| Literature DB >> 10404183 |
C Lumeng1, S Phelps, G E Crawford, P D Walden, K Barald, J S Chamberlain.
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.Entities:
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Year: 1999 PMID： 10404183 DOI： 10.1038/10165
Source DB: PubMed Journal: Nat Neurosci ISSN： 1097-6256 Impact factor: 24.884