Interactions between beta 2-syntrophin and a family of microtubule-associated serine/threonine kinases.
Journal Article (Journal Article)
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.
Full Text
Duke Authors
Cited Authors
- Lumeng, C; Phelps, S; Crawford, GE; Walden, PD; Barald, K; Chamberlain, JS
Published Date
- July 1999
Published In
Volume / Issue
- 2 / 7
Start / End Page
- 611 - 617
PubMed ID
- 10404183
International Standard Serial Number (ISSN)
- 1097-6256
Digital Object Identifier (DOI)
- 10.1038/10165
Language
- eng
Conference Location
- United States