM","key":"ref47","unstructured":"Miranda, A. M. et al. Neuronal lysosomal dysfunction releases exosomes harboring APP C-terminal fragments and unique lipid signatures. Nat. Commun. 2018 91 9, 1\u201316 (2018)."},{"key":"ref48","doi-asserted-by":"crossref","first-page":"794","DOI":"10.4161\/auto.19390","article-title":"Internalized gap junctions are degraded by autophagy","volume":"8","author":"Fong JT","year":"2012","unstructured":"Fong, J. T. et al. Internalized gap junctions are degraded by autophagy. Autophagy 8, 794\u2013811 (2012).","journal-title":"Autophagy"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1016\/S0008-6363(98)00060-1","article-title":"Proteolysis of connexin43-containing gap junctions in normal and heat-stressed cardiac myocytes","volume":"38","author":"Laing JG","year":"1998","unstructured":"Laing, J. G., Tadros, P. N., Green, K., Saffitz, J. E. & Beyer, E. C. Proteolysis of connexin43-containing gap junctions in normal and heat-stressed cardiac myocytes. Cardiovasc. Res. 38, 711\u2013718 (1998).","journal-title":"Cardiovasc. Res."},{"key":"ref50","doi-asserted-by":"crossref","first-page":"2834","DOI":"10.1091\/mbc.e13-02-0111","article-title":"Two tyrosine-based sorting signals in the Cx43 C-terminus cooperate to mediate gap junction endocytosis","volume":"24","author":"Fong JT","year":"2013","unstructured":"Fong, J. T., Kells, R. M. & Falk, M. M. Two tyrosine-based sorting signals in the Cx43 C-terminus cooperate to mediate gap junction endocytosis. Mol. Biol. Cell 24, 2834\u20132848 (2013).","journal-title":"Mol. Biol. Cell"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1016\/S0092-8674(01)00421-4","article-title":"Plasma membrane repair is mediated by Ca2+-regulated exocytosis of lysosomes","volume":"106","author":"Reddy A","year":"2001","unstructured":"Reddy, A., Caler, E. V. & Andrews, N. W. Plasma membrane repair is mediated by Ca2+-regulated exocytosis of lysosomes. Cell 106, 157\u2013169 (2001).","journal-title":"Cell"},{"key":"ref52","doi-asserted-by":"publisher","DOI":"10.1080\/15419060801891034","article-title":"Cell Communication & Adhesion Mimetic Peptides as Blockers of Connexin Channel-Facilitated Intercellular Communication","author":"Evans WH","year":"2009","unstructured":"Evans, W. H. & Leybaert, L. Cell Communication & Adhesion Mimetic Peptides as Blockers of Connexin Channel-Facilitated Intercellular Communication. (2009). doi:10.1080\/15419060801891034"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"3767","DOI":"10.1016\/j.celrep.2019.11.060","article-title":"Calcium-Independent Exo-endocytosis Coupling at Small Central Synapses","volume":"29","author":"Orlando M","year":"2019","unstructured":"Orlando, M., Schmitz, D., Rosenmund, C. & Herman, M. A. Calcium-Independent Exo-endocytosis Coupling at Small Central Synapses. Cell Rep. 29, 3767\u20133774.e3 (2019).","journal-title":"Cell Rep."},{"key":"ref54","first-page":"1","article-title":"Self-organizing actin patterns shape membrane architecture but not cell mechanics","volume":"2017 81 8","author":"Fritzsche M","year":"2017","unstructured":"Fritzsche, M. et al. Self-organizing actin patterns shape membrane architecture but not cell mechanics. Nat. Commun. 2017 81 8, 1\u201314 (2017).","journal-title":"Nat. Commun."},{"year":"2019","author":"Colin-York H","key":"ref55","unstructured":"Colin-York, H. et al. Cytoskeletal actin patterns shape mast cell activation. Commun. Biol. 2019 21 2, 1\u201312 (2019)."},{"key":"ref56","doi-asserted-by":"crossref","first-page":"3165","DOI":"10.1016\/j.cub.2019.07.088","article-title":"Capping Protein Insulates Arp2\/3-Assembled Actin Patches from Formins","volume":"29","author":"Billault-Chaumartin I","year":"2019","unstructured":"Billault-Chaumartin, I. & Martin, S. G. Capping Protein Insulates Arp2\/3-Assembled Actin Patches from Formins. Curr. Biol. 29, 3165\u20133176.e6 (2019).","journal-title":"Curr. Biol."},{"key":"ref57","doi-asserted-by":"crossref","first-page":"489","DOI":"10.1016\/j.cub.2017.12.044","article-title":"Nanoscale Dynamism of Actin Enables Secretory Function in Cytolytic Cells","volume":"28","author":"Carisey AF","year":"2018","unstructured":"Carisey, A. F., Mace, E. M., Saeed, M. B., Davis, D. M. & Orange, J. S. Nanoscale Dynamism of Actin Enables Secretory Function in Cytolytic Cells. Curr. Biol. 28, 489\u2013502.e9 (2018).","journal-title":"Curr. Biol."},{"key":"ref58","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1111\/imcb.12304","article-title":"Partial loss of actin nucleator actin-related protein 2\/3 activity triggers blebbing in primary T lymphocytes","volume":"98","author":"Obeidy P","year":"2020","unstructured":"Obeidy, P. et al. Partial loss of actin nucleator actin-related protein 2\/3 activity triggers blebbing in primary T lymphocytes. Immunol. Cell Biol. 98, 93 (2020).","journal-title":"Immunol. Cell Biol."},{"key":"ref59","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1207968109\/-\/DCSupplemental","article-title":"Cell mechanics control rapid transitions between blebs and lamellipodia during migration","author":"Bergert M","unstructured":"Bergert, M., Chandradoss, S. D., Desai, R. A. & Paluch, E. Cell mechanics control rapid transitions between blebs and lamellipodia during migration. doi:10.1073\/pnas.1207968109\/-\/DCSupplemental"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0143-4160(88)90004-8","article-title":"Calcium dependence of bleb formation and cell death in hepatocytes","volume":"9","author":"Nieminen AL","year":"1988","unstructured":"Nieminen, A. L. et al. Calcium dependence of bleb formation and cell death in hepatocytes. Cell Calcium 9, 237\u2013246 (1988).","journal-title":"Cell Calcium"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/j.devcel.2011.07.016","article-title":"Transcriptional activation of lysosomal exocytosis promotes cellular clearance","volume":"21","author":"Medina DL","year":"2011","unstructured":"Medina, D. L. et al. Transcriptional activation of lysosomal exocytosis promotes cellular clearance. Dev. Cell 21, 421\u2013430 (2011).","journal-title":"Dev. Cell"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"15793","DOI":"10.1038\/ncomms15793","article-title":"mTORC1-independent TFEB activation via Akt inhibition promotes cellular clearance in neurodegenerative storage diseases","volume":"8","author":"Palmieri M","year":"2017","unstructured":"Palmieri, M. et al. Corrigendum: mTORC1-independent TFEB activation via Akt inhibition promotes cellular clearance in neurodegenerative storage diseases. Nat. Commun. 8, 15793 (2017).","journal-title":"Nat. Commun."},{"key":"ref63","doi-asserted-by":"crossref","first-page":"995","DOI":"10.1194\/jlr.R046896","article-title":"Lysosomal exocytosis and lipid storage disorders","volume":"55","author":"Samie MA","year":"2014","unstructured":"Samie, M. A. & Xu, H. Lysosomal exocytosis and lipid storage disorders. J. Lipid Res. 55, 995\u20131009 (2014).","journal-title":"J. Lipid Res."},{"key":"ref64","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1002\/emmm.201202176","article-title":"Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease","volume":"5","author":"Spampanato C","year":"2013","unstructured":"Spampanato, C. et al. Transcription factor EB (TFEB) is a new therapeutic target for Pompe disease. EMBO Mol. Med. 5, 691\u2013706 (2013).","journal-title":"EMBO Mol. Med."},{"key":"ref65","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1126\/science.1174447","article-title":"A gene network regulating lysosomal biogenesis and function","volume":"325","author":"Sardiello M","year":"2009","unstructured":"Sardiello, M. et al. A gene network regulating lysosomal biogenesis and function. Science (80-.). 325, 473\u2013477 (2009).","journal-title":"Science (80-.)."},{"year":"2013","author":"Decressac M","key":"ref66","unstructured":"Decressac, M. et al. TFEB-mediated autophagy rescues midbrain dopamine neurons from \u03b1-synuclein toxicity. Proc. Natl. Acad. Sci. U. S. A. 110, E1817 (2013)."},{"key":"ref67","doi-asserted-by":"crossref","first-page":"5925","DOI":"10.1038\/s41380-020-0738-0","article-title":"TFEB regulates lysosomal exocytosis of tau and its loss of function exacerbates tau pathology and spreading","volume":"26","author":"Xu Y","year":"2021","unstructured":"Xu, Y. et al. TFEB regulates lysosomal exocytosis of tau and its loss of function exacerbates tau pathology and spreading. Mol. Psychiatry 26, 5925 (2021).","journal-title":"Mol. Psychiatry"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1016\/j.molcel.2019.12.028","article-title":"AMPK, a Regulator of Metabolism and Autophagy, Is Activated by Lysosomal Damage via a Novel Galectin-Directed Ubiquitin Signal Transduction System","volume":"77","author":"Jia J","year":"2020","unstructured":"Jia, J. et al. AMPK, a Regulator of Metabolism and Autophagy, Is Activated by Lysosomal Damage via a Novel Galectin-Directed Ubiquitin Signal Transduction System. Mol. Cell 77, 951\u2013969 (2020).","journal-title":"Mol. Cell"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"122","DOI":"10.1038\/nrm732","article-title":"Secretory lysosomes","volume":"3","author":"Blott EJ","year":"2002","unstructured":"Blott, E. J. & Griffiths, G. M. Secretory lysosomes. Nat Rev Mol Cell Biol 3, 122\u2013131 (2002).","journal-title":"Nat Rev Mol Cell Biol"},{"year":"2021","author":"Domingues N","key":"ref70","unstructured":"Domingues, N. et al. Cholesteryl Hemiazelate Induces Lysosome Dysfunction and Exocytosis in Macrophages. bioRxiv 2021.01.05.422575 (2021)."},{"key":"ref71","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1083\/jcb.200711082","article-title":"Flightless-I regulates proinflammatory caspases by selectively modulating intracellular localization and caspase activity","volume":"181","author":"Li J","year":"2008","unstructured":"Li, J., Yin, H. L. & Yuan, J. Flightless-I regulates proinflammatory caspases by selectively modulating intracellular localization and caspase activity. J. Cell Biol. 181, 321\u2013333 (2008).","journal-title":"J. Cell Biol."},{"key":"ref72","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1111\/boc.201100070","article-title":"TI-VAMP\/VAMP7 is the SNARE of secretory lysosomes contributing to ATP secretion from astrocytes","volume":"104","author":"Verderio C","year":"2012","unstructured":"Verderio, C. et al. TI-VAMP\/VAMP7 is the SNARE of secretory lysosomes contributing to ATP secretion from astrocytes. Biol. Cell 104, 213\u2013228 (2012).","journal-title":"Biol. Cell"},{"key":"ref73","doi-asserted-by":"publisher","DOI":"10.3402\/jev.v5.32538","article-title":"Presence of Cx43 in extracellular vesicles reduces the cardiotoxicity of the anti-tumour therapeutic approach with doxorubicin","author":"Martins-Marques T","year":"2016","unstructured":"Martins-Marques, T. et al. Presence of Cx43 in extracellular vesicles reduces the cardiotoxicity of the anti-tumour therapeutic approach with doxorubicin. J. Extracell. Vesicles (2016). doi:10.3402\/jev.v5.32538","journal-title":"J. Extracell. Vesicles"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1016\/j.mcn.2017.05.006","article-title":"Membrane shaping by actin and myosin during regulated exocytosis","volume":"84","author":"Papadopulos A","year":"2017","unstructured":"Papadopulos, A. Membrane shaping by actin and myosin during regulated exocytosis. Mol. Cell. Neurosci. 84, 93\u201399 (2017).","journal-title":"Mol. Cell. Neurosci."},{"key":"ref75","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.hrthm.2011.11.025","article-title":"Reduced Heterogeneous Expression Of Cx43 Results In Decreased Nav1.5 Expression And Reduced Sodium Current Which Accounts For Arrhythmia Vulnerability In Conditional Cx43 Knockout Mice","volume":"9","author":"Jansen JA","year":"2012","unstructured":"Jansen, J. A. et al. Reduced Heterogeneous Expression Of Cx43 Results In Decreased Nav1.5 Expression And Reduced Sodium Current Which Accounts For Arrhythmia Vulnerability In Conditional Cx43 Knockout Mice. Hear. Rhythm 9, 600 (2012).","journal-title":"Hear. Rhythm"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"348","DOI":"10.1007\/s00395-013-0348-y","article-title":"Deletion of the last five C-terminal amino acid residues of connexin43 leads to lethal ventricular arrhythmias in mice without affecting coupling via gap junction channels","volume":"108","author":"L\u00fcbkemeier I","year":"2013","unstructured":"L\u00fcbkemeier, I. et al. Deletion of the last five C-terminal amino acid residues of connexin43 leads to lethal ventricular arrhythmias in mice without affecting coupling via gap junction channels. Basic Res. Cardiol. 108, 348 (2013).","journal-title":"Basic Res. Cardiol."},{"key":"ref77","doi-asserted-by":"crossref","first-page":"12725","DOI":"10.1074\/jbc.273.21.12725","article-title":"Direct Association of the Gap Junction Protein Connexin-43 with ZO-1 in Cardiac Myocytes *","volume":"273","author":"Toyofuku T","year":"1998","unstructured":"Toyofuku, T. et al. Direct Association of the Gap Junction Protein Connexin-43 with ZO-1 in Cardiac Myocytes *. J. Biol. Chem. 273, 12725\u201312731 (1998).","journal-title":"J. Biol. Chem."},{"key":"ref78","doi-asserted-by":"publisher","DOI":"10.1101\/2022.01.05.475034","article-title":"GJA1-20k, an internally translated isoform of Connexin 43, is an actin capping protein","author":"Baum R","unstructured":"Baum, R. et al. GJA1-20k, an internally translated isoform of Connexin 43, is an actin capping protein. doi:10.1101\/2022.01.05.475034"},{"year":"2015","author":"Papadopulos A","key":"ref79","unstructured":"Papadopulos, A. et al. Activity-driven relaxation of the cortical actomyosin II network synchronizes Munc18-1-dependent neurosecretory vesicle docking. Nat. Commun. 2015 61 6, 1\u201311 (2015)."},{"year":"2011","author":"Wen PJ","key":"ref80","unstructured":"Wen, P. J. et al. Phosphatidylinositol(4,5)bisphosphate coordinates actin-mediated mobilization and translocation of secretory vesicles to the plasma membrane of chromaffin cells. Nat. Commun. 2011 21 2, 1\u201311 (2011)."},{"key":"ref81","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1083\/jcb.200610144","article-title":"Regulation of connexin43 gap junctional communication by phosphatidylinositol 4,5-bisphosphate","volume":"177","author":"Zeijl L","year":"2007","unstructured":"Van Zeijl, L. et al. Regulation of connexin43 gap junctional communication by phosphatidylinositol 4,5-bisphosphate. J. Cell Biol. 177, 881\u2013891 (2007).","journal-title":"J. Cell Biol."},{"key":"ref82","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1016\/j.cub.2013.05.063","article-title":"Membrane Tension in Rapidly Moving Cells Is Determined by Cytoskeletal Forces","volume":"23","author":"Lieber AD","year":"2013","unstructured":"Lieber, A. D., Yehudai-Resheff, S., Barnhart, E. L., Theriot, J. A. & Keren, K. Membrane Tension in Rapidly Moving Cells Is Determined by Cytoskeletal Forces. Curr. Biol. 23, 1409\u20131417 (2013).","journal-title":"Curr. Biol."},{"key":"ref83","first-page":"2139","article-title":"Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. Rapid Publication Adhesion-activating Phorbol Ester Increases the Mobility of Leukocyte Integrin LFA-1 in Cultured Lymphocytes cytoskeleton \u2022 cell mem-brane \u2022 diffusion \u2022 microscopy \u2022 microspheres","volume":"97","author":"Kucik DF","year":"1996","unstructured":"Kucik, D. F. et al. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. Rapid Publication Adhesion-activating Phorbol Ester Increases the Mobility of Leukocyte Integrin LFA-1 in Cultured Lymphocytes cytoskeleton \u2022 cell mem-brane \u2022 diffusion \u2022 microscopy \u2022 microspheres. J. Clin. Invest 97, 2139\u20132144 (1996).","journal-title":"J. Clin. Invest"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1016\/S0006-3495(00)76614-8","article-title":"Drug-Induced Changes of Cytoskeletal Structure and Mechanics in Fibroblasts: An Atomic Force Microscopy Study","volume":"78","author":"Rotsch C","year":"2000","unstructured":"Rotsch, C. & Radmacher, M. Drug-Induced Changes of Cytoskeletal Structure and Mechanics in Fibroblasts: An Atomic Force Microscopy Study. Biophys. J. 78, 520\u2013535 (2000).","journal-title":"Biophys. J."},{"key":"ref85","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1038\/ncb2614","article-title":"Coordinated oscillations in cortical actin and Ca2 + correlate with cycles of vesicle secretion","volume":"14","author":"Wollman R","year":"2012","unstructured":"Wollman, R. & Meyer, T. Coordinated oscillations in cortical actin and Ca2 + correlate with cycles of vesicle secretion. Nat. Cell Biol. 14, 1261 (2012).","journal-title":"Nat. Cell Biol."},{"key":"ref86","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/ncomms1037","article-title":"PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2 + release channels in the endolysosome","volume":"1","author":"Dong X","year":"2010","unstructured":"Dong, X. et al. PI(3,5)P2 controls membrane trafficking by direct activation of mucolipin Ca2 + release channels in the endolysosome. Nat. Commun. 1, 1\u201311 (2010).","journal-title":"Nat. Commun."},{"year":"2015","author":"Tran DT","key":"ref87","unstructured":"Tran, D. T., Masedunskas, A., Weigert, R. & Ten Hagen, K. G. Arp2\/3-mediated F-actin formation controls regulated exocytosis in vivo. Nat. Commun. 2015 61 6, 1\u201310 (2015)."},{"key":"ref88","doi-asserted-by":"crossref","first-page":"486","DOI":"10.1111\/j.1600-0854.2007.00548.x","article-title":"The ternary Rab27a-Myrip-Myosin VIIa complex regulates melanosome motility in the retinal pigment epithelium","volume":"8","author":"Lopes VS","year":"2007","unstructured":"Lopes, V. S. et al. The ternary Rab27a-Myrip-Myosin VIIa complex regulates melanosome motility in the retinal pigment epithelium. Traffic 8, 486\u2013499 (2007).","journal-title":"Traffic"},{"key":"ref89","doi-asserted-by":"crossref","first-page":"135","DOI":"10.15252\/embj.201695148","article-title":"VCP\/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy","volume":"36","author":"Papadopoulos C","year":"2017","unstructured":"Papadopoulos, C. et al. VCP\/p97 cooperates with YOD1, UBXD1 and PLAA to drive clearance of ruptured lysosomes by autophagy. EMBO J. 36, 135\u2013150 (2017).","journal-title":"EMBO J."},{"key":"ref90","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1016\/j.celrep.2013.10.009","article-title":"Autoregulation of connexin43 gap junction formation by internally translated isoforms","volume":"5","author":"Smyth JW","year":"2013","unstructured":"Smyth, J. W. & Shaw, R. M. Autoregulation of connexin43 gap junction formation by internally translated isoforms. Cell Rep. 5, 611\u2013618 (2013).","journal-title":"Cell Rep."},{"key":"ref91","first-page":"53","article-title":"mScarlet: a bright monomeric red fluorescent protein for cellular imaging","volume":"141 14","author":"Bindels DS","year":"2016","unstructured":"Bindels, D. S. et al. mScarlet: a bright monomeric red fluorescent protein for cellular imaging. Nat. Methods 2016 141 14, 53\u201356 (2016).","journal-title":"Nat. Methods 2016"},{"key":"ref92","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1038\/nprot.2011.419","article-title":"Quantitative imaging of membrane lipid order in cells and organisms","volume":"7","author":"Owen DM","year":"2012","unstructured":"Owen, D. M., Rentero, C., Magenau, A., Abu-Siniyeh, A. & Gaus, K. Quantitative imaging of membrane lipid order in cells and organisms. Nat. Protoc. 7, 24\u201335 (2012).","journal-title":"Nat. Protoc."},{"key":"ref93","doi-asserted-by":"crossref","first-page":"4609","DOI":"10.1021\/nn1009648","article-title":"Atomic force microscopy-based molecular recognition of a fibrinogen receptor on human erythrocytes","volume":"4","author":"Carvalho FA","year":"2010","unstructured":"Carvalho, F. A. et al. Atomic force microscopy-based molecular recognition of a fibrinogen receptor on human erythrocytes. ACS Nano 4, 4609\u20134620 (2010).","journal-title":"ACS Nano"},{"key":"ref94","doi-asserted-by":"crossref","first-page":"19390","DOI":"10.1039\/C6NR04465D","article-title":"Atomic force microscopy and graph analysis to study the P-cadherin\/SFK mechanotransduction signalling in breast cancer cells","volume":"8","author":"Ribeiro AS","year":"2016","unstructured":"Ribeiro, A. S. et al. Atomic force microscopy and graph analysis to study the P-cadherin\/SFK mechanotransduction signalling in breast cancer cells. Nanoscale 8, 19390\u201319401 (2016).","journal-title":"Nanoscale"},{"key":"ref95","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1128\/MMBR.62.1.130-180.1998","article-title":"Cell Wall and Secreted Proteins of Candida albicans: Identification, Function, and Expression","volume":"62","author":"Chaffin WL","year":"1998","unstructured":"Chaffin, W. L., L\u00f3pez-Ribot, J. L., Casanova, M., Gozalbo, D. & Mart\u00ednez, J. P. Cell Wall and Secreted Proteins of Candida albicans: Identification, Function, and Expression. Microbiol. Mol. Biol. Rev. 62, 130\u2013180 (1998).","journal-title":"Microbiol. Mol. Biol. Rev."},{"key":"ref96","doi-asserted-by":"crossref","first-page":"2757","DOI":"10.1039\/C8NR04398A","article-title":"Fibrinogen-erythrocyte binding and hemorheology measurements in the assessment of essential arterial hypertension patients","volume":"11","author":"Guedes AF","year":"2019","unstructured":"Guedes, A. F., Moreira, C., Nogueira, J. B., Santos, N. C. & Carvalho, F. A. Fibrinogen-erythrocyte binding and hemorheology measurements in the assessment of essential arterial hypertension patients. Nanoscale 11, 2757\u20132766 (2019).","journal-title":"Nanoscale"},{"year":"2016","author":"Guedes AF","key":"ref97","unstructured":"Guedes, A. F. et al. Atomic force microscopy as a tool to evaluate the risk of cardiovascular diseases in patients. Nat. Nanotechnol. 2016 118 11, 687\u2013692 (2016)."},{"key":"ref98","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1080\/15384101.2016.1172147","article-title":"Modulation of membrane properties of lung cancer cells by azurin enhances the sensitivity to EGFR-targeted therapy and decreased \u03b21 integrin-mediated adhesion","volume":"15","author":"Bernardes N","year":"2016","unstructured":"Bernardes, N. et al. Modulation of membrane properties of lung cancer cells by azurin enhances the sensitivity to EGFR-targeted therapy and decreased \u03b21 integrin-mediated adhesion. Cell Cycle 15, 1415\u20131424 (2016).","journal-title":"Cell Cycle"},{"key":"ref99","doi-asserted-by":"crossref","first-page":"15","DOI":"10.5685\/plmorphol.29.15","article-title":"Quantitative evaluation of cytoskeletal organizations by microscopic image analysis","volume":"29","author":"Higaki Takumi","year":"2017","unstructured":"Higaki Takumi. Quantitative evaluation of cytoskeletal organizations by microscopic image analysis. Plant Morphol. 29, 15\u201321 (2017).","journal-title":"Plant Morphol."},{"key":"ref100","doi-asserted-by":"crossref","DOI":"10.3389\/fpls.2020.575573","article-title":"Proteins SINE1 and SINE2 Are Involved in Microtubule Reorganization During ABA-Induced Stomatal Closure","volume":"11","author":"Biel A","year":"2020","unstructured":"Biel, A., Moser, M. & Meier, I. Arabidopsis KASH Proteins SINE1 and SINE2 Are Involved in Microtubule Reorganization During ABA-Induced Stomatal Closure. Front. Plant Sci. 11, (2020).","journal-title":"Front. Plant Sci."}],"container-title":[],"original-title":[],"link":[{"URL":"https:\/\/www.researchsquare.com\/article\/rs-2277227\/v1","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.researchsquare.com\/article\/rs-2277227\/v1.html","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,11,17]],"date-time":"2023-11-17T16:41:35Z","timestamp":1700239295000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.researchsquare.com\/article\/rs-2277227\/v1"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,12,21]]},"references-count":100,"URL":"https:\/\/doi.org\/10.21203\/rs.3.rs-2277227\/v1","relation":{},"subject":[],"published":{"date-parts":[[2022,12,21]]},"subtype":"preprint"}}