TY - JOUR
T1 - Requirement for annexin A1 in plasma membrane repair
AU - McNeil, Anna K.
AU - Rescher, Ursula
AU - Gerke, Volker
AU - McNeil, Paul L.
PY - 2006/11/17
Y1 - 2006/11/17
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=33845951914&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33845951914&partnerID=8YFLogxK
U2 - 10.1074/jbc.M606406200
DO - 10.1074/jbc.M606406200
M3 - Article
C2 - 16984915
AN - SCOPUS:33845951914
SN - 0021-9258
VL - 281
SP - 35202
EP - 35207
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 46
ER -