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PMID: 6181509 Published · ppublish English Journal Article

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

Ito S, Richert N, Pastan I

Abstract

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.

MeSH Terms
Avian Sarcoma Viruses/enzymology Cell Transformation, Viral Enzyme Activation Magnesium/pharmacology Manganese/pharmacology Muscle Proteins/metabolism Phosphatidylinositols/pharmacology Phospholipids/pharmacology Phosphorylation Phosphotyrosine Protein Kinases/metabolism Substrate Specificity Tyrosine/analogs & derivatives,metabolism Vinculin
Chemicals
Muscle Proteins Phosphatidylinositols Phospholipids Vinculin Phosphotyrosine Tyrosine Manganese Protein Kinases Magnesium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Ito S
Richert N
Pastan I
References (29)
29 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1982-08-00
Pages
4628-31
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC346728
Subset
IM
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