Requirement for annexin A1 in plasma membrane repair

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

Research output: Contribution to journalArticlepeer-review

183 Scopus citations


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
Issue number46
StatePublished - Nov 17 2006

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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