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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
Published on: October 4, 2024
948
Structure, Function, and Regulation of the SRMS Tyrosine Kinase
Chakia J McClendon1, W Todd Miller1,2
1Department of Physiology and Biophysics, Stony Brook University, Stony Brook, NY 11794-8661, USA.
International Journal of Molecular Sciences
|June 18, 2020
Summary
Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (SRMS) is a tyrosine kinase with limited known functions. This review summarizes current SRMS knowledge, identifies signaling partners, and discusses its role in cancer.
Area of Science:
- Biochemistry
- Molecular Biology
- Oncology
Background:
- Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristoylation sites (SRMS) is a nonreceptor tyrosine kinase.
- SRMS belongs to a family including Brk (PTK6) and Frk.
- Limited information exists on SRMS structure, function, and regulation compared to other tyrosine kinases.
Purpose of the Study:
- To review the current state of knowledge on SRMS.
- To identify downstream signaling partners of SRMS.
- To discuss the potential involvement of SRMS in cancer cell signaling.
Main Methods:
- Literature review of existing SRMS research.
- Analysis of recent findings on SRMS downstream signaling.
- Development of a structural model for SRMS.
Main Results:
- Summarized current understanding of SRMS.
- Identified potential downstream signaling partners.
- Presented a structural model for SRMS enzyme.
Conclusions:
- SRMS is an understudied tyrosine kinase.
- Further research is needed to elucidate SRMS function and regulation.
- SRMS may play a role in cancer cell signaling.
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