ArticleCancer letters2007
Cooperative activation of Src family kinases by SH3 and SH2 ligands.
Article in Cancer letters, 2007. 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, 35 citations in OpenAlex.
- Fyn nanoclustering requires switching to an open conformation and is enhanced by FTLD-Tau biomolecular condensates.Molecular psychiatry · 2023Article
- IGF2BP1 is a targetable SRC/MAPK-dependent driver of invasive growth in ovarian cancer.RNA biology · 2021Article
- Myosin XVI in the Nervous System.Cells · 2020Review
- ST5 Positively Regulates Osteoclastogenesis via Src/Syk/calcium Signaling Pathways.Molecules and cells · 2019Article
- Article
- MUC1-mediated motility in breast cancer: a review highlighting the role of the MUC1/ICAM-1/Src signaling triad.Clinical & experimental metastasis · 2015Review
- A selective NMR probe to monitor the conformational transition from inactive to active kinase.ACS chemical biology · 2015Article
- SH2 Ligand-Like Effects of Second Cytosolic Domain of Na/K-ATPase α1 Subunit on Src Kinase.PloS one · 2015Article
- The SH3 regulatory domain of the hematopoietic cell kinase Hck binds ELMO via its polyproline motif.FEBS open bio · 2015Article
- SH2-catalytic domain linker heterogeneity influences allosteric coupling across the SFK family.Biochemistry · 2014Article
- Cellular settings mediating Src Substrate switching between focal adhesion kinase tyrosine 861 and CUB-domain-containing protein 1 (CDCP1) tyrosine 734.The Journal of biological chemistry · 2011Article
- Hematopoietic cell kinase associates with the 40S ribosomal subunit and mediates the ribotoxic stress response to deoxynivalenol in mononuclear phagocytes.Toxicological sciences : an official journal of the Society of Toxicology · 2010Article
- Toggle switches, pulses and oscillations are intrinsic properties of the Src activation/deactivation cycle.The FEBS journal · 2009Article
- The evolutionarily conserved arrangement of domains in SRC family kinases is important for substrate recognition.Biochemistry · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Src family nonreceptor tyrosine kinases are kept in a repressed state by intramolecular interactions involving the SH3 and SH2 domains of the enzymes. Ligands for these domains can displace the intramolecular associations and activate the kinases. Here, we carried out in vitro activation experiments with purified, down-regulated hematopoietic cell kinase (Hck), a Src family kinase. We show that SH3 and SH2 ligands act cooperatively to activate Src family kinases: the presence of one ligand lowers the concentration of the second ligand necessary for activation. To confirm the findings in intact cells, we studied Cas, a Src substrate that possesses SH2 and SH3 ligands. In contrast to wild-type Cas, mutant forms of Cas lacking the SH3 or SH2 ligands were unable to stimulate Src autophosphorylation when expressed in Cas-deficient fibroblasts. Cells expressing the Cas mutants also showed decreased amounts of activated Src at focal adhesions. The results suggest that proteins containing ligands for both SH3 and SH2 domains can produce a synergistic activation of Src family kinases.
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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.