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

Nature neuroscience | Jul 2, 1999

http://www.ncbi.nlm.nih.gov/pubmed/10404183

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 RIS Download

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

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Associated grants

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

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