SH3-domain mutations selectively disrupt Csk homodimerization or PTPN22 binding.

doi:10.1038/s41598-022-09589-9

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Article

SH3-domain mutations selectively disrupt Csk homodimerization or PTPN22 binding.

Scientific reports - 7 Apr 2022

Brian Ben F, Sjaastad Frances V, Freedman Tanya S

Abstract excerpt

The kinase Csk is the primary negative regulator of the Src-family kinases (SFKs, e.g., Lck, Fyn, Lyn, Hck, Fgr, Blk, Yes), phosphorylating a tyrosine on the SFK C-terminal tail that mediates autoinhibition. Csk also binds phosphatases, including PTPN12 (PTP-PEST) and immune-cell PTPN22 (LYP/Pep), which dephosphorylate the SFK activation loop to promote autoinhibition. Csk-binding proteins (e.g., CBP/PAG1)...

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Share to Adaptor Proteins, Signal Transducing
Share to CSK Tyrosine-Protein Kinase
Share to Membrane Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Tyrosine Phosphatase, Non-Receptor Type 22

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Identifiers

PMID: 35393453
DOI: 10.1038/s41598-022-09589-9
PMCID: PMC8989918

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