Interactions between β2-syntrophin and a family of microtubule-associated serine/threonine kinases

被引：134

作者：

Lumeng, C

Phelps, S

Crawford, GE

Walden, PD

Barald, K

Chamberlain, JS ^{[1
]}

机构：

[1] Univ Michigan, Sch Med, Dept Human Genet, Ann Arbor, MI 48109 USA

[2] Univ Michigan, Sch Med, Mol & Cellular Biol Program, Ann Arbor, MI 48109 USA

[3] Univ Michigan, Sch Med, Ctr Gene Therapy, Ann Arbor, MI 48109 USA

[4] NYU, Sch Med, Dept Urol, New York, NY 10016 USA

[5] Univ Michigan, Sch Med, Dept Anat & Cell Biol, Ann Arbor, MI 48109 USA

来源：

NATURE NEUROSCIENCE | 1999年 / 2卷 / 07期

关键词：

D O I：

10.1038/10165

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

引用

页码：611 / 617

页数：7

共 48 条

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