Phospholipids stimulate phosphorylation of vinculin by the tyrosine-specific protein kinase of Rous sarcoma virus. | Zendy

Seiji Ito | Zendy; Nancy Richert | Zendy; Ira Pastan | Zendy

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Phospholipids stimulate phosphorylation of vinculin by the tyrosine-specific protein kinase of Rous sarcoma virus.

Author(s) -

Seiji Ito,

Nancy Richert,

Ira Pastan

Publication year - 1982

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.79.15.4628

Subject(s) - phosphatidylinositol , phosphatidic acid , vinculin , rous sarcoma virus , phosphorylation , biochemistry , phosphatidylserine , diacylglycerol kinase , tyrosine phosphorylation , biology , phospholipid , dephosphorylation , chemistry , microbiology and biotechnology , phosphatase , protein kinase c , membrane , gene , focal adhesion

The phosphorylation of vinculin by a highly purified tyrosine-specific protein kinase was enhanced more than 10-fold by anionic phospholipids: the phosphorylation of casein, actin, and alpha-actinin was inhibited. The effect of phospholipid was dependent on the divalent cation used. Stimulation was observed by phosphatidylinositol or phosphatidylglycerol in the presence of either 0.5 mM Mn2+ of 5 mM Mg2+; with either phospholipid, more enzyme activity was observed with Mn2+. Maximal stimulation by phosphatidylinositol was observed at about 400 micrograms/ml. In contrast, marked stimulation by phosphatidylserine was observed only with Mn2+ and marked stimulation by phosphatidic acid was observed only with Mg2+. These results raise the possibility that phospholipids modulate vinculin phosphorylation in Rous sarcoma virus-transformed cells.

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