Lumeng C, Phelps S, Crawford G E, Walden P D, Barald K, Chamberlain J S
Department of Human Genetics, University of Michigan Medical School, Ann Arbor 48109-0618, USA.
Nat Neurosci. 1999 Jul;2(7):611-7. doi: 10.1038/10165.
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.
一项针对与β2-肌养蛋白相互作用的蛋白质的筛选，导致了MAST205（微管相关丝氨酸/苏氨酸激酶-205 kD）和一个新鉴定的同系物SAST（肌养蛋白相关丝氨酸/苏氨酸激酶）的分离。结合研究表明，β2-肌养蛋白与MAST205/SAST通过PDZ-PDZ结构域相互作用而结合。MAST205在神经肌肉接头处与β2-肌养蛋白和肌养蛋白相关蛋白共定位。SAST在脑血管系统、精子顶体和神经突中与肌养蛋白共定位。SAST和肌养蛋白与纯化的微管和微管相关蛋白高度相关，而肌养蛋白相关蛋白和肌营养不良蛋白仅部分与微管相关。我们的数据表明，MAST205和SAST通过肌养蛋白将肌营养不良蛋白/肌养蛋白相关蛋白网络与微管丝连接起来。
