Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases

Bogoyevitch, Marie A. and Kobe, Bostjan (2006) Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases. Microbiology and Molecular Biology Reviews, 70 4: 1061-1095. doi:10.1128/MMBR.00025-06

Attached Files (Some files may be inaccessible until you login with your UQ eSpace credentials)
Name Description MIMEType Size Downloads
UQ81879_OA.pdf Full text (open access) application/pdf 1.05MB 0

Author Bogoyevitch, Marie A.
Kobe, Bostjan
Title Uses for JNK: the many and varied substrates of the c-Jun N-terminal kinases
Journal name Microbiology and Molecular Biology Reviews   Check publisher's open access policy
ISSN 1092-2172
Publication date 2006-12
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1128/MMBR.00025-06
Open Access Status File (Publisher version)
Volume 70
Issue 4
Start page 1061
End page 1095
Total pages 35
Place of publication Washington, DC, United States
Publisher American Society for Microbiology
Collection year 2006
Language eng
Abstract The c-Jun N-terminal kinases (JNKs) are members of a larger group of serine/ threonine (Ser/Thr) protein kinases from the mitogen-activated protein kinase family. JNKs were originally identified as stress-activated protein kinases in the livers of cycloheximide-challenged rats. Their subsequent purification, cloning, and naming as JNKs have emphasized their ability to phosphorylate and activate the transcription factor c-Jun. Studies of c-Jun and related transcription factor substrates have provided clues about both the preferred substrate phosphorylation sequences and additional docking domains recognized by JNK There are now more than 50 proteins shown to be substrates for JNK These include a range of nuclear substrates, including transcription factors and nuclear hormone receptors, heterogeneous nuclear ribonucleoprotein K and the Pol I-specific transcription factor TIF-IA, which regulates ribosome synthesis. Many nonnuclear substrates have also been characterized, and these are involved in protein degradation (e.g., the E3 ligase Itch), signal transduction (e.g., adaptor and scaffold proteins and protein kinases), apoptotic cell death (e.g., mitochondrial Bcl2 family members), and cell movement (e.g., paxillin, DCX, microtubule-associated proteins, the stathmin family member SCG10, and the intermediate filament protein keratin 8). The range of JNK actions in the cell is therefore likely to be complex. Further characterization of the substrates of JNK should provide clearer explanations of the intracellular actions of the JNKs and may allow new avenues for targeting the JNK pathways with therapeutic agents downstream of JNK itself.
Keyword Activated-protein-kinase
Insulin-receptor Substrate-1
Signal-transduction Pathway
Microtubule-associated Protein-2
Ubiquitin Ligase Itch
Kappa-b Activation
Atf2 Transcription Factor
Cyclin-dependent Kinases
Q-Index Code C1
Additional Notes This document is a journal review. ____________________ DOI 10.1128/MMBR.00025-06

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Excellence in Research Australia (ERA) - Collection
2007 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 261 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 286 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Wed, 15 Aug 2007, 10:01:07 EST