ArticleProceedings of the National Academy of Sciences of the United States of America1994
Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
80 citing papers in PubMed, 223 citations in OpenAlex.
- Csk controls leukocyte extravasation via local regulation of Src family kinases and cortactin signaling.Frontiers in immunology · 2024Article
- Elucidating the susceptibility to breast cancer: an in-depth proteomic and transcriptomic investigation into novel potential plasma protein biomarkers.Frontiers in molecular biosciences · 2023Article
- CSK-mediated signalling by integrins in cancer.Frontiers in cell and developmental biology · 2023Review
- Dissection of the catalytic and regulatory structure-function relationships of Csk protein tyrosine kinase.Frontiers in cell and developmental biology · 2023Review
- A phospho-tyrosine-based signaling module using SPOP, CSK, and LYN controls TLR-induced IRF activity.Science advances · 2022Article
- SH3-domain mutations selectively disrupt Csk homodimerization or PTPN22 binding.Scientific reports · 2022Article
- GDF6-CD99 Signaling Regulates Src and Ewing Sarcoma Growth.Cell reports · 2020Article
- FAK-Dependent Cell Motility and Cell Elongation.Cells · 2020Review
- Controlling Fibronectin Fibrillogenesis Using Visible Light.Frontiers in molecular biosciences · 2020Article
- SUMOylation of Csk Negatively Modulates its Tumor Suppressor Function.Neoplasia (New York, N.Y.) · 2019Article
- P-glycoprotein attenuates DNA repair activity in multidrug-resistant cells by acting through the Cbp-Csk-Src cascade.Oncotarget · 2017Article
- GRIM-19: A master regulator of cytokine induced tumor suppression, metastasis and energy metabolism.Cytokine & growth factor reviews · 2017Review
- PAG--a multipurpose transmembrane adaptor protein.Oncogene · 2014Review
- Functions of the FAK family kinases in T cells: beyond actin cytoskeletal rearrangement.Immunologic research · 2014Review
- GRIM-19 mutations fail to inhibit v-Src-induced oncogenesis.Oncogene · 2014Article
- Article
- Syndecan-1 regulates vascular smooth muscle cell phenotype.PloS one · 2014Article
- Article
- Differential polarization of C-terminal Src kinase between naive and antigen-experienced CD8+ T cells.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Expression of mutant α1 Na/K-ATPase defective in conformational transition attenuates Src-mediated signal transduction.The Journal of biological chemistry · 2013Article
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Csk (C-terminal Src kinase), a protein-tyrosine kinase, bearing the Src homology 2 and 3 (SH2 and SH3) domains, has been implicated in phosphorylation of c-Src Tyr-527, resulting in suppression of c-Src kinase activity. We found that mutations in the SH2 or SH3 domain of Csk, though they did not affect its kinase activity, resulted in a loss of suppression of c-Src activity in fibroblasts. In normal fibroblasts, tyrosine-phosphorylated paxillin and focal adhesion kinase pp125FAK, which colocalize at focal adhesion plaques, were the major proteins to which the Csk SH2 domain bound. Loss of binding to these proteins by the Csk SH2 mutants correlated with loss of the activity to suppress c-Src. Consistent with this observation, the levels of tyrosine phosphorylation of paxillin and pp125FAK were greatly reduced during mitosis, whereas the kinase activity of c-Src was elevated. We suggest that the SH2 domain is required for Csk to suppress c-Src, perhaps in combination with the SH3 domain, by anchoring Csk to a particular subcellular location where c-Src may exist. Our data also indicate that a certain fraction of the Csk and Src family kinases function at the focal adhesion plaques. The activity of the c-Src kinase localized at the focal adhesion plaques appears to be regulated by cell adhesion to the extracellular matrix.
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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.