Parton R G
Department of Physiology & Pharmacology, Centre for Molecular and Cellular Biology, University of Queensland, 4072Brisbane, Australia.
Curr Opin Cell Biol. 1996 Aug;8(4):542-8. doi: 10.1016/s0955-0674(96)80033-0.
In the past year, we have witnessed considerable progress towards an understanding of the workings of caveolae. Highlights include the identification of new caveolin family members, the characterization of VIP21-caveolin as a cholesterol-binding oligomeric protein, and evidence for functional interactions between caveolins and heterotrimeric G proteins. In addition, novel systems for caveolae purification and for studying caveolae biogenesis are starting to reveal insights into the molecular basis of caveolae formation and function.
在过去的一年里,我们在对小窝(caveolae)运作机制的理解方面取得了显著进展。其中的亮点包括鉴定出新的小窝蛋白(caveolin)家族成员,将VIP21-小窝蛋白表征为一种胆固醇结合寡聚蛋白,以及小窝蛋白与异源三聚体G蛋白之间功能相互作用的证据。此外,用于小窝纯化和研究小窝生物发生的新系统开始揭示小窝形成和功能的分子基础。