Document Detail

Membrane-mediated assembly of annexins studied by site-directed spin labeling.
MedLine Citation:
PMID:  9712869     Owner:  NLM     Status:  MEDLINE    
Annexins are soluble proteins that bind to membranes in the presence of Ca2+. Crystal structures have been determined for some soluble forms, but little is known about the important membrane-bound state. We employed site-directed spin labeling to demonstrate that 1) annexin XII assumes a trimer configuration similar to the crystal structure when bound to bilayers under physiological conditions; 2) trimer assembly on bilayers is remarkably rapid, occurring on a millisecond time scale, whereas subunit exchange requires hours; and 3) different annexins can mix to form heterotrimers. The rapid assembly and heterotrimer formation have important implications concerning the cellular functions of annexins.
R Langen; J M Isas; H Luecke; H T Haigler; W L Hubbell
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  273     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  1998 Aug 
Date Detail:
Created Date:  1998-09-24     Completed Date:  1998-09-24     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  22453-7     Citation Subset:  IM    
Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095, USA.
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MeSH Terms
Annexins / chemistry,  genetics,  metabolism*
Cell Membrane / metabolism
Electron Spin Resonance Spectroscopy
Models, Molecular
Mutagenesis, Site-Directed
Spin Labels
Grant Support
Reg. No./Substance:
0/Annexins; 0/Spin Labels

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