Biology:MAPK3
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Mitogen-activated protein kinase 3, also known as p44MAPK and ERK1,[1] is an enzyme that in humans is encoded by the MAPK3 gene.[2]
Function
The protein encoded by this gene is a member of the mitogen-activated protein kinase (MAP kinase) family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.[3]
Clinical significance
It has been suggested that MAPK3, along with the gene IRAK1, is turned off by two microRNAs that were activated after the influenza A virus had been made to infect human lung cells.[4]
Signaling pathways
Pharmacological inhibition of ERK1/2 restores GSK3β activity and protein synthesis levels in a model of tuberous sclerosis.[5]
Interactions
MAPK3 has been shown to interact with:
- DUSP3,[6]
- DUSP6[7]
- GTF2I,[8]
- HDAC4,[9]
- MAP2K1,[10][11][12][13][14]
- MAP2K2,[10][11][14]
- PTPN7,[15][16][17]
- RPS6KA2,[18][19] and
- SPIB.[20]
References
- ↑ Thomas, Gareth M.; Huganir, Richard L. (1 March 2004). "MAPK cascade signalling and synaptic plasticity". Nature Reviews Neuroscience 5 (3): 173–183. doi:10.1038/nrn1346. ISSN 1471-003X. PMID 14976517.
- ↑ "Molecular cloning and characterization of the human p44 mitogen-activated protein kinase gene". Genomics 50 (1): 69–78. 15 May 1998. doi:10.1006/geno.1998.5315. PMID 9628824.
- ↑ "Entrez Gene: MAPK3 mitogen-activated protein kinase 3". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5595.
- ↑ "Influenza A virus infection of human respiratory cells induces primary microRNA expression". J. Biol. Chem. 287 (37): 31027–40. 2012. doi:10.1074/jbc.M112.387670. PMID 22822053.
- ↑ "Inhibition of ERK1/2 Restores GSK3β Activity and Protein Synthesis Levels in a Model of Tuberous Sclerosis". Sci. Rep. 7 (1): 4174. 2017. doi:10.1038/s41598-017-04528-5. PMID 28646232. Bibcode: 2017NatSR...7.4174P.
- ↑ "Extracellular regulated kinases (ERK) 1 and ERK2 are authentic substrates for the dual-specificity protein-tyrosine phosphatase VHR. A novel role in down-regulating the ERK pathway". J. Biol. Chem. 274 (19): 13271–80. May 1999. doi:10.1074/jbc.274.19.13271. PMID 10224087.
- ↑ "The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity". J. Biol. Chem. 273 (15): 9323–9. April 1998. doi:10.1074/jbc.273.15.9323. PMID 9535927.
- ↑ "Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter". Mol. Cell. Biol. 20 (4): 1140–8. February 2000. doi:10.1128/mcb.20.4.1140-1148.2000. PMID 10648599.
- ↑ "Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras". Proc. Natl. Acad. Sci. U.S.A. 97 (26): 14329–33. December 2000. doi:10.1073/pnas.250494697. PMID 11114188. Bibcode: 2000PNAS...9714329Z.
- ↑ 10.0 10.1 "Actin-binding protein-280 binds the stress-activated protein kinase (SAPK) activator SEK-1 and is required for tumor necrosis factor-alpha activation of SAPK in melanoma cells". J. Biol. Chem. 272 (5): 2620–8. January 1997. doi:10.1074/jbc.272.5.2620. PMID 9006895.
- ↑ 11.0 11.1 "Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2". J. Biol. Chem. 271 (8): 4230–5. February 1996. doi:10.1074/jbc.271.8.4230. PMID 8626767.
- ↑ "Routing MAP kinase cascades". Science 281 (5383): 1625–6. September 1998. doi:10.1126/science.281.5383.1625. PMID 9767029.
- ↑ "ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK". J. Biol. Chem. 275 (21): 15799–808. May 2000. doi:10.1074/jbc.M910060199. PMID 10748187.
- ↑ 14.0 14.1 "Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases". J. Biol. Chem. 268 (32): 23933–9. November 1993. doi:10.1016/S0021-9258(20)80474-8. PMID 8226933.
- ↑ "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". Oncogene 19 (7): 858–69. February 2000. doi:10.1038/sj.onc.1203408. PMID 10702794.
- ↑ "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase". Nat. Cell Biol. 1 (5): 305–11. September 1999. doi:10.1038/13024. PMID 10559944.
- ↑ "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)". J. Biol. Chem. 274 (17): 11693–700. April 1999. doi:10.1074/jbc.274.17.11693. PMID 10206983.
- ↑ "Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity". Mol. Cell. Biol. 23 (14): 4796–804. July 2003. doi:10.1128/mcb.23.14.4796-4804.2003. PMID 12832467.
- ↑ "Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases". J. Biol. Chem. 271 (47): 29773–9. November 1996. doi:10.1074/jbc.271.47.29773. PMID 8939914.
- ↑ "Differential phosphorylations of Spi-B and Spi-1 transcription factors". Oncogene 12 (4): 863–73. February 1996. PMID 8632909.
Further reading
- "Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway". J. Neurovirol. 8 Suppl 2 (2): 91–6. 2002. doi:10.1080/13550280290167885. PMID 12491158.
- "The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition". Oncogene 26 (22): 3227–39. 2007. doi:10.1038/sj.onc.1210414. PMID 17496918.
- "Modulatory Actions of Neuropeptide y on Prostate Cancer Growth: Role of MAP Kinase/ERK 1/2 Activatio", Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation, Advances In Experimental Medicine And Biology, 604, Springer, 2007, pp. 96–100, doi:10.1007/978-0-387-69116-9_7, ISBN 978-0-387-69114-5, PMID 17695723, https://archive.org/details/advancesinmolecu00inte/page/96
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