SH3 Domains Specifically Regulate Kinase Activity of Expressed Src Family Proteins (*)
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Summary
It is demonstrated that the regulation of Lyn is different than Src, and new evidence is provided that despite their homology, there are important functional differences between the SH3 domains of the various Src family members.
- Type
- article
- Published
- 1995-01-06
- Cited by
- 25
- References
- 51
- Access
- Open access
- OpenAlex
- https://openalex.org/W2011366314
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:30321958
Keywords
Proto-oncogene tyrosine-protein kinase Src, SH3 domain, Src family kinase, Cell biology, Kinase
References
- Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells.
- The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110.
- N‐terminal mutations activate the leukemogenic potential of the myristoylated form of c‐abl.
- Regulation of the enzymatic function of the lymphocyte-specific tyrosine protein kinase p56lck by the non-catalytic SH2 and SH3 domains.
- Peptides and Protein Phosphorylation
- Deletion of the SH3 domain of Src interferes with regulation by the phosphorylated carboxyl-terminal tyrosine.
- Csk inhibition of c‐Src activity requires both the SH2 and SH3 domains of Src.
- Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb/c 3T3 cells.
- Analysis of the catalytic domain of phosphotransferase activity of two avian sarcoma virus-transforming proteins.
- Site-directed mutagenesis of the SH2- and SH3-coding domains of c-src produces varied phenotypes, including oncogenic activation of p60c-src
- Deletions within the amino-terminal half of the c-src gene product that alter the functional activity of the protein
- Biological and biochemical properties of the c-src+ gene product overexpressed in chicken embryo fibroblasts
- Amino acid substitutions sufficient to convert the nontransforming p60c-src protein to a transforming protein
- A short sequence in the p60src N terminus is required for p60src myristylation and membrane association and for cell transformation
- Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src
- Overexpressed pp60c-src can induce focus formation without complete transformation of NIH 3T3 cells
- Evidence for regulation of the human ABL tyrosine kinase by a cellular inhibitor.
- Structural basis for the binding of proline-rich peptides to SH3 domains.
- The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
- Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
Cited by
- Angiogenesis and angiogenesis inhibition: an overview.
- Combination of Dasatinib and Dexamethasone targets the myeloma plasma cell through its interaction with the bone marrow microenvironment
- Isolation from spleen of a 57-kDa protein substrate of the tyrosine kinase Lyn. Identification as a protein related to protein disulfide-isomerase and localisation of the phosphorylation sites.
- Specific stimulation of c-Fgr kinase by tyrosine-phosphorylated (poly)peptides--possible implication in the sequential mode of protein phosphorylation.
- Flotillin-1 Regulates IgE Receptor-Mediated Signaling in Rat Basophilic Leukemia (RBL-2H3) Cells
- Pharmacological reactivity of neoplastic and non‐neoplastic associated neovasculature to vasoconstrictors
- Stac3 Is a Novel Regulator of Skeletal Muscle Development in Mice
- Involvement of the SH3 domain in Ca2+-mediated regulation of Src family kinases.
- Roles for SH2 and SH3 Domains in Lyn Kinase Association with Activated FcεRI in RBL Mast Cells Revealed by Patterned Surface Analysis
- Phosphatidylinositol(3, 4, 5) -Trisphosphate Stimulates Phosphorylation of Pleckstrin in Human Platelets (*)
- Comparison of SH3 and SH2 domain dynamics when expressed alone or in an SH(3+2) construct: the role of protein dynamics in functional regulation.
- The Lck SH3 Domain Is Required for Activation of the Mitogen-activated Protein Kinase Pathway but Not the Initiation of T-cell Antigen Receptor Signaling*
- Signalling by Src family kinases: lessons learnt from DNA tumour viruses.
- The catalytic activity of Src‐family tyrosine kinase is required for B cell antigen receptor signaling
- Modular peptide recognition domains in eukaryotic signaling.
- The phosphatidylinositol 3-kinase/Akt signaling pathway modulates the endocrine differentiation of trophoblast cells.
- Src regulated by C-terminal phosphorylation is monomeric.
- Directed Evolution of a Highly Specific FN3 Monobody to the SH3 Domain of Human Lyn Tyrosine Kinase
- The SLE variant Ala71Thr of BLK severely decreases protein abundance and binding to BANK1 through impairment of the SH3 domain function
- MOLECULAR ADAPTATION TO ANTI-CANCER CHEMOTHERAPY IN LEUKEMIA
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