VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles.
Open Access
- 1 September 1992
- journal article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 118 (5) , 1003-1014
- https://doi.org/10.1083/jcb.118.5.1003
Abstract
In simple epithelial cells, apical and basolateral proteins are sorted into separate vesicular carriers before delivery to the appropriate plasma membrane domains. To dissect the putative sorting machinery, we have solubilized Golgi-derived transport vesicles with the detergent CHAPS and shown that an apical marker, influenza haemagglutinin (HA), formed a large complex together with several integral membrane proteins. Remarkably, a similar set of CHAPS-insoluble proteins was found after solubilization of a total cellular membrane fraction. This allowed the cloning of a cDNA encoding one protein of this complex, VIP21 (Vesicular Integral-membrane Protein of 21 kD). The transiently expressed protein appeared on the Golgi-apparatus, the plasma membrane and vesicular structures. We propose that VIP21 is a component of the molecular machinery of vesicular transport.Keywords
This publication has 54 references indexed in Scilit:
- On the preparation of cryosections for immunocytochemistryPublished by Elsevier ,2004
- Plasma membrane protein sorting in polarized epithelial cells.The Journal of cell biology, 1992
- A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein β-adaptinNature, 1991
- SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeastPublished by Elsevier ,1990
- Clathrin-coated vesiclesCurrent Opinion in Cell Biology, 1989
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986
- A new type of coated vesicular carrier that appears not to contain clathrin: Its possible role in protein transport within the Golgi stackCell, 1986
- Reconstitution of the transport of protein between successive compartments of the golgi measured by the coupled incorporation of N-acetylglucosamineCell, 1984
- Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylationPublished by Elsevier ,1983
- Passage of viral membrane proteins through the Golgi complexJournal of Molecular Biology, 1981