[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki\/extracellular-signal-regulated-kinases-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki\/extracellular-signal-regulated-kinases-wikipedia\/","headline":"Extracellular signal-regulated kinases &#8211; Wikipedia","name":"Extracellular signal-regulated kinases &#8211; Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Class of enzymes In molecular biology, extracellular signal-regulated kinases (ERKs) or classical MAP","datePublished":"2022-12-04","dateModified":"2022-12-04","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/44a4cee54c4c053e967fe3e7d054edd4?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki\/extracellular-signal-regulated-kinases-wikipedia\/","wordCount":4224,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Class of enzymesIn molecular biology, extracellular signal-regulated kinases (ERKs) or classical MAP kinases are widely expressed protein kinase intracellular signalling molecules that are involved in functions including the regulation of meiosis, mitosis, and postmitotic functions in differentiated cells.  Many different stimuli, including growth factors, cytokines, virus infection, ligands for  heterotrimeric G protein-coupled receptors, transforming agents, and carcinogens, activate the ERK pathway.[citation needed]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4The term, &#8220;extracellular signal-regulated kinases&#8221;, is sometimes used as a synonym for mitogen-activated protein kinase (MAPK), but has more recently been adopted for a specific subset of the mammalian MAPK family.[citation needed]In the MAPK\/ERK pathway, Ras activates c-Raf, followed by mitogen-activated protein kinase kinase (abbreviated as MKK, MEK, or MAP2K) and then MAPK1\/2 (below).  Ras is typically activated by growth hormones through receptor tyrosine kinases and GRB2\/SOS, but may also receive other signals.  ERKs are known to activate many transcription factors, such as ELK1,[1] and some downstream protein kinases.Disruption of the ERK pathway is common in cancers, especially Ras, c-Raf, and receptors such as HER2.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsMitogen-activated protein kinase 1[edit]Mitogen-activated protein kinase 3[edit]Clinical significance[edit]References[edit]External links[edit]Mitogen-activated protein kinase 1[edit]Mitogen-activated protein kinase 1 (MAPK1) is also known as extracellular signal-regulated kinase 2 (ERK2). Two similar protein kinases with 85% sequence identity were originally called ERK1 and ERK2.[2] They were found during a search for protein kinases that are rapidly phosphorylated after activation of cell surface tyrosine kinases such as the epidermal growth factor receptor. Phosphorylation of ERKs leads to the activation of their kinase activity.The molecular events linking cell surface receptors to activation of ERKs are complex. It was found that Ras GTP-binding proteins are involved in the activation of ERKs.[3] Another protein kinase, Raf-1, was shown to phosphorylate a &#8220;MAP kinase-kinase&#8221;, thus qualifying as a &#8220;MAP kinase kinase kinase&#8221;.[4] The MAP kinase-kinase, which activates ERK, was named &#8220;MAPK\/ERK kinase&#8221; (MEK).[5]Receptor-linked tyrosine kinases, Ras, Raf, MEK, and MAPK could be fitted into a signaling cascade linking an extracellular signal to MAPK activation.[6] See: MAPK\/ERK pathway.Transgenic gene knockout mice lacking MAPK1 have major defects in early development.[7] Conditional deletion of Mapk1 in B cells showed a role for MAPK1 in T-cell-dependent antibody production.[8] A dominant gain-of-function mutant of Mapk1 in transgenic mice showed a role for MAPK1 in T-cell development.[9] Conditional inactivation of Mapk1 in neural progenitor cells of the developing cortex lead to a reduction of cortical thickness and reduced proliferation in neural progenitor cells.[10]Mitogen-activated protein kinase 3[edit]Mitogen-activated protein kinase 3 (MAPK3) is also known as extracellular signal-regulated kinase 1 (ERK1). Transgenic gene knockout mice lacking MAPK3 are viable and it is thought that MAPK1 can fulfill some MAPK3 functions in most cells.[11] The main exception is in T cells. Mice lacking MAPK3 have  reduced T cell development past the CD4+ and CD8+ stage.Clinical significance[edit]Activation of the ERK1\/2 pathway by aberrant RAS\/RAF signalling, DNA damage, and oxidative stress leads to cellular senescence.[12] Low doses of DNA damage resulting from cancer therapy cause ERK1\/2 to induce senescence, whereas higher doses of DNA damage fail to activate ERK1\/2, and thus induce cell death by apoptosis.[12]References[edit]^ Rao VN, Reddy ES (July 1994). &#8220;elk-1 proteins interact with MAP kinases&#8221;. Oncogene. 9 (7): 1855\u201360. PMID\u00a08208531.^ Boulton TG, Cobb MH (May 1991). &#8220;Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies&#8221;. Cell Regulation. 2 (5): 357\u201371. doi:10.1091\/mbc.2.5.357. PMC\u00a0361802. PMID\u00a01654126.^ Leevers SJ, Marshall CJ (February 1992). &#8220;Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein&#8221;. The EMBO Journal. 11 (2): 569\u201374. doi:10.1002\/j.1460-2075.1992.tb05088.x. PMC\u00a0556488. PMID\u00a01371463.^ Kyriakis JM, App H, Zhang XF, Banerjee P, Brautigan DL, Rapp UR, Avruch J (July 1992). &#8220;Raf-1 activates MAP kinase-kinase&#8221;. Nature. 358 (6385): 417\u201321. Bibcode:1992Natur.358..417K. doi:10.1038\/358417a0. PMID\u00a01322500. S2CID\u00a04335307.^ Crews CM, Erikson RL (September 1992). &#8220;Purification of a murine protein-tyrosine\/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product&#8221;. Proceedings of the National Academy of Sciences of the United States of America. 89 (17): 8205\u20139. Bibcode:1992PNAS&#8230;89.8205C. doi:10.1073\/pnas.89.17.8205. PMC\u00a049886. PMID\u00a01381507.^ Itoh T, Kaibuchi K, Masuda T, Yamamoto T, Matsuura Y, Maeda A, Shimizu K, Takai Y (February 1993). &#8220;A protein factor for ras p21-dependent activation of mitogen-activated protein (MAP) kinase through MAP kinase kinase&#8221;. Proceedings of the National Academy of Sciences of the United States of America. 90 (3): 975\u20139. Bibcode:1993PNAS&#8230;90..975I. doi:10.1073\/pnas.90.3.975. PMC\u00a045793. PMID\u00a08381539.^ Yao Y, Li W, Wu J, Germann UA, Su MS, Kuida K, Boucher DM (October 2003). &#8220;Extracellular signal-regulated kinase 2 is necessary for mesoderm differentiation&#8221;. Proceedings of the National Academy of Sciences of the United States of America. 100 (22): 12759\u201364. Bibcode:2003PNAS..10012759Y. doi:10.1073\/pnas.2134254100. PMC\u00a0240691. PMID\u00a014566055.^ Sanjo, Hideki; Hikida, Masaki; Aiba, Yuichi; Mori, Yoshiko; Hatano, Naoya; Ogata, Masato; Kurosaki, Tomohiro (2007). &#8220;Extracellular signal-regulated protein kinase 2 is required for efficient generation of B cells bearing antigen-specific immunoglobulin G&#8221;. Molecular and Cellular Biology. 27 (4): 1236\u20131246. doi:10.1128\/MCB.01530-06. ISSN\u00a00270-7306. PMC\u00a01800707. PMID\u00a017145771.^ Sharp, L. L.; Schwarz, D. A.; Bott, C. M.; Marshall, C. J.; Hedrick, S. M. (1997). &#8220;The influence of the MAPK pathway on T cell lineage commitment&#8221;. Immunity. 7 (5): 609\u2013618. doi:10.1016\/s1074-7613(00)80382-9. ISSN\u00a01074-7613. PMID\u00a09390685.^ Samuels, Ivy S.; Karlo, J. Colleen; Faruzzi, Alicia N.; Pickering, Kathryn; Herrup, Karl; Sweatt, J. David; Saitta, Sulagna C.; Landreth, Gary E. (2008-07-02). &#8220;Deletion of ERK2 mitogen-activated protein kinase identifies its key roles in cortical neurogenesis and cognitive function&#8221;. The Journal of Neuroscience. 28 (27): 6983\u20136995. doi:10.1523\/JNEUROSCI.0679-08.2008. ISSN\u00a01529-2401. PMC\u00a04364995. PMID\u00a018596172.^ Pag\u00e8s G, Gu\u00e9rin S, Grall D, Bonino F, Smith A, Anjuere F, Auberger P, Pouyss\u00e9gur J (November 1999). &#8220;Defective thymocyte maturation in p44 MAP kinase (Erk 1) knockout mice&#8221;. Science. 286 (5443): 1374\u20137. doi:10.1126\/science.286.5443.1374. PMID\u00a010558995.^ a b Anerillas C, Abdelmohsen K, Gorospe M (2020). &#8220;Regulation of senescence traits by MAPKs&#8221;. GeroScience. 42 (2): 397\u2013408. doi:10.1007\/s11357-020-00183-3. PMC\u00a07205942. PMID\u00a032300964.External links[edit]     (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki\/extracellular-signal-regulated-kinases-wikipedia\/#breadcrumbitem","name":"Extracellular signal-regulated kinases &#8211; Wikipedia"}}]}]