NDLI: Complexes of p21RAS with JUN N-terminal kinase and JUN proteins.

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Complexes of p21RAS with JUN N-terminal kinase and JUN proteins.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Brandt-rauf, P. W. Adler, V. Pincus, M. R. Ronai, Z.
Description	Author Affiliation: Adler V ( Molecular Carcinogenesis Program, American Health Foundation, Valhalla, NY 10595, USA.);
Abstract	RAS gene-encoded p21 protein has been found to increase in vitro phosphorylation of JUN via its kinase, JUN N-terminal kinase (JNK). This effect is mediated by increased phosphorylation of JNK in the presence of wild-type and oncogenic (Val-12) p21 protein in a dose-dependent manner. Oncogenic p21 protein is more potent in mediating this effect than its normal counterpart. Both normal and oncogenic p21 proteins bind to purified JNK and to JNK that is present in cell extracts from transformed fibroblasts and melanoma cells. Oncogenic and normal p21 proteins have also been found to bind to bacterially expressed JUN protein. This binding is dose dependent, enhanced by the presence of GTP, and depends on the presence of the first 89 amino acids of JUN (the delta domain), as it does not occur with v-jun. While the ability of both normal and oncogenic p21 proteins to bind JNK is strongly inhibited by a p21 peptide corresponding to aa 96-110, and more weakly inhibited by the p21 peptide corresponding to aa 115-126, p21-JUN interaction is inhibited by peptides corresponding to aa 96-110 and, to a lesser degree, by peptides corresponding to aa 35-47. The results suggest that the p21 protein interacts specifically with both JNK and JUN proteins.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Calcium-Calmodulin-Dependent Protein Kinases Metabolism Mitogen-Activated Protein Kinases Proto-Oncogene Proteins C-jun Ras Proteins 3T3 Cells Animals Binding Sites Blotting, Western Genetics JNK Mitogen-Activated Protein Kinases Mice Phosphorylation Protein Binding Recombinant Fusion Proteins Subcellular Fractions Tumor Cells, Cultured Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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