Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. INVOLVEMENT IN CHOLESTEROL TRAFFICKING.
作者： Annette Uittenbogaard , Yun-shu Ying , Eric J. Smart
关键词: Cyclophilin A 、 Endoplasmic reticulum 、 Caveolae 、 Biology 、 Cyclophilin 、 Chaperone complex 、 Transfection 、 Caveolin 、 Cyclosporin a 、 Cell biology
摘要: Caveolin is a 22-kDa protein that appears to play critical role in regulating the cholesterol concentration of caveolae. Even though caveolin thought be membrane protein, several reports suggest this peculiar can traffic independently vesicles. We now present evidence cytosolic pool part heat-shock protein-immunophilin chaperone complex consisting caveolin, 56, cyclophilin 40, A, and cholesterol. Treatment NIH 3T3 cells with 1 microM cyclosporin A or 100 nM rapamycin disrupted putative transport prevented rapid (10-20 min) The lymphoid cell line, L1210-JF, does not express form an immunophilin-caveolin complex, newly synthesized Transfection cDNA into L1210-JF allowed assembly identical found cells. In addition, transfected was rapidly specifically transported These data strongly caveolin-chaperone mechanism by which from endoplasmic reticulum through cytoplasm
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