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Structure, Function, and Regulation of the SRMS Tyrosine Kinase

1
Department of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA
2
Department of Veterans Affairs Medical Center, Northport, NY 11768, USA
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2020, 21(12), 4233; https://doi.org/10.3390/ijms21124233
Received: 21 May 2020 / Revised: 8 June 2020 / Accepted: 12 June 2020 / Published: 14 June 2020
(This article belongs to the Special Issue Kinase Signal Transduction 2020)
Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (SRMS) is a tyrosine kinase that was discovered in 1994. It is a member of a family of nonreceptor tyrosine kinases that also includes Brk (PTK6) and Frk. Compared with other tyrosine kinases, there is relatively little information about the structure, function, and regulation of SRMS. In this review, we summarize the current state of knowledge regarding SRMS, including recent results aimed at identifying downstream signaling partners. We also present a structural model for the enzyme and discuss the potential involvement of SRMS in cancer cell signaling. View Full-Text
Keywords: tyrosine kinase; signal transduction; phosphorylation; SH3 domains; SH2 domains; Src family kinases tyrosine kinase; signal transduction; phosphorylation; SH3 domains; SH2 domains; Src family kinases
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McClendon, C.J.; Miller, W.T. Structure, Function, and Regulation of the SRMS Tyrosine Kinase. Int. J. Mol. Sci. 2020, 21, 4233.

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