MAPKAPK2: Difference between revisions

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* [[PHC2]],<ref name = pmid15094067>{{cite journal | vauthors = Yannoni YM, Gaestel M, Lin LL | title = P66(ShcA) interacts with MAPKAP kinase 2 and regulates its activity | journal = FEBS Lett. | volume = 564 | issue = 1-2 | pages = 205–11 | date = Apr 2004 | pmid = 15094067 | doi = 10.1016/S0014-5793(04)00351-5 }}</ref>  and
* [[PHC2]],<ref name = pmid15094067>{{cite journal | vauthors = Yannoni YM, Gaestel M, Lin LL | title = P66(ShcA) interacts with MAPKAP kinase 2 and regulates its activity | journal = FEBS Lett. | volume = 564 | issue = 1-2 | pages = 205–11 | date = Apr 2004 | pmid = 15094067 | doi = 10.1016/S0014-5793(04)00351-5 }}</ref>  and
* [[SHC1]].<ref name = pmid15094067/>
* [[SHC1]].<ref name = pmid15094067/>
* [[RIPK1]] <ref>{{cite journal | vauthors = Dondelinger Y, Delanghe T, Rojas-Rivera D, Priem D, Delvaeye T, Bruggeman I, Van Herreweghe F, Vandenabeele P, Bertrand MJ | title = MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death | journal = Nature Cell Biology | volume = 19 | issue = 10 | pages = 1237–1247 | date = October 2017 | pmid = 28920952 | doi = 10.1038/ncb3608 }}</ref>


== References ==
== References ==
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== Further reading ==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
* {{cite journal | vauthors = Kapopara PR, von Felden J, Soehnlein O, Wang Y, Napp LC, Sonnenschein K, Wollert KC, Schieffer B, Gaestel M, Bauersachs J, Bavendiek U |author-link10=Johann Bauersachs | title = Deficiency of MAPK-activated protein kinase 2 (MK2) prevents adverse remodelling and promotes endothelial healing after arterial injury | journal = Thromb Haemost. | volume = 112 | issue = 6 | pages = 1–13 | year = 2014 | pmid = 25120198 | doi = 10.1160/TH14-02-0174 }}
* {{cite journal | vauthors = Kapopara PR, von Felden J, Soehnlein O, Wang Y, Napp LC, Sonnenschein K, Wollert KC, Schieffer B, Gaestel M, Bauersachs J, Bavendiek U |author-link10=Johann Bauersachs | title = Deficiency of MAPK-activated protein kinase 2 (MK2) prevents adverse remodelling and promotes endothelial healing after arterial injury | journal = Thromb. Haemost. | volume = 112 | issue = 6 | pages = 1–13 | year = 2014 | pmid = 25120198 | doi = 10.1160/TH14-02-0174 }}
* {{cite journal | vauthors = Ben-Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ | title = Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2 | journal = Curr. Biol. | volume = 8 | issue = 19 | pages = 1049–57 | year = 1999 | pmid = 9768359 | doi = 10.1016/S0960-9822(98)70442-7 }}
* {{cite journal | vauthors = Ben-Levy R, Hooper S, Wilson R, Paterson HF, Marshall CJ | title = Nuclear export of the stress-activated protein kinase p38 mediated by its substrate MAPKAP kinase-2 | journal = Curr. Biol. | volume = 8 | issue = 19 | pages = 1049–57 | year = 1999 | pmid = 9768359 | doi = 10.1016/S0960-9822(98)70442-7 }}
* {{cite journal | vauthors = Stokoe D, Engel K, Campbell DG, Cohen P, Gaestel M | title = Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins | journal = FEBS Lett. | volume = 313 | issue = 3 | pages = 307–13 | year = 1992 | pmid = 1332886 | doi = 10.1016/0014-5793(92)81216-9 }}
* {{cite journal | vauthors = Stokoe D, Engel K, Campbell DG, Cohen P, Gaestel M | title = Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins | journal = FEBS Lett. | volume = 313 | issue = 3 | pages = 307–13 | year = 1992 | pmid = 1332886 | doi = 10.1016/0014-5793(92)81216-9 }}

Latest revision as of 06:00, 28 August 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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MAP kinase-activated protein kinase 2 is an enzyme that in humans is encoded by the MAPKAPK2 gene.[1][2]

Function

This gene encodes a member of the Ser/Thr protein kinase family. This kinase is regulated through direct phosphorylation by p38 MAP kinase. In conjunction with p38 MAP kinase, this kinase is known to be involved in many cellular processes including stress and inflammatory responses, nuclear export, gene expression regulation and cell proliferation. Heat shock protein HSP27 was shown to be one of the substrates of this kinase in vivo. Two transcript variants encoding two different isoforms have been found for this gene.[3]

See also

  • SB 203580, suppresses the activation of MAPKAPK2

Interactions

MAPKAPK2 has been shown to interact with:

References

  1. Zu YL, Wu F, Gilchrist A, Ai Y, Labadia ME, Huang CK (Jun 1994). "The primary structure of a human MAP kinase activated protein kinase 2". Biochem Biophys Res Commun. 200 (2): 1118–24. doi:10.1006/bbrc.1994.1566. PMID 8179591.
  2. Stokoe D, Caudwell B, Cohen PT, Cohen P (Feb 1994). "The substrate specificity and structure of mitogen-activated protein (MAP) kinase-activated protein kinase-2". Biochem J. 296 (Pt 3): 843–9. PMC 1137771. PMID 8280084.
  3. "Entrez Gene: MAPKAPK2 mitogen-activated protein kinase-activated protein kinase 2".
  4. 4.0 4.1 Rane MJ, Coxon PY, Powell DW, Webster R, Klein JB, Pierce W, Ping P, McLeish KR (Feb 2001). "p38 Kinase-dependent MAPKAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils". J. Biol. Chem. 276 (5): 3517–23. doi:10.1074/jbc.M005953200. PMID 11042204.
  5. Janknecht R (Nov 2001). "Cell type-specific inhibition of the ETS transcription factor ER81 by mitogen-activated protein kinase-activated protein kinase 2". J. Biol. Chem. 276 (45): 41856–61. doi:10.1074/jbc.M106630200. PMID 11551945.
  6. 6.0 6.1 Yannoni YM, Gaestel M, Lin LL (Apr 2004). "P66(ShcA) interacts with MAPKAP kinase 2 and regulates its activity". FEBS Lett. 564 (1–2): 205–11. doi:10.1016/S0014-5793(04)00351-5. PMID 15094067.
  7. Dondelinger Y, Delanghe T, Rojas-Rivera D, Priem D, Delvaeye T, Bruggeman I, Van Herreweghe F, Vandenabeele P, Bertrand MJ (October 2017). "MK2 phosphorylation of RIPK1 regulates TNF-mediated cell death". Nature Cell Biology. 19 (10): 1237–1247. doi:10.1038/ncb3608. PMID 28920952.

Further reading