PMID: 9168470May 1, 1997Paper

pp60v-src transformation of rat cells but not chicken cells strongly correlates with low-affinity phosphopeptide binding by the SH2 domain

Molecular Biology of the Cell
M F Verderame

Abstract

Substrates critical for transformation by pp60v-src remain unknown, as does the precise role of the src homology 2 (SH2) domain in this process. To continue exploring the role of the SH2 domain in pp60v-src-mediated transformation, site-directed mutagenesis was used to create mutant v-src alleles predicted to encode proteins with overall structural integrity intact but with reduced ability to bind phosphotyrosine-containing peptides. Arginine-175, which makes critical contacts in the phosphotyrosine-binding pocket, was mutated to lysine or alanine. Unexpectedly, both mutations created v-src alleles that transform chicken cells with wild-type (wt) efficiency and are reduced for transformation of rat cells; these alleles are host dependent for transformation. Additionally, these alleles resulted in a round morphological transformation of chicken cells, unlike 12 of the 13 known host-dependent src SH2 mutations that result in a fusiform morphology. Analysis of phosphopeptide binding by the mutant SH2 domains reveal that the in vitro ability to bind phosphopeptides known to have a high affinity for wt src SH2 correlates with wt (round) morphological transformation in chicken cells and in vitro ability to bind phosphopeptides known ...Continue Reading

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Citations

Jul 1, 1997·Molecular Biology of the Cell·M Tian, G S Martin
Apr 5, 2008·PLoS Computational Biology·Ignacio E SánchezLuis Serrano
Jan 5, 2011·The FEBS Journal·Bradley R GrovemanXian-Min Yu
Mar 25, 2021·Cell Reports·Makio HiguchiNaoki Watanabe

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