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- Title
Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases.
- Authors
Lumeng, C; Phelps, S; Crawford, G E; Walden, P D; Barald, K; Chamberlain, J S
- 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.
- Publication
Nature neuroscience, 1999, Vol 2, Issue 7, p611
- ISSN
1097-6256
- Publication type
Journal Article
- DOI
10.1038/10165