Title : Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion.

Pub. Date : 1996 Oct 1

PMID : 8855260






7 Functional Relationships(s)
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1 Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion. Guanosine Triphosphate annexin A7 Homo sapiens
2 Membrane fusion protein synexin (annexin VII) as a Ca2+/GTP sensor in exocytotic secretion. Guanosine Triphosphate annexin A7 Homo sapiens
3 However, the calcium-dependent membrane fusion reaction driven by synexin (annexin VII) is an in vitro model for this process, which we have now found to be further activated by GTP. Guanosine Triphosphate annexin A7 Homo sapiens
4 However, the calcium-dependent membrane fusion reaction driven by synexin (annexin VII) is an in vitro model for this process, which we have now found to be further activated by GTP. Guanosine Triphosphate annexin A7 Homo sapiens
5 The mechanism of fusion activation depends on the unique ability of synexin to bind and hydrolyze GTP in a calcium-dependent manner, both in vitro and in vivo in streptolysin O-permeabilized chromaffin cells. Guanosine Triphosphate annexin A7 Homo sapiens
6 The required [Ca2+] for GTP binding by synexin is in the range of 50-200 microM, which is known to occur at exocytotic sites in chromaffin cells, neurons, and other cell types. Guanosine Triphosphate annexin A7 Homo sapiens
7 Previous immunolocalization studies place synexin at exocytotic sites in chromaffin cells, and we conclude that synexin is an atypical G protein that may be responsible for both detecting and mediating the Ca2+/GTP signal for exocytotic membrane fusion. Guanosine Triphosphate annexin A7 Homo sapiens