ArticlePloS one2009
The tyrosine kinase Csk dimerizes through Its SH3 domain.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Review
- Dissection of the catalytic and regulatory structure-function relationships of Csk protein tyrosine kinase.Frontiers in cell and developmental biology · 2023Review
- SH3-domain mutations selectively disrupt Csk homodimerization or PTPN22 binding.Scientific reports · 2022Article
- Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions.The Journal of biological chemistry · 2019Article
- Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association.Scientific reports · 2019Article
- Protein Tyrosine Signaling and its Potential Therapeutic Implications in Carcinogenesis.Current pharmaceutical design · 2017Review
- Article
- Domain interactions of C-terminal Src Kinase determined through NMR spectroscopy with segmental isotope labeling.Protein & cell · 2017Article
- Identification and characterization of the role of c-terminal Src kinase in dengue virus replication.Scientific reports · 2016Article
- Evolutionary, physicochemical, and functional mechanisms of protein homooligomerization.Progress in molecular biology and translational science · 2013Review
- IGF-I stimulates cooperative interaction between the IGF-I receptor and CSK homologous kinase that regulates SHPS-1 phosphorylation in vascular smooth muscle cells.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.Physical biology · 2011Review
- Proteins at work: a combined small angle X-RAY scattering and theoretical determination of the multiple structures involved on the protein kinase functional landscape.The Journal of biological chemistry · 2010Article
- Bivalent inhibitors of protein kinases.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The Src family kinases possess two sites of tyrosine phosphorylation that are critical to the regulation of kinase activity. Autophosphorylation on an activation loop tyrosine residue (Tyr 416 in commonly used chicken c-Src numbering) increases catalytic activity, while phosphorylation of a C-terminal tyrosine (Tyr 527 in c-Src) inhibits activity. The latter modification is achieved by the tyrosine kinase Csk (C-terminal Src Kinase), but the complete inactivation of the Src family kinases also requires the dephosphorylation of the activation loop tyrosine. The SH3 domain of Csk recruits the tyrosine phosphatase PEP, allowing for the coordinated inhibition of Src family kinase activity. We have discovered that Csk forms homodimers through interactions mediated by the SH3 domain in a manner that buries the recognition surface for SH3 ligands. The formation of this dimer would therefore block the recruitment of tyrosine phosphatases and may have important implications for the regulation of Src kinase activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.