VIP17/MAL, a proteolipid in apical transport vesicles
Open Access
- 27 December 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 377 (3) , 465-469
- https://doi.org/10.1016/0014-5793(95)01396-2
Abstract
VIP17 is a proteolipid enriched in the CHAPS‐insoluble complexes from MDCK cells, and a candidate component of the molecular machinery responsible for the sorting and targeting of proteins to the apical surface. Cloning and sequencing of the cDNA encoding the protein revealed that it is the canine homolog of the human and rat MAL proteins. Analysis by immunofluorescence microscopy of epitope‐tagged VIP17/MAL expressed transiently in BHK cells and stably in MDCK cells revealed a perinuclear, vesicular, and plasmalemmal staining. In MDCK cells the distribution was mainly in vesicular structures in the apical cytoplasm. These and other results suggest that VIP17/MAL is an important component in vesicular trafficking cycling between the Golgi complex and the apical plasma membrane.Keywords
This publication has 34 references indexed in Scilit:
- Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytesJournal of Neuroscience Research, 1995
- Different requirements for NSF, SNAP, and Rab proteins in apical and basolateral transport in MDCK cellsCell, 1995
- VIP21, a 21-kD membrane protein is an integral component of trans-Golgi-network-derived transport vesicles.The Journal of cell biology, 1992
- Caveolin, a protein component of caveolae membrane coatsPublished by Elsevier ,1992
- 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
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- The trans Golgi Network: Sorting at the Exit Site of the Golgi ComplexScience, 1986
- Immunogenic structure of the influenza virus hemagglutininCell, 1982
- ProteolipidsAnnual Review of Biochemistry, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970