VIP17/MAL, a proteolipid in apical transport vesicles

Daniele Zacchetti, Johan Peränen, Masayuki Murata, Klaus Fiedler, Kai Simons

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)465-469
Number of pages5
JournalFEBS Letters
Issue number3
Publication statusPublished - Dec 27 1995


  • Apical transport
  • Detergent-insoluble complex
  • Madin-Darby canine kidney cell
  • Myelin biogenesis
  • Proteolipid
  • Vesicular trafficking

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology


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