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 Previous Article

Microbiology and Molecular Biology Reviews, December 2006, p. 1061-1095, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00025-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Uses for JNK: the Many and Varied Substrates of the c-Jun N-Terminal Kinases

Marie A. Bogoyevitch1* and Bostjan Kobe2

Cell Signalling Laboratory, Biochemistry and Molecular Biology, School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, Crawley, Australia,1 School of Molecular and Microbial Sciences, Institute for Molecular Bioscience and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Australia2

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.

* Corresponding author. Mailing address: Cell Signalling Laboratory, Biochemistry and Molecular Biology (M310), School of Biomedical, Biomolecular and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Crawley, Western Australia 6009, Australia. Phone: 61 8 6488 1348. Fax: 61 8 6488 1148. E-mail: marieb{at}cyllene.uwa.edu.au.

Microbiology and Molecular Biology Reviews, December 2006, p. 1061-1095, Vol. 70, No. 4
1092-2172/06/$08.00+0     doi:10.1128/MMBR.00025-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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