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词条 MAPK3
释义

  1. Function

  2. Clinical significance

  3. Signaling pathways

  4. Interactions

  5. References

  6. Further reading

  7. External links

{{main|Extracellular signal-regulated kinases}}{{Infobox_gene}}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:

{{div col|colwidth=20em}}
  • 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]
{{Div col end}}{{Clear}}

References

1. ^{{Cite journal|last=Thomas|first=Gareth M.|last2=Huganir|first2=Richard L.|date=1 March 2004|title=MAPK cascade signalling and synaptic plasticity|journal=Nature Reviews Neuroscience|volume=5|issue=3|pages=173–183|doi=10.1038/nrn1346|pmid=14976517|issn=1471-003X}}
2. ^{{cite journal | vauthors = García F, Zalba G, Páez G, Encío I, de Miguel C | title = Molecular cloning and characterization of the human p44 mitogen-activated protein kinase gene | journal = Genomics | volume = 50 | issue = 1 | pages = 69–78 | date = 15 May 1998 | pmid = 9628824 | pmc = | doi = 10.1006/geno.1998.5315 }}
3. ^{{cite web | title = Entrez Gene: MAPK3 mitogen-activated protein kinase 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5595| accessdate = }}
4. ^{{cite journal | vauthors = Buggele WA, Johnson KE, Horvath CM | title = Influenza A virus infection of human respiratory cells induces primary microRNA expression | journal = J. Biol. Chem. | volume = 287 | issue = 37 | pages = 31027–40 | year = 2012 | pmid = 22822053 | pmc = 3438935 | doi = 10.1074/jbc.M112.387670 }}
5. ^{{cite journal | vauthors = Pal R, Bondar VV, Adamski CJ, Rodney GG, Sardiello M | title = Inhibition of ERK1/2 Restores GSK3β Activity and Protein Synthesis Levels in a Model of Tuberous Sclerosis | journal = Sci. Rep. | volume = 7 | issue = 1 | pages = 4174 | year = 2017 | pmid = 28646232 | doi = 10.1038/s41598-017-04528-5 | pmc=5482840}}
6. ^{{cite journal | vauthors = Todd JL, Tanner KG, Denu JM | title = 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 | journal = J. Biol. Chem. | volume = 274 | issue = 19 | pages = 13271–80 | date = May 1999 | pmid = 10224087 | doi = 10.1074/jbc.274.19.13271}}
7. ^{{cite journal | vauthors = Muda M, Theodosiou A, Gillieron C, Smith A, Chabert C, Camps M, Boschert U, Rodrigues N, Davies K, Ashworth A, Arkinstall S | title = The mitogen-activated protein kinase phosphatase-3 N-terminal noncatalytic region is responsible for tight substrate binding and enzymatic specificity | journal = J. Biol. Chem. | volume = 273 | issue = 15 | pages = 9323–9 | date = April 1998 | pmid = 9535927 | doi = 10.1074/jbc.273.15.9323}}
8. ^{{cite journal | vauthors = Kim DW, Cochran BH | title = Extracellular signal-regulated kinase binds to TFII-I and regulates its activation of the c-fos promoter | journal = Mol. Cell. Biol. | volume = 20 | issue = 4 | pages = 1140–8 | date = February 2000 | pmid = 10648599 | pmc = 85232 | doi = 10.1128/mcb.20.4.1140-1148.2000}}
9. ^{{cite journal | vauthors = Zhou X, Richon VM, Wang AH, Yang XJ, Rifkind RA, Marks PA | title = Histone deacetylase 4 associates with extracellular signal-regulated kinases 1 and 2, and its cellular localization is regulated by oncogenic Ras | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 97 | issue = 26 | pages = 14329–33 | date = December 2000 | pmid = 11114188 | pmc = 18918 | doi = 10.1073/pnas.250494697 }}
10. ^1 {{cite journal | vauthors = Marti A, Luo Z, Cunningham C, Ohta Y, Hartwig J, Stossel TP, Kyriakis JM, Avruch J | title = 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 | journal = J. Biol. Chem. | volume = 272 | issue = 5 | pages = 2620–8 | date = January 1997 | pmid = 9006895 | doi = 10.1074/jbc.272.5.2620}}
11. ^1 {{cite journal | vauthors = Butch ER, Guan KL | title = Characterization of ERK1 activation site mutants and the effect on recognition by MEK1 and MEK2 | journal = J. Biol. Chem. | volume = 271 | issue = 8 | pages = 4230–5 | date = February 1996 | pmid = 8626767 | doi = 10.1074/jbc.271.8.4230}}
12. ^{{cite journal | vauthors = Elion EA | title = Routing MAP kinase cascades | journal = Science | volume = 281 | issue = 5383 | pages = 1625–6 | date = September 1998 | pmid = 9767029 | doi = 10.1126/science.281.5383.1625}}
13. ^{{cite journal | vauthors = Yung Y, Yao Z, Hanoch T, Seger R | title = ERK1b, a 46-kDa ERK isoform that is differentially regulated by MEK | journal = J. Biol. Chem. | volume = 275 | issue = 21 | pages = 15799–808 | date = May 2000 | pmid = 10748187 | doi = 10.1074/jbc.M910060199 }}
14. ^1 {{cite journal | vauthors = Zheng CF, Guan KL | title = Properties of MEKs, the kinases that phosphorylate and activate the extracellular signal-regulated kinases | journal = J. Biol. Chem. | volume = 268 | issue = 32 | pages = 23933–9 | date = November 1993 | pmid = 8226933 | doi = }}
15. ^{{cite journal | vauthors = Pettiford SM, Herbst R | title = The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP | journal = Oncogene | volume = 19 | issue = 7 | pages = 858–69 | date = February 2000 | pmid = 10702794 | doi = 10.1038/sj.onc.1203408 }}
16. ^{{cite journal | vauthors = Saxena M, Williams S, Taskén K, Mustelin T | title = Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase | journal = Nat. Cell Biol. | volume = 1 | issue = 5 | pages = 305–11 | date = September 1999 | pmid = 10559944 | doi = 10.1038/13024 }}
17. ^{{cite journal | vauthors = Saxena M, Williams S, Brockdorff J, Gilman J, Mustelin T | title = Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP) | journal = J. Biol. Chem. | volume = 274 | issue = 17 | pages = 11693–700 | date = April 1999 | pmid = 10206983 | doi = 10.1074/jbc.274.17.11693}}
18. ^{{cite journal | vauthors = Roux PP, Richards SA, Blenis J | title = Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity | journal = Mol. Cell. Biol. | volume = 23 | issue = 14 | pages = 4796–804 | date = July 2003 | pmid = 12832467 | pmc = 162206 | doi = 10.1128/mcb.23.14.4796-4804.2003}}
19. ^{{cite journal | vauthors = Zhao Y, Bjorbaek C, Moller DE | title = Regulation and interaction of pp90(rsk) isoforms with mitogen-activated protein kinases | journal = J. Biol. Chem. | volume = 271 | issue = 47 | pages = 29773–9 | date = November 1996 | pmid = 8939914 | doi = 10.1074/jbc.271.47.29773}}
20. ^{{cite journal | vauthors = Mao C, Ray-Gallet D, Tavitian A, Moreau-Gachelin F | title = Differential phosphorylations of Spi-B and Spi-1 transcription factors | journal = Oncogene | volume = 12 | issue = 4 | pages = 863–73 | date = February 1996 | pmid = 8632909 | doi = }}

Further reading

{{refbegin|35em}}
  • {{cite journal | vauthors = Peruzzi F, Gordon J, Darbinian N, Amini S | title = Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway | journal = J. Neurovirol. | volume = 8 Suppl 2 | issue = 2 | pages = 91–6 | year = 2002 | pmid = 12491158 | doi = 10.1080/13550280290167885 }}
  • {{cite journal | vauthors = Meloche S, Pouysségur J | title = The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition | journal = Oncogene | volume = 26 | issue = 22 | pages = 3227–39 | year = 2007 | pmid = 17496918 | doi = 10.1038/sj.onc.1210414 }}
  • {{citation | vauthors = Ruscica M, Dozio E, Motta M, Magni P | title = Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation | volume = 604 | issue = | pages = 96–100 | year = 2007 | pmid = 17695723 | doi = 10.1007/978-0-387-69116-9_7 | isbn = 978-0-387-69114-5 | series = Advances In Experimental Medicine And Biology | chapter = Modulatory Actions of Neuropeptide y on Prostate Cancer Growth: Role of MAP Kinase/ERK 1/2 Activatio }}
{{refend}}

External links

  • MAP Kinase Resource.
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