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Phosphorylation of talin at tyrosine in Rous sarcoma virus-transformed cells

Journal Article · · Mol. Cell. Biol.; (United States)
DOI:https://doi.org/10.1128/MCB.7.1.371· OSTI ID:6523550
;
The cytoskeletal protein talin was found to undergo enhanced phosphorylation at tyrosine residues in chicken embryo fibroblasts following transformation by Rous sarcoma virus. An increase in the tyrosine phosphorylation of talin was also observed within 6 h in cells infected by the temperature-sensitive mutant tsNY68 after a shift from the nonpermissive to the permissive temperature. The overall extent of phosphorylation was 0.07 mol of phosphate per mol of talin and was not appreciably altered by transformation. In uninfected cells talin was shown to be phosphorylated at multiple sites by tryptic peptide mapping. Following transformation most of these sites remained phosphorylated, to the same or to a lesser extent, while novel, phosphotyrosine-containing phosphopeptides appeared. Talin was phosphorylated at tyrosine in cells infected by Rous sarcoma virus mutants which induce altered or partial transformation morphologies; thus the increased phosphorylation of talin at tyrosine occurred irrespective of the morphology induced. Transformation by Y73 also induced elevated levels of phosphotyrosine in talin, whereas transformation by the avian erythroblastosis and Fujinami sarcoma viruses did not.
Research Organization:
Univ. of California, Berkeley
OSTI ID:
6523550
Journal Information:
Mol. Cell. Biol.; (United States), Journal Name: Mol. Cell. Biol.; (United States) Vol. 1; ISSN MCEBD
Country of Publication:
United States
Language:
English

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Related Subjects

550401* -- Genetics-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACIDS
ANIMAL CELLS
ANIMALS
BIRDS
CARBOXYLIC ACIDS
CELL TRANSFORMATIONS
CHEMICAL REACTIONS
CHICKENS
CONNECTIVE TISSUE CELLS
ENZYMES
FIBROBLASTS
FOWL
HYDROLASES
HYDROXY ACIDS
ISOTOPE APPLICATIONS
LABELLED COMPOUNDS
MICROORGANISMS
MUTATIONS
ONCOGENIC TRANSFORMATIONS
ONCOGENIC VIRUSES
ORGANIC ACIDS
ORGANIC COMPOUNDS
PARASITES
PEPTIDE HYDROLASES
PHOSPHORUS COMPOUNDS
PHOSPHORYLATION
PROTEINS
SERINE PROTEINASES
SOMATIC CELLS
TRACER TECHNIQUES
TRYPSIN
TYROSINE
VERTEBRATES
VIRUSES