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Protein A000519
Author-entered Data
V1.0, Peer Reviewed
Published 4 Feb 2005
Automated Data
Not Reviewed
As At Publication
Automated Data
Not Reviewed
Latest from 28 Jun 2010

UCSD-Nature Molecule Pages
Published online: 4 Feb 2005 | doi:10.1038/mp.a000519.01

Caveolin 1

Pingsheng Liu1, Richard G Anderson1

1Cell Biology, UT Southwestern Medical Center, TX 75390, US.

Correspondence should be addressed to Pingsheng Liu: Pingsheng.Liu@utsouthwestern.edu


Caveolin-1 is a 21 kDa integral membrane protein that functions as a principal structural component of invaginated caveolae in most mammalian cells. Although numerous studies indicate that caveolin-1 plays a role in signal transduction from caveolae, the molecular mechanisms of how caveolin-1 regulates cell signaling are still not well understood. The most popular hypothesis is that caveolin-1 may physically organize the signaling activity of multiple signaling molecules, in some cases, by its scaffolding domain (amino acids 82-101). Another hypothesis is that caveolin-1 functions to maintain the proper biological properties of caveolae, which may be necessary for signal transduction from this domain. One more postulated function of caveolin-1 is that caveolin-1 may bind to cholesterol and be involved in intracellular cholesterol transport.

Alternative names for this molecule: Cav; Cav-1; Cav1; Caveolin 1; Caveolin 1, caveolae protein, 22kD; Caveolin, caveolae protein, 22 kDa; Caveolin-1; VIP21

Transition Network Graph This molecule exists in 6 states and has 8 transitions between these states.

[map] View high resolution network map
 

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