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.
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
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
Nat. Neurosci.
Date: Jul. 01, 1999
PubMed ID: 10404183
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