caveolin 1
Last updated 18 Aug 2020
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The CAV1 gene provides instructions for making a protein called caveolin-1. This protein appears to have diverse functions in cells and tissues throughout the body.
Normal function
The CAV1 gene provides instructions for making a protein called caveolin-1. This protein appears to have diverse functions in cells and tissues throughout the body.
Caveolin-1 is the major component of caveolae, which are small pouches in the membrane that surrounds cells. Caveolae have multiple functions, some of which are not well understood. They are known to be involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways. Studies suggest that caveolae are particularly numerous in adipocytes, which are cells that store fats for energy. Adipocytes make up most of the body's fatty (adipose) tissue. In these cells, caveolae appear to be essential for the normal transport, processing, and storage of fats.
Caveolin-1 is also found in many other parts of cells, where it regulates various chemical signaling pathways. Through these pathways, caveolin-1 is involved in regulating cell growth and division (proliferation), the process by which cells mature to perform specific functions (differentiation), cell survival and the self-destruction of cells (apoptosis), and cell movement. The functions of caveolin-1 likely differ depending on the type of cell and the part of the cell where the protein is found.
Conditions referring to this gene or chromosome
Other names
BSCL3
CAV
caveolin 1, caveolae protein, 22kDa
caveolin-1 isoform alpha
caveolin-1 isoform beta
cell growth-inhibiting protein 32
CGL3
LCCNS
MSTP085
PPH3
VIP21
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Further reading and references
- caveolin 1; MedlinePlus, National Library of Medicine.
- Boscher C, Nabi IR. Caveolin-1: role in cell signaling. Adv Exp Med Biol. 2012;729:29-50. doi: 10.1007/978-1-4614-1222-9_3.
- Cao H, Alston L, Ruschman J, Hegele RA. Heterozygous CAV1 frameshift mutations (MIM 601047) in patients with atypical partial lipodystrophy and hypertriglyceridemia. Lipids Health Dis. 2008 Jan 31;7:3. doi: 10.1186/1476-511X-7-3.
- Garg A, Kircher M, Del Campo M, Amato RS, Agarwal AK; University of Washington Center for Mendelian Genomics. Whole exome sequencing identifies de novo heterozygous CAV1 mutations associated with a novel neonatal onset lipodystrophy syndrome. Am J Med Genet A. 2015 Aug;167A(8):1796-806. doi: 10.1002/ajmg.a.37115. Epub 2015 Apr 21.
- Kim CA, Delepine M, Boutet E, El Mourabit H, Le Lay S, Meier M, Nemani M, Bridel E, Leite CC, Bertola DR, Semple RK, O'Rahilly S, Dugail I, Capeau J, Lathrop M, Magre J. Association of a homozygous nonsense caveolin-1 mutation with Berardinelli-Seip congenital lipodystrophy. J Clin Endocrinol Metab. 2008 Apr;93(4):1129-34. doi: 10.1210/jc.2007-1328. Epub 2008 Jan 22.
- Quest AF, Lobos-Gonzalez L, Nunez S, Sanhueza C, Fernandez JG, Aguirre A, Rodriguez D, Leyton L, Torres V. The caveolin-1 connection to cell death and survival. Curr Mol Med. 2013 Feb;13(2):266-81. doi: 10.2174/156652413804810745.
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