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- W2896982772 abstract "The mode of regulation of Src kinases has been elucidated by crystallographic studies identifying conserved structured protein modules involved in an orderly set of intramolecular associations and ligand interactions. Despite these detailed insights, much of the complex behavior and diversity in the Src family remains unexplained. A key missing piece is the function of the unstructured N-terminal region. We report here the function of the N-terminal region in binding within a hydrophobic pocket in the kinase domain of a dimerization partner. Dimerization substantially enhances autophosphorylation and phosphorylation of selected substrates, and interfering with dimerization is disruptive to these functions. Dimerization and Y419 phosphorylation are codependent events creating a bistable switch. Given the versatility inherent in this intrinsically disordered region, its multisite phosphorylations, and its divergence within the family, the unique domain likely functions as a central signaling hub overseeing much of the activities and unique functions of Src family kinases." @default.
- W2896982772 created "2018-10-26" @default.
- W2896982772 creator A5006839105 @default.
- W2896982772 creator A5030082572 @default.
- W2896982772 creator A5046122480 @default.
- W2896982772 creator A5068783039 @default.
- W2896982772 date "2018-10-01" @default.
- W2896982772 modified "2023-10-06" @default.
- W2896982772 title "A Dimerization Function in the Intrinsically Disordered N-Terminal Region of Src" @default.
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- W2896982772 doi "https://doi.org/10.1016/j.celrep.2018.09.035" @default.
- W2896982772 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6226010" @default.
- W2896982772 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30304684" @default.
- W2896982772 hasPublicationYear "2018" @default.
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