VIP17/MAL, a Proteolipid in Apical Transport Vesicles

FEBS Lett. 1995 Dec 27;377(3):465-9. doi: 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.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Biological Transport
  • Cell Compartmentation
  • Cell Polarity / physiology*
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Dogs
  • Fluorescent Antibody Technique
  • Kidney / cytology
  • Membrane Transport Proteins*
  • Molecular Sequence Data
  • Myelin Proteins*
  • Myelin and Lymphocyte-Associated Proteolipid Proteins
  • Proteolipids / genetics*
  • Proteolipids / isolation & purification
  • Proteolipids / metabolism
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Transfection

Substances

  • DNA, Complementary
  • MAL protein, human
  • Mal protein, rat
  • Membrane Transport Proteins
  • Myelin Proteins
  • Myelin and Lymphocyte-Associated Proteolipid Proteins
  • Proteolipids

Associated data

  • GENBANK/M15800
  • GENBANK/U31367
  • GENBANK/X82557
  • GENBANK/X92505