The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
Diverse physiological functions for dual-specificity MAP kinase phosphatases
Open accessAbstract
A structurally distinct subfamily of ten dual-specificity (Thr/Tyr) protein phosphatases is responsible for the regulated dephosphorylation and inactivation of mitogen-activated protein kinase (MAPK) family members in mammals. These MAPK phosphatases (MKPs) interact specifically with their substrates through a modular kinase-interaction motif (KIM) located within the N-terminal non-catalytic domain of the protein. In addition, MAPK binding is often accompanied by enzymatic activation of the C-terminal catalytic domain, thus ensuring specificity of action. Despite our knowledge of the biochemical and structural basis for the catalytic mechanism of the MKPs, we know much less about their regulation and physiological functions in mammalian cells and tissues. However, recent studies employing a range of model systems have begun to reveal essential non-redundant roles for the MKPs in determining the outcome of MAPK signalling in a variety of physiological contexts. These include development, immune system function, metabolic homeostasis and the regulation of cellular stress responses. Interestingly, these functions may reflect both restricted subcellular MKP activity and changes in the levels of signalling through multiple MAPK pathways.
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Citations
Cites
Mammalian MAP kinase signalling cascades
Chang, L., & Karin, M. (2001) · Nature · doi:10.1038/35065000 · Cited by 5,111
Mitogen-Activated Protein Kinase Pathways Mediated by ERK, JNK, and p38 Protein Kinases
Johnson, G. L., & Lapadat, R. (2002) · Science · doi:10.1126/science.1072682 · Cited by 4,295
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
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A central role for JNK in obesity and insulin resistance
Hirosumi, J., Tuncman, G., Chang, L., Görgün, C. Z., Uysal, K. T., Maeda, K., Karin, M., & Hotamisligil, G. S. (2002) · Nature · doi:10.1038/nature01137 · Cited by 3,359
Protein Tyrosine Phosphatases in the Human Genome
Alonso, A., Sasin, J., Bottini, N., Friedberg, I., Friedberg, I., Osterman, A., Godzik, A., Hunter, T., Dixon, J., & Mustelin, T. (2004) · Cell · doi:10.1016/j.cell.2004.05.018 · Cited by 1,886
Mitogen-activated protein kinases in apoptosis regulation
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“Introduction Mitogen-activated protein kinases (MAPKs) constitute a conserved family of enzymes that regulate a large number of physiological processes, including proliferation, differentiation, development, immune function, stress responses and apoptosis (Chang and Karin, 2001; Davis, 2000; Johnson and Lapadat, 2002;…”
BackgroundOrganization and regulation of mitogen-activated protein kinase signaling pathways
Garrington, T. P., & Johnson, G. L. (1999) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(99)80028-3 · Cited by 1,275
MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
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Cited by
Dual-specificity phosphatases: critical regulators with diverse cellular targets
Patterson, K. I., Brummer, T., O'brien, P. M., & Daly, R. J. (2009) · Biochemical Journal · doi:10.1042/bj20082234 · Cited by 744
Dual‐specificity MAP kinase phosphatases (MKPs): Shaping the outcome of MAP kinase signalling
Caunt, C. J., & Keyse, S. M. (2013) · The FEBS Journal · doi:10.1111/j.1742-4658.2012.08716.x · Cited by 535
Self-citationBeck, I. M. E., Vanden Berghe, W., Vermeulen, L., Yamamoto, K. R., Haegeman, G., & De Bosscher, K. (2009) · Endocrine Reviews · doi:10.1210/er.2009-0013 · Cited by 298
Protein tyrosine phosphatase function: the substrate perspective
Tiganis, T., & Bennett, A. M. (2007) · Biochemical Journal · doi:10.1042/bj20061548 · Cited by 297
Vandevyver, S., Dejager, L., Tuckermann, J., & Libert, C. (2013) · Endocrinology · doi:10.1210/en.2012-2045 · Cited by 296
Metadata
- Authors
- Dickinson, R. J., & Keyse, S. M.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2006-11-15
- Volume
- 119
- Issue
- 22
- Pages
- 4607-4615
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W2107149701
- Cited by
- 329
- References
- 76
- FWCI
- 8.60
- Type
- journal article
- Language
- en
- Open access
- green
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