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

Citation
K. Das et al., The membrane-spanning domains of caveolins-1 and-2 mediate the formation of gaveolin hetero-oligomers - Implications for the assembly of caveolae membranes in vivo, J BIOL CHEM, 274(26), 1999, pp. 18721-18728
Citations number
52
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF BIOLOGICAL CHEMISTRY
ISSN journal
00219258 → ACNP
Volume
274
Issue
26
Year of publication
1999
Pages
18721 - 18728
Database
ISI
SICI code
0021-9258(19990625)274:26<18721:TMDOCA>2.0.ZU;2-G
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 i nvestigate 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 glutathion e S-transferase fusion proteins and synthetic peptides. Taken together, our results indicate that the membrane-spanning domains of both caveolins-1 an d -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-prote in interactions.