The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for tile assembly of caveolae membranes in vivo

Kallol Das, Renée Y. Lewis, Philipp E. Scherer, Michael P. Lisanti

Research output: Contribution to journalArticle

97 Citations (Scopus)

Abstract

The mammalian caveolin gene family consists of caveolins-1, -2, and -3. The expression of caveolin-3 is muscle-specific. In contrast, caveolins-1 and -2 are co-expressed, and they form a hetero-oligomeric complex in many cell types, with particularly high levels in adipocytes, endothelial cells, and fibroblasts. These caveolin hetero-oligomers are thought to represent the functional assembly units that drive caveolae formation in vivo. Here, we investigate the mechanism by which caveolins-1 and -2 form hetero-oligomers. We reconstituted this reciprocal interaction in vivo and in vitro using a variety of complementary approaches, including the generation of glutathione S-transferase fusion proteins and synthetic peptides. Taken together, our results indicate that the membrane-spanning domains of both caveolins-1 and - 2 play a critical role in mediating their ability to interact with each other. This is the first demonstration that these unusual membrane-spanning regions found in the caveolin family play a specific role in protein-protein interactions.

Original languageEnglish (US)
Pages (from-to)18721-18728
Number of pages8
JournalJournal of Biological Chemistry
Volume274
Issue number26
DOIs
StatePublished - Jun 25 1999

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Caveolin 2
Caveolins
Caveolin 1
Caveolae
Tile
Oligomers
Membranes
Caveolin 3
Proteins
Endothelial cells
Fibroblasts
Glutathione Transferase
Adipocytes
Muscle
Demonstrations
Fusion reactions
Endothelial Cells
Genes
Muscles
Peptides

ASJC Scopus subject areas

  • Biochemistry

Cite this

The membrane-spanning domains of caveolins-1 and -2 mediate the formation of caveolin hetero-oligomers. Implications for tile assembly of caveolae membranes in vivo. / Das, Kallol; Lewis, Renée Y.; Scherer, Philipp E.; Lisanti, Michael P.

In: Journal of Biological Chemistry, Vol. 274, No. 26, 25.06.1999, p. 18721-18728.

Research output: Contribution to journalArticle

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