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Annexins – unique membrane binding proteins with diverse functions
Author(s) -
Ursula Rescher,
Volker Gerke
Publication year - 2004
Publication title -
journal of cell science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.384
H-Index - 278
eISSN - 1477-9137
pISSN - 0021-9533
DOI - 10.1242/jcs.01245
Subject(s) - annexin a2 , biology , microbiology and biotechnology , annexin , membrane protein , phospholipid scramblase , annexin a1 , gene knockdown , biochemistry , membrane , phospholipid , cell , phosphatidylserine , gene
Annexins are a well-known multigene family of Ca(2+)-regulated phospholipid-binding and membrane-binding proteins. Recent work employing annexin-knockdown or - knockout models has provided new insights into the biological functions of different annexin proteins. Transient annexin depletion by RNA interference and the expression of dominant-negative mutant proteins has revealed roles for the proteins in membrane processes ranging from the control of membrane structure to certain membrane transport phenomena. Although such functions correlate well with the ability of annexins to interact with cellular membranes in a reversible and regulated manner, some activities are membrane independent, probably because annexins can also engage in specific protein-protein interactions. Among other things, this is evident in annexin A1- and A2-knockout mice, which show impaired regulation of neutrophil extravasation and defects in plasmin generation, respectively.

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