Kinesin-1 plays a role in transport of SNAP-25 to the plasma membrane

April M Morton, Anthony L. Cunningham, Russell J Diefenbach

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

The cellular molecular motor kinesin-1 mediates the microtubule-dependent transport of a range of cargo. We have previously identified an interaction between the cargo-binding domain of kinesin-1 heavy chain KIF5B and the membrane-associated SNARE proteins SNAP-25 and SNAP-23. In this study we further defined the minimal SNAP-25 binding domain in KIF5B to residues 874-894. Overexpression of a fragment of KIF5B (residues 594-910) resulted in significant colocalization with SNAP-25 with resulting blockage of the trafficking of SNAP-25 to the periphery of cells. This indicates that kinesin-1 facilitates the transport of SNAP-25 containing vesicles as a prerequisite to SNAP-25 driven membrane fusion events.

Original languageEnglish
Pages (from-to)388-393
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume391
Issue number1
DOIs
Publication statusPublished - 1 Jan 2010
Externally publishedYes

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Keywords

  • Binding Sites
  • Cell Membrane
  • HeLa Cells
  • Humans
  • Kinesin
  • Protein Structure, Tertiary
  • Protein Transport
  • Synaptic Vesicles
  • Synaptosomal-Associated Protein 25
  • Journal Article
  • Research Support, Non-U.S. Gov't

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