Caveolae, caveolin and caveolin-rich membrane domains: a signalling hypothesis

MP Lisanti, PE Scherer, ZL Tang, M Sargiacomo - Trends in cell biology, 1994 - Elsevier
MP Lisanti, PE Scherer, ZL Tang, M Sargiacomo
Trends in cell biology, 1994Elsevier
Abstract Caveolae, 50–100 nm invaginations that represent a subcompartment of the
plasma membrane, have been known for many years, but their exact roles remain uncertain.
The findings that the caveola coat protein caveolin is a v-Src substrate and that G-protein-
coupled receptors are present in caveolae have suggested a relationship between
caveolae, caveolin and transmembrane signalling. The recent isolation of caveolin-rich
membrane domains in which caveolin exists as a hetero-oligomeric complex with integral …
Abstract
Caveolae, 50–100 nm invaginations that represent a subcompartment of the plasma membrane, have been known for many years, but their exact roles remain uncertain. The findings that the caveola coat protein caveolin is a v-Src substrate and that G-protein-coupled receptors are present in caveolae have suggested a relationship between caveolae, caveolin and transmembrane signalling. The recent isolation of caveolin-rich membrane domains in which caveolin exists as a hetero-oligomeric complex with integral membrane proteins and known cytoplasmic signalling molecules provides support for this hypothesis. Compartmentalization of certain signalling molecules within caveolae could allow efficient and rapid coupling of activated receptors to more than one effector system.
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