期刊
PROCESSES
卷 8, 期 12, 页码 -出版社
MDPI
DOI: 10.3390/pr8121598
关键词
protein Ser/Thr phosphatase; Scp1; peptide phage display; substrate identification
资金
- Japanese Society for the Promotion of Sciences [15K05560, 19H03512, 20K21541]
- JSPS [18J20422]
- U-go grant from Niigata University
- Grants-in-Aid for Scientific Research [19H03512, 18J20422, 20K21541, 15K05560] Funding Source: KAKEN
Protein phosphorylation is the most widespread type of post-translational modification and is properly controlled by protein kinases and phosphatases. Regarding the phosphorylation of serine (Ser) and threonine (Thr) residues, relatively few protein Ser/Thr phosphatases control the specific dephosphorylation of numerous substrates, in contrast with Ser/Thr kinases. Recently, protein Ser/Thr phosphatases were reported to have rigid substrate recognition and exert various biological functions. Therefore, identification of targeted proteins by individual protein Ser/Thr phosphatases is crucial to clarify their own biological functions. However, to date, information on the development of methods for identification of the substrates of protein Ser/Thr phosphatases remains scarce. In turn, substrate-trapping mutants are powerful tools to search the individual substrates of protein tyrosine (Tyr) phosphatases. This review focuses on the development of novel methods for the identification of Ser/Thr phosphatases, especially small C-terminal domain phosphatase 1 (Scp1), using peptide-displayed phage library with AlF4-/BeF3-, and discusses the identification of putative inhibitors.
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