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Journal of Cell Science, Vol 103, Issue 4 1177-1192, Copyright © 1992 by Company of Biologists
JOURNAL ARTICLES |
CE Creutz, NG Kambouris, SL Snyder, HC Hamman, MR Nelson, W Liu and P Rock
Department of Pharmacology, University of Virginia, Charlottesville 22908.
The hypothesis that calcium-dependent membrane-binding proteins of the annexin family can influence intracellular membrane trafficking was tested by expressing five mammalian annexins in wild-type yeast cells (Saccharomyces cerevisiae) and in 13 yeast secretory (sec) mutants. Expression of human synexin (annexin VII) inhibited the growth of sec2, sec4 and sec15 mutants at a semi-permissive temperature. These three sec mutants are defective in the final step in the secretory pathway, the process of exocytosis. The inhibition of growth correlated with reduced viability and increased accumulation of internal invertase in these mutants when expressing synexin. Bovine endonexin (annexin IV) partially suppressed the growth defect of a sec2 mutant incubated at a semi-permissive temperature. Human synexin, human lipocortin (annexin I), and murine p68 (annexin VI) reduced the lag time associated with adaptation of sec2 mutants to galactose-containing medium. These interactions suggest that the annexins may influence specific steps in membrane trafficking associated with cell growth, secretion and plasma membrane remodelling.
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A. M. Brownawell and C. E. Creutz Calcium-dependent Binding of Sorcin to the N-terminal Domain of Synexin (Annexin VII) J. Biol. Chem., August 29, 1997; 272(35): 22182 - 22190. [Abstract] [Full Text] [PDF] |
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