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Stress‐induced tyrosine phosphorylation of actin in Dictyostelium cells and localization of the phosphorylation site to tyrosine‐53 adjacent to the DNase I binding loop
Author(s) -
Jungbluth Andreas,
Eckerskorn Christoph,
Gerisch Günther,
Lottspeich Friedrich,
Stocker Susanne,
Schweiger Anton
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01165-b
Subject(s) - tyrosine , phosphorylation , tyrosine phosphorylation , actin , actin binding protein , biochemistry , biology , protein tyrosine phosphatase , actin remodeling , serine , chemistry , microbiology and biotechnology , actin cytoskeleton , cytoskeleton , cell
Actin is known to be phosphorylated at tyrosine, serine, or threonine residues in various cells. In cells of Dictyostelium discoideum , a rise in the tyrosine phosphorylation of actin is observed in response to ATP depletion. An actin fraction rich in phosphotyrosine was obtained by chromatography on the weak anion exchanger Mono‐P. Mass spectrometry and amino acid sequencing of protease cleavage products indicated that a single tyrosine residue was phosphorylated. Localization of this residue to position 53 of the actin sequence attributed the modification to a site that is critical for the capability of actin to polymerize. Induction of the tyrosine phosphorylation by heat shock and Cd 2+ ions indicates that this modification of actin is implicated in the response of Dictyostelium cells to stress.