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Identification of a dynein molecular motor component in Torpedo electroplax; binding and phosphorylation of Tctex‐1 by Fyn 1
Author(s) -
Mou Tao,
Kraas Jonathan R.,
Fung Eric T.,
Swope Sheridan L.
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01069-2
Subject(s) - torpedo , dynein , fyn , microtubule , microbiology and biotechnology , biology , acetylcholine receptor , phosphorylation , biochemistry , chemistry , proto oncogene tyrosine protein kinase src , receptor
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.