- Caveolin
protein
Name = Caveolin 1, caveolae protein, 22kDa
caption =
width =
HGNCid = 1527
Symbol =CAV1
AltSymbols = CAV
EntrezGene = 857
OMIM = 601047
RefSeq = NM_001753
UniProt = Q03135
PDB =
ECnumber =
Chromosome = 7
Arm = q
Band = 31
LocusSupplementaryData = protein
Name = Caveolin 2
caption =
width =
HGNCid = 1528
Symbol =CAV2
AltSymbols =
EntrezGene = 858
OMIM = 601048
RefSeq = NM_001233
UniProt = P51636
PDB =
ECnumber =
Chromosome = 7
Arm = q
Band = 31
LocusSupplementaryData = protein
Name =Caveolin 3
caption =
width =
HGNCid = 1529
Symbol = CAV3
AltSymbols =
EntrezGene = 859
OMIM = 601253
RefSeq = NM_001234
UniProt = P56539
PDB =
ECnumber =
Chromosome = 3
Arm = p
Band = 25
LocusSupplementaryData =Caveolins are a family of proteins that are involved in receptor independent endocytosis. The caveolin
gene family has three members invertebrate s: CAV1, CAV2, and CAV3, coding for the proteins caveolin-1, caveolin-2 and caveolin-3, respectively. All three members aremembrane proteins with similar structure. Caveolin formsoligomers and associates with cholesterol and sphingolipids in certain areas of thecell membrane , leading to the formation ofcaveolae .Structure and expression
The caveolins are similar in structure. They all form hairpin loops that are inserted into the cell membrane. Both the
C-terminus and theN-terminus face the cytoplasmic side of the membrane. There are twoisoform s of caveolin-1: caveolin-1α and caveolin-1β, the latter lacking a part of the N-terminus.Caveolins are found in the majority of adherent, mammalian cells.
* Caveolin-1 is most prominently expressed in endothelial, fibrous and adipose tissue.
* The expression pattern of caveolin-2 is similar to that of caveolin-1; it seems to be co-expressed with caveolin-1.
* The expression of caveolin-3 is restricted to striated and smooth muscle.Function
The functions of caveolins are still under intensive investigation. They are best known for their role in the formation of 50
nanometer -sizedinvagination s of the plasma membrane, called caveolae.Oligomer s of caveolin form the coat of these domains. Cells that lack caveolins also lack caveolae. Many functions are ascribed to these domains, ranging fromendocytosis andtranscytosis tosignal transduction .Caveolin-1 has also been shown to play a role in the
integrin signaling. Thetyrosine phosphorylated form of caveolin-1 colocalizes withfocal adhesion s, suggesting a role for caveolin-1 in migration. Indeed, downregulation of caveolin-1 leads to less efficient migrationin vitro .Genetically engineered mice that lack caveolin-1 and caveolin-2 are viable and fertile, showing that neither the caveolins, nor caveolae are essential in embryonic development or reproduction of these animals. However, knock-out animals do develop abnormal, hypertrophic lungs and cardiac myopathy, leading to a reduction in life span. Mice lacking caveolins also suffer from impaired angiogenic responses as well as abnormal responses to vasoconstrictive stimuli. In
zebrafish , lack of caveolins leads to embryonic lethality, suggesting that higher vertebrates (as exemplified by mice) have developed compensation or redundancy for the functions of caveolins.Role in disease
Cancer
Caveolins have a paradoxical role in the development of this disease. They have been implicated in both tumor suppression and oncogenesis. High expression of caveolins leads to inhibition of cancer-related pathways, such as
growth factor signaling pathways. However, certain cancer cells that express caveolins have been shown to be more aggressive and metastatic, because of a potential for anchorage-independent growth.Cardiovascular diseases
Caveolins are thought to play an important role during the development of atherosclerosis.Furthermore, caveolin-3 has been associated with
Long QT syndrome .Muscular dystrophy
Caveolin-3 has been implicated in the development of certain muscular dystrophies.
External links
* [http://macromoleculeinsights.com/caveolin.php The Caveolin Protein]
*
* [http://www.dmd.nl/cav3_home.html Caveolin-3 page]References
*cite journal
title=The Caveolin proteins
author=Terence M Williams
coauthors=Michael P Lisanti
journal=Genome Biol.
year=2004
volume=5
issue=3
pages=214
pmid=15003112
doi=10.1186/gb-2004-5-3-214
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