Identification of a dynein molecular motor component in Torpedo electroplax; binding and phosphorylation of Tctex‐1 by Fyn

FEBS Letters

Kraas, Jonathan R.²  Mou, Tao²  Swope, Sheridan L.²  Fung, Eric T.¹ 

[1] Department of Neuroscience, Howard Hughes Medical Institute, The Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA;EP08 Research Bld, Department of Neurology, Division of Neuroscience, Georgetown Institute for Cognitive and Computational Sciences, Georgetown University Medical Center, 3970 Reservoir Rd NW, Washington, DC 20007, USA

关键词: Neuromuscular junction;    Synaptogenesis;    Microtubule;    Phosphorylation;    Protein tyrosine kinase;    NMJ;    neuromuscular junction;    AChR;    acetylcholine receptor;    SH2;    Src homology 2;    SH3;    Src homology 3;    GST;    glutathione S-transferase;    pBK-CMV;    pBK-CMVΔlac;    CT-SrcK;    carboxy terminal pan Src kinase antibody;   

DOI  :  10.1016/S0014-5793(98)01069-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The microtubule protein Tctex-1 was cloned from Torpedo electroplax, a biochemical model of the neuromuscular junction, using the unique domain of Fyn in the yeast two hybrid system. Binding of Tctex-1 and Fyn also occurred in vitro. Torpedo Tctex-1 was contained within the molecular motor protein dynein. A Src class kinase was also complexed with dynein. Tctex-1 was enriched in electric organ vs. skeletal muscle, was present in the postsynaptic membrane, and coprecipitated with the acetylcholine receptor. The sequence of Tctex-1 contained a tyrosine phosphorylation motif and Tctex-1 could be phosphorylated by Fyn in vitro and in vivo. These data demonstrated that Tctex-1-containing dynein is a cytoskeletal element at the acetylcholine receptor-enriched postsynaptic membrane and suggested that Tctex-1 may be a substrate for Fyn.

【 授权许可】

Unknown