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    Nat Neurosci. 1999 Jul;2(7):611-7.

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

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

    Source

    Department of Human Genetics, University of Michigan Medical School, Ann Arbor 48109-0618, USA.

    Abstract

    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.

    PMID:
    10404183
    [PubMed - indexed for MEDLINE]

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