Document Detail


Stress-activated kinases regulate protein stability.
MedLine Citation:
PMID:  9779995     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Proteasome inhibitors have been used to demonstrate that many proteins of the signal transduction pathways are regulated by degradation via the ubiquitin-proteasome pathway. The key question is what events target specific proteins for ubiquitination at one time and prevent ubiquitination at other times? In this review, we develop the notion that there is a direct relationship between the phosphorylation/dephosphorylation cascade of the signal transduction pathways and the targeting of the regulatory proteins for ubiquitination. We present examples where phosphorylation appears to alter the interaction between the targeting systems and the substrate by modifying the targeting system, the substrate, or both. These interacting systems are seen in the response of p53, c-jun and ATF-2 in cells subjected to stress or DNA damage and to the normal regulated response in a variety of pathways including the IkappaB-NFkappaB and JAK-STAT pathways. The interweaving of the two post-translational networks, phosphorylation and ubiquitination, provides a powerful insight into global regulatory control pathways.
Authors:
S Y Fuchs; V A Fried; Z Ronai
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Publication Detail:
Type:  Journal Article; Review    
Journal Detail:
Title:  Oncogene     Volume:  17     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  1998 Sep 
Date Detail:
Created Date:  1998-11-23     Completed Date:  1998-11-23     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  1483-90     Citation Subset:  IM    
Affiliation:
The Ruttenberg Cancer Center, Mount Sinai Medical School, New York, New York 10029, USA.
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MeSH Terms
Descriptor/Qualifier:
Animals
Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
Cytoskeletal Proteins / metabolism*
DNA-Binding Proteins / metabolism
Glycogen Synthase Kinase 3
Humans
I-kappa B Kinase
JNK Mitogen-Activated Protein Kinases
Janus Kinase 3
Mitogen-Activated Protein Kinases*
NF-kappa B / metabolism
Protein Kinase C / metabolism
Protein-Serine-Threonine Kinases / metabolism*
Protein-Tyrosine Kinases / metabolism
Proteins / metabolism*
STAT1 Transcription Factor
Stress, Physiological*
Trans-Activators / metabolism
beta Catenin
Chemical
Reg. No./Substance:
0/CTNNB1 protein, human; 0/Cytoskeletal Proteins; 0/DNA-Binding Proteins; 0/JAK3 protein, human; 0/NF-kappa B; 0/Proteins; 0/STAT1 Transcription Factor; 0/STAT1 protein, human; 0/Trans-Activators; 0/beta Catenin; EC 2.7.1.-/IKBKE protein, human; EC 2.7.10.1/Janus Kinase 3; EC 2.7.10.1/Protein-Tyrosine Kinases; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.10/CHUK protein, human; EC 2.7.11.10/I-kappa B Kinase; EC 2.7.11.10/IKBKB protein, human; EC 2.7.11.13/Protein Kinase C; EC 2.7.11.17/Calcium-Calmodulin-Dependent Protein Kinases; EC 2.7.11.24/JNK Mitogen-Activated Protein Kinases; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 2.7.11.26/Glycogen Synthase Kinase 3

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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