Mutations in the non-catalytic domains of Fyn and Fgr tyrosine kinases reveal differences in mechanisms of their regulation.
Non-catalytic domains of tyrosine kinases from the Src family are believed to be regulated intra- and intermolecularly through protein-protein interactions. We have deleted the SH2 and SH3 domains from Fyn and Fgr and have generated two point mutations in residues completely conserved in all members of the Src family. The dramatically different biological effects of these mutations suggest that non-catalytic domains regulate Src family kinase activities through distinctly different mechanisms.
Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, Maryland 20892-4330, USA.
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Rivero-Lezcano
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Marcilla
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Robbins
D016475:3T3 Cells; D000818:Animals; D002471:Cell Transformation, Neoplastic; D051379:Mice; D017354:Point Mutation; D011505:Protein-Tyrosine Kinases / Q000502:physiology*; D011518:Proto-Oncogene Proteins / Q000737:chemistry / Q000502:physiology*; D051076:Proto-Oncogene Proteins c-fyn; D013329:Structure-Activity Relationship; D018909:src Homology Domains; D019061:src-Family Kinases
D011518:Proto-Oncogene Proteins; D011505:Protein-Tyrosine Kinases; C494960:Fyn protein, mouse; D051076:Proto-Oncogene Proteins c-fyn; C053102:proto-oncogene proteins c-fgr; D019061:src-Family Kinases