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Kinesin-dependent axonal transport is mediated by the sunday driver (SYD) protein.

A broadly conserved membrane-associated protein required for the functional interaction of kinesin-I with axonal cargo was identified. Mutations in sunday driver (syd) and the axonal transport motor kinesin-I cause similar phenotypes in Drosophila, including aberrant accumulations of axonal cargoes. GFP-tagged mammalian SYD localizes to tubulovesicular structures that costain for kinesin-I and a marker of the secretory pathway. Coimmunoprecipitation analysis indicates that mouse SYD forms a complex with kinesin-I in vivo. Yeast two-hybrid analysis and in vitro interaction studies reveal that SYD directly binds kinesin-I via the tetratricopeptide repeat (TPR) domain of kinesin light chain (KLC) with K(d) congruent with 200 nM. We propose that SYD mediates the axonal transport of at least one class of vesicles by interacting directly with KLC.

Pubmed ID: 11106729

Authors

  • Bowman AB
  • Kamal A
  • Ritchings BW
  • Philp AV
  • McGrail M
  • Gindhart JG
  • Goldstein LS

Journal

Cell

Publication Data

November 10, 2000

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM35252

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Axonal Transport
  • Behavior, Animal
  • Biological Transport
  • Carrier Proteins
  • Cell Compartmentation
  • Cloning, Molecular
  • Drosophila
  • Drosophila Proteins
  • Insect Proteins
  • Kinesin
  • Larva
  • Membrane Proteins
  • Microtubule-Associated Proteins
  • Microtubules
  • Molecular Motor Proteins
  • Molecular Sequence Data
  • Multigene Family
  • Mutation
  • Protein Binding
  • Protein Subunits
  • Two-Hybrid System Techniques
  • trans-Golgi Network