Structure, Function, and Regulation of the SRMS Tyrosine Kinase

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 rela...

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Detalles Bibliográficos
Autores principales: McClendon, Chakia J., Miller, W. Todd
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2020
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7352994/
https://www.ncbi.nlm.nih.gov/pubmed/32545875
http://dx.doi.org/10.3390/ijms21124233
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author McClendon, Chakia J.
Miller, W. Todd
author_facet McClendon, Chakia J.
Miller, W. Todd
author_sort McClendon, Chakia J.
collection PubMed
description 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.
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spelling pubmed-73529942020-07-15 Structure, Function, and Regulation of the SRMS Tyrosine Kinase McClendon, Chakia J. Miller, W. Todd Int J Mol Sci Review 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. MDPI 2020-06-14 /pmc/articles/PMC7352994/ /pubmed/32545875 http://dx.doi.org/10.3390/ijms21124233 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
McClendon, Chakia J.
Miller, W. Todd
Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title_full Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title_fullStr Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title_full_unstemmed Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title_short Structure, Function, and Regulation of the SRMS Tyrosine Kinase
title_sort structure, function, and regulation of the srms tyrosine kinase
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7352994/
https://www.ncbi.nlm.nih.gov/pubmed/32545875
http://dx.doi.org/10.3390/ijms21124233
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