Requirement for annexin A1 in plasma membrane repair

Anna K. McNeil, Ursula Rescher, Volker Gerke, Paul L McNeil

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Abstract

Ca2+ entering a cell through a torn or disrupted plasma membrane rapidly triggers a combination of homotypic and exocytotic membrane fusion events. These events serve to erect a reparative membrane patch and then anneal it to the defect site. Annexin A1 is a cytosolic protein that, when activated by micromolar Ca2+, binds to membrane phospholipids, promoting membrane aggregation and fusion. We demonstrate here that an annexin A1 function-blocking antibody, a small peptide competitor, and a dominant-negative annexin A1 mutant protein incapable of Ca2+ binding all inhibit resealing. Moreover, we show that, coincident with a resealing event, annexin A1 becomes concentrated at disruption sites. We propose that Ca2+ entering through a disruption locally induces annexin A1 binding to membranes, initiating emergency fusion events whenever and wherever required.

Original languageEnglish (US)
Pages (from-to)35202-35207
Number of pages6
JournalJournal of Biological Chemistry
Volume281
Issue number46
DOIs
Publication statusPublished - Nov 17 2006

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ASJC Scopus subject areas

  • Biochemistry

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McNeil, A. K., Rescher, U., Gerke, V., & McNeil, P. L. (2006). Requirement for annexin A1 in plasma membrane repair. Journal of Biological Chemistry, 281(46), 35202-35207. https://doi.org/10.1074/jbc.M606406200