Abstract:
:Caveolin, a 21- to 24-kDa integral membrane protein, is a principal component of caveolae membranes. Caveolin interacts directly with heterotrimeric guanine nucleotide binding proteins (G proteins) and can functionally regulate their activity. Here, an approximately 20-kDa caveolin-related protein, caveolin-2, was identified through microsequencing of adipocyte-derived caveolin-enriched membranes; caveolin was retermed caveolin-1. Caveolins 1 and 2 are similar in most respects. mRNAs for both caveolin-1 and caveolin-2 are most abundantly expressed in white adipose tissue and are induced during adipocyte differentiation. Caveolin-2 colocalizes with caveolin-1, indicating that caveolin-2 also localizes to caveolae. However, caveolin-1 and caveolin-2 differ in their functional interactions with heterotrimeric G proteins, possibly explaining why caveolin-1 and -2 are coexpressed within a single cell.
journal_name
Proc Natl Acad Sci U S Aauthors
Scherer PE,Okamoto T,Chun M,Nishimoto I,Lodish HF,Lisanti MPdoi
10.1073/pnas.93.1.131subject
Has Abstractpub_date
1996-01-09 00:00:00pages
131-5issue
1eissn
0027-8424issn
1091-6490journal_volume
93pub_type
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:1971-12-01 00:00:00
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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更新日期:2003-07-22 00:00:00