The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Regulation of Mitogen-Activated Protein Kinase Signaling Networks by G Protein-Coupled Receptors
Abstract
The family of receptors that transmit signals through the activation of heterotrimeric GTP-binding proteins (G proteins) constitutes the largest group of cell surface proteins involved in signal transduction. These receptors participate in a broad range of important biological functions and are implicated in a number of disease states. More than half of all drugs currently available influence G protein-coupled receptors (GPCRs). These receptors affect the generation of small molecules that act as intracellular mediators or second messengers, and can regulate a highly interconnected network of biochemical routes controlling the activity of several members of the mitogen-activated protein kinase (MAPK) superfamily. They include extracellular signal-regulated kinase 1 (ERK1) and ERK2 (or p44 MAPK and p42 MAPK ), c-Jun NH 2 -terminal kinases (JNKs), ERK5 (or BMK), and p38 MAPKs, including p38α (or CSBP-1), p38β, p38γ (or SAPK3 or ERK6), and p38δ?(or SAPK4). This review will focus on the molecular mechanisms by which GPCRs signal to the nucleus through this intricate network of second messenger-generating systems and MAPK signaling pathways, thereby affecting the expression of genes whose products influence many biological processes, including normal and aberrant cell growth.
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Cites
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Regulation of Phosphoinositide-specific Phospholipase C Isozymes
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Gutkind, J. S. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.4.1839 · Cited by 812
Self-citationA Cytoplasmic Inhibitor of the JNK Signal Transduction Pathway
Dickens, M., Rogers, J. S., Cavanagh, J., Raitano, A., Xia, Z., Halpern, J. R., Greenberg, M. E., Sawyers, C. L., & Davis, R. J. (1997) · Science · doi:10.1126/science.277.5326.693 · Cited by 675
A Mammalian Scaffold Complex That Selectively Mediates MAP Kinase Activation
Whitmarsh, A. J., Cavanagh, J., Tournier, C., Yasuda, J., & Davis, R. J. (1998) · Science · doi:10.1126/science.281.5383.1671 · Cited by 652 · cited 1×
“For the JNK pathway, two proteins, JIP (JNK inhibitory protein) and JSAP (a novel JNK inhibitory protein), perform this function, bridging together MLKs, MKK7, and JNK (214, 215), and MEKK1, SEK (stress-activated protein kinase kinase or ERK kinase), and JNK (216), respectively.”
BackgroundNuclear Accumulation of NFAT4 Opposed by the JNK Signal Transduction Pathway
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Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
González-Maeso, J., Weisstaub, N. V., Zhou, M., Chan, P., Ivic, L., Ang, R., Lira, A., Bradley-Moore, M., Ge, Y., Zhou, Q., et al. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.008 · Cited by 925
Dynorphin, stress, and depression
Knoll, A. T., & Carlezon, W. A. (2010) · Brain Research · doi:10.1016/j.brainres.2009.09.074 · Cited by 465
Desale, S. E., Chidambaram, H., & Chinnathambi, S. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00036-1 · Cited by 99
Intracellular signaling mechanisms of the melanocortin receptors: current state of the art
Rodrigues, A. R., Almeida, H., & Gouveia, A. M. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1800-3 · Cited by 64
Metadata
- Authors
- Gutkind, J. S.
- Venue
- Science's STKE
- Published
- 2000-07-11
- Volume
- 2000
- Issue
- 40
- Pages
- re1-re1
- ISSN
- 1525-8882 (ISSN-L)
- OpenAlex
- W2140975775
- Cited by
- 264
- References
- 9
- FWCI
- 6.53
- Type
- journal article
- Language
- en
- Open access
- closed
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