ArticleOncogene2005
Transactivation of Abl by the Crk II adapter protein requires a PNAY sequence in the Crk C-terminal SH3 domain.
Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 31 citations in OpenAlex.
- CrkII/Abl phosphorylation cascade is critical for NLRC4 inflammasome activity and is blocked by Pseudomonas aeruginosa ExoT.Nature communications · 2022Article
- Article
- Kinetic Insights into the Binding between the nSH3 Domain of CrkII and Proline-Rich Motifs in cAbl.Biophysical journal · 2016Article
- Cyclophilin A promotes cell migration via the Abl-Crk signaling pathway.Nature chemical biology · 2016Article
- Article
- SH3 domains: modules of protein-protein interactions.Biophysical reviews · 2013Review
- Models of crk adaptor proteins in cancer.Genes & cancer · 2012Article
- Roles for crk in cancer metastasis and invasion.Genes & cancer · 2012Article
- Phosphorylation of Crk on tyrosine 251 in the RT loop of the SH3C domain promotes Abl kinase transactivation.Oncogene · 2011Article
- Structural basis for regulation of the Crk signaling protein by a proline switch.Nature chemical biology · 2011Article
- Emerging roles for crk in human cancer.Genes & cancer · 2010Article
- ABL tyrosine kinases: evolution of function, regulation, and specificity.Science signaling · 2010Review
- Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts.Journal of cell science · 2009Article
- A proposed syntax for Minimotif Semantics, version 1.BMC genomics · 2009Article
- Crk and CrkL adaptor proteins: networks for physiological and pathological signaling.Cell communication and signaling : CCS · 2009Article
- Proline cis-trans isomerization controls autoinhibition of a signaling protein.Molecular cell · 2007Article
- Cardiovascular and craniofacial defects in Crk-null mice.Molecular and cellular biology · 2006Article
- Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II.Biochemistry · 2006Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
To gain a better understanding of how Crk II regulates the function of the Abl tyrosine kinase, we explored the function of the C-terminal linker and SH3 domain, a region of Crk II that is still poorly understood. Molecular modeling, tryptophan fluorescence, and covariation sequence alignment indicate that the Crk-SH3-C has a unique binding groove and RT loop not observed in typical SH3 domains. Based on these models, we made a series of mutations in the linker and in residues predicted to destabilize the putative binding pocket and RT loop. In Abl transactivation assays, Y222F and P225A mutations in the linker resulted in strong transactivation of Abl by Crk II. However, mutations predicted to be at the surface of the Crk SH3-C were not activators of Abl. Interestingly, combinations of activating mutations of Crk II with mutations in the highly conserved PNAY sequence in the SH3-C inactivated the activating mutations, suggesting that the SH3-C is necessary for activation. Our data provide insight into the role of highly conserved residues in the Crk-SH3-C, suggesting a mechanism for how the linker and the Crk-SH3-C function in the transactivation of the Abl tyrosine kinase.
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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.