VIP21/CAVEOLIN IS A CHOLESTEROL-BINDING PROTEIN

被引:779
作者
MURATA, M
PERANEN, J
SCHREINER, R
WIELAND, F
KURZCHALIA, TV
SIMONS, K
机构
[1] EUROPEAN MOLEC BIOL LAB,CELL BIOL PROGRAMME,D-69117 HEIDELBERG,GERMANY
[2] MAX DELBRUCK CENTRUM MOLEK MED,D-13121 BERLIN,GERMANY
[3] UNIV HEIDELBERG,INST BIOCHEM 1,D-69120 HEIDELBERG,GERMANY
关键词
MEMBRANE MICRODOMAINS; INTRACELLULAR TRANSPORT; MEMBRANE RECONSTITUTION;
D O I
10.1073/pnas.92.22.10339
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
MP21/caveolin is localized to both caveolae and apical transport vesicles and presumably cycles between the cell surface and the Golgi complex. We have studied the lipid interactions of this protein by reconstituting Escherichia coli-expressed VIP21/caveolin into liposomes. Surprisingly, the protein reconstituted only with cholesterol-containing lipid mixtures. We demonstrated that the protein binds at least 1 mol of cholesterol per mole of protein and that this binding promotes formation of protein oligomers. These findings suggest that VIP21/caveolin, through its cholesterol-binding properties, serves a specific function in microdomain formation during membrane trafficking.
引用
收藏
页码:10339 / 10343
页数:5
相关论文
共 30 条