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

Published

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

Pubmed Central ID

  • 10404183

Electronic International Standard Serial Number (EISSN)

  • 1546-1726

International Standard Serial Number (ISSN)

  • 1097-6256

Digital Object Identifier (DOI)

  • 10.1038/10165

Language

  • eng