Article
Conformational defects slow Golgi exit, block oligomerization, and reduce raft affinity of caveolin-1 mutant proteins.
Molecular biology of the cell - 1 Oct 2004
Ren Xiaoyan, Ostermeyer Anne G, Ramcharan Lynne T, Zeng Youchun, Lublin Douglas M, Brown Deborah A
Abstract excerpt
Caveolin-1, a structural protein of caveolae, is cleared unusually slowly from the Golgi apparatus during biosynthetic transport. Furthermore, several caveolin-1 mutant proteins accumulate in the Golgi apparatus. We examined this behavior further in this mutant study. Golgi accumulation probably resulted from loss of Golgi exit information, not exposure of cryptic retention signals, because several deletion...
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