NDLI: MEKK1/JNK signaling stabilizes and activates p53.

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MEKK1/JNK signaling stabilizes and activates p53.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Adler, V. Pincus, M. R. Ronai, Z. Fuchs, S. Y.
Description	Author Affiliation: Fuchs SY ( Ruttenberg Cancer Center, Mount Sinai School of Medicine, New York, NY 10029, USA.);
Abstract	Activation of the tumor suppressor p53 by stress and damage stimuli often correlates with induction of stress kinases, Jun-NH2 kinase (JNK). As JNK association with p53 plays an important role in p53 stability, in the present study we have elucidated the relationship between the JNK-signaling pathway and p53 stability and activity. Expression of a constitutively active form of JNKK upstream kinase, mitogen-activated protein kinase kinase kinase (DeltaMEKK1), increased the level of the exogenously transfected form of p53 in p53 null (10.1) cells as well as of endogenous p53 in MCF7 breast cancer cells. Increased p53 level by forced expression of DeltaMEKK1 coincided with a decrease in p53 ubiquitination in vivo and with prolonged p53 half-life. Computerized modeling of the JNK-binding site (amino acids 97-116; p7 region) enabled us to design mutations of exposed residues within this region. Respective mutations (p53(101-5-8)) and deletion (p53(Deltap7)) forms of p53 did not exhibit the same increase in p53 levels upon DeltaMEKK1 expression. In vitro phosphorylation of p53 by JNK abolished Mdm2 binding and targeting of p53 ubiquitination. Similarly, DeltaMEKK1 expression increased p53 phosphorylation by immunopurified JNK and dissociated p53-Mdm2 complexes. Transcriptional activity of p53, as measured via mdm2 promoter-driven luciferase, exhibited a substantial increase in DeltaMEKK1-expressing cells. Cotransfection of p53 and DeltaMEKK1 into p53 null cells potentiated p53-dependent apoptosis, suggesting that MEKK1 effectors contribute to the ability of p53 to mediate programmed cell death. Our results point to the role of MEKK1-JNK signaling in p53 stability, transcriptional activities, and apoptotic capacity as part of the cellular response to stress.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	MAP Kinase Kinase Kinase 1 Nuclear Proteins Protein-Serine-Threonine Kinases Metabolism Signal Transduction Tumor Suppressor Protein P53 Apoptosis Cell Line, Transformed Cells, Cultured Computer Simulation Phosphorylation Proto-Oncogene Proteins Proto-Oncogene Proteins C-mdm2 Transcriptional Activation Ubiquitins Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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