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

FEBS Letters

Schweiger, Anton¹  Eckerskorn, Christoph¹  Lottspeich, Friedrich¹  Jungbluth, Andreas¹  Stocker, Susanne¹  Gerisch, Günther¹ 

[1] Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany

关键词: Actin;    Tyrosine phosphorylation;    Dictyostelium;    Anoxia;   

DOI  :  10.1016/0014-5793(95)01165-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Cd²⁺ ions indicates that this modification of actin is implicated in the response of Dictyostelium cells to stress.

【 授权许可】

Unknown