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Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases.

A screen for proteins that interact with beta 2-syntrophin led to the isolation of MAST205 (microtubule-associated serine/threonine kinase-205 kD) and a newly identified homologue, SAST (syntrophin-associated serine/threonine kinase). Binding studies showed that beta 2-syntrophin and MAST205/SAST associated via a PDZ-PDZ domain interaction. MAST205 colocalized with beta 2-syntrophin and utrophin at neuromuscular junctions. SAST colocalized with syntrophin in cerebral vasculature, spermatic acrosomes and neuronal processes. SAST and syntrophin were highly associated with purified microtubules and microtubule-associated proteins, whereas utrophin and dystrophin were only partially associated with microtubules. Our data suggest that MAST205 and SAST link the dystrophin/utrophin network with microtubule filaments via the syntrophins.

Pubmed ID: 10404183


  • Lumeng C
  • Phelps S
  • Crawford GE
  • Walden PD
  • Barald K
  • Chamberlain JS


Nature neuroscience

Publication Data

July 2, 1999

Associated Grants

  • Agency: NIAMS NIH HHS, Id: AR44533
  • Agency: NIAMS NIH HHS, Id: P60AR20557

Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Brain
  • Cells, Cultured
  • Dystrophin-Associated Proteins
  • Hippocampus
  • Male
  • Membrane Proteins
  • Mice
  • Mice, Inbred C57BL
  • Mice, Inbred mdx
  • Microtubule-Associated Proteins
  • Molecular Sequence Data
  • Muscle, Skeletal
  • Neurons
  • Protein-Serine-Threonine Kinases
  • Pyramidal Cells
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Testis