ArticleMolecular and cellular biochemistry1996
Src homology domains of v-Src stabilize an active conformation of the tyrosine kinase catalytic domain.
Article in Molecular and cellular biochemistry, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 20 citations in OpenAlex.
- Encoding optical control in LCK kinase to quantitatively investigate its activity in live cells.Nature structural & molecular biology · 2017Article
- Theoretical Insights Reveal Novel Motions in Csk's SH3 Domain That Control Kinase Activation.PloS one · 2015Article
- Molecular mechanisms of SH2- and PTB-domain-containing proteins in receptor tyrosine kinase signaling.Cold Spring Harbor perspectives in biology · 2013Review
- The growing arsenal of ATP-competitive and allosteric inhibitors of BCR-ABL.Cancer research · 2012Review
- SH2 domains: modulators of nonreceptor tyrosine kinase activity.Current opinion in structural biology · 2009Review
- Phosphoprotein phosphatase-2A docks to Dishevelled and counterregulates Wnt3a/beta-catenin signaling.Journal of molecular signaling · 2007Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
To examine the interactions between Src homology domains and the tyrosine kinase catalytic domain of v-Src, various combinations of domains have been expressed in bacteria as fusion proteins. Constructs containing the isolated catalytic domain, SH2 + catalytic domain, and SH3 + SH2 + catalytic domains were active in autophosphorylation assays. For the catalytic domain of v-Src, but not for v-Abl, addition of exogenous Src SH3-SH2 domains stimulated the autophosphorylation activity. In contrast to results for autophosphorylation, constructs containing Src homology domains were more active towards a synthetic peptide substrate than the isolated catalytic domain. The ability of the SH2 and SH3 domains of v-Src to stabilize an active enzyme conformation was also confirmed by refolding after denaturation in guanidinium hydrochloride. Collectively the data suggest that, in addition to their roles in intermolecular protein-protein interactions, the Src homology regions of v-Src exert a positive influence on tyrosine kinase function, potentially by maintaining an active conformation of the catalytic domain.
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Registered trials
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