VIP21‐Caveolin, a protein of the trans‐Golgi network and caveolae
- 6 June 1994
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 346 (1), 88-91
- https://doi.org/10.1016/0014-5793(94)00466-8
Abstract
VIP21-Caveolin is a component of the filamentous coat surrounding the invaginations of the plasma membrane called caveolae. Unlike the vesicular coat proteins identified so far, VIP21-Caveolin can be classified as an integral membrane protein. Furthermore, it is found in high molecular mass oligomers. Based on its localisation in specialised membrane subdomains, a role for VIP21-Caveolin in membrane protein sorting has been proposed.Keywords
This publication has 39 references indexed in Scilit:
- Occludin: a novel integral membrane protein localizing at tight junctions.The Journal of cell biology, 1993
- Multisubunit assembly of an integral plasma membrane channel protein, gap junction connexin43, occurs after exit from the ERCell, 1993
- The sequence of human caveolin reveals identity with VIP21, a component of transport vesiclesFEBS Letters, 1992
- Caveolin, a protein component of caveolae membrane coatsCell, 1992
- Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surfaceCell, 1992
- Potocytosis: Sequestration and Transport of Small Molecules by CaveolaeScience, 1992
- Cholesterol controls the clustering of the glycophospholipid-anchored membrane receptor for 5-methyltetrahydrofolate.The Journal of cell biology, 1990
- Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells.The Journal of cell biology, 1990
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986
- THE FINE STRUCTURE OF THE GALL BLADDER EPITHELIUM OF THE MOUSEThe Journal of cell biology, 1955