Difference between revisions of "Phosphatase Subfamily DSP23"

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[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
 
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
  
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summary...
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DSP23 is a nuclear phosphatase found in metazoa but lost in most ecdysozoa.
  
 
=== Evolution ===
 
=== Evolution ===
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DSP23 is found in metazoan but lost in nematodes and most arthropods ([http://resdev.gene.com/gOrtholog/view/cluster/MC0006453/overview unpublished data from gOrtholog]) has a single member in human, DUSP23.
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DSP23 is found in metazoa but lost in nematodes and most arthropods ([http://resdev.gene.com/gOrtholog/view/cluster/MC0006453/overview unpublished data from gOrtholog]). It has a single human member, DUSP23 (VHZ).
  
 
=== Domain ===
 
=== Domain ===
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DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family.
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DSP23 has a single domain, the phosphatase domain. Sequence and structure show that it is the shortest known DSP <cite>Alonso04</cite>.
  
 
=== Function ===
 
=== Function ===
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Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite>.
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Human DUSP23 dephosphorylates Ser322 on GCM1 (Glial cells missing homolog 1), a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation <cite>Lin11</cite>.  
  
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laforin is also a phosphatase of muscle glycogen synthase (GS1) in polyglucosan bodies (PBs).
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DSP23 is also called VHZ for its similarity with VHR phosphatase. Different from MAP kinases phosphatases which negatively regulate MAP kinases such as JNK and p38, DSP23 has been reported to enhance activation of JNK and p38 <cite>Takagaki04</cite>. Human DSP23 locates at centrosome in [http://en.wikipedia.org/wiki/MCF-7 MCF-7] cells and is proposed to be involved in cell growth and human primary cancers. <cite>Tang10</cite>.  
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In [http://en.wikipedia.org/wiki/Lafora_disease Lafora disease] (LD), the deficiency of either laforin or E3 ligase malin causes massive accumulation of less-branched glycogen inclusions, known as [http://en.wikipedia.org/wiki/Lafora_disease#Lafora_bodies Lafora bodies], also called polyglucosan bodies (PBs), in several types of cells including neurons. Once GS1-synthesized polyglucosan accumulates into PBs, laforin recruits malin to the PBs where laforin dephosphorylates, and malin degrades the GS1 in concert with GPBB and AGL1, resulting in a breakdown of polyglucosan <cite>Liu14</cite>. Laforin also dephosphorylates Ser 9 of Glycogen synthase kinase 3 <cite>Lohi05</cite>.
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Laforin also as an adaptor protein involved in several physiological pathways <cite>Gentry13</cite>. For instance, the complex of laforin and malin modules protein phosphatase 1 regulatory subunit PPP1R3D via ubiquitination <cite>Rubio-Villena13</cite>. See <cite>Gentry13</cite> for details.
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=== Links ===
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[http://phosphatome.net/3.0/database/gene/uid/HsapP023 Human DUSP23 page] in Phosphatome.Net database.
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=== References ===
 
=== References ===
 
<biblio>
 
<biblio>
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#Alonso04 pmid=15201283
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#Lin11 pmid=20855292
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#Takagaki04 pmid=15281913
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#Tang10 pmid=20509867
 
</biblio>
 
</biblio>

Latest revision as of 05:57, 22 March 2017

Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily DSP23

DSP23 is a nuclear phosphatase found in metazoa but lost in most ecdysozoa.

Evolution

DSP23 is found in metazoa but lost in nematodes and most arthropods (unpublished data from gOrtholog). It has a single human member, DUSP23 (VHZ).

Domain

DSP23 has a single domain, the phosphatase domain. Sequence and structure show that it is the shortest known DSP [1].

Function

Human DUSP23 dephosphorylates Ser322 on GCM1 (Glial cells missing homolog 1), a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation [2].

DSP23 is also called VHZ for its similarity with VHR phosphatase. Different from MAP kinases phosphatases which negatively regulate MAP kinases such as JNK and p38, DSP23 has been reported to enhance activation of JNK and p38 [3]. Human DSP23 locates at centrosome in MCF-7 cells and is proposed to be involved in cell growth and human primary cancers. [4].

References

  1. Alonso A, Burkhalter S, Sasin J, Tautz L, Bogetz J, Huynh H, Bremer MC, Holsinger LJ, Godzik A, and Mustelin T. The minimal essential core of a cysteine-based protein-tyrosine phosphatase revealed by a novel 16-kDa VH1-like phosphatase, VHZ. J Biol Chem. 2004 Aug 20;279(34):35768-74. DOI:10.1074/jbc.M403412200 | PubMed ID:15201283 | HubMed [Alonso04]
  2. Lin FY, Chang CW, Cheong ML, Chen HC, Lee DY, Chang GD, and Chen H. Dual-specificity phosphatase 23 mediates GCM1 dephosphorylation and activation. Nucleic Acids Res. 2011 Feb;39(3):848-61. DOI:10.1093/nar/gkq838 | PubMed ID:20855292 | HubMed [Lin11]
  3. Takagaki K, Satoh T, Tanuma N, Masuda K, Takekawa M, Shima H, and Kikuchi K. Characterization of a novel low-molecular-mass dual-specificity phosphatase-3 (LDP-3) that enhances activation of JNK and p38. Biochem J. 2004 Nov 1;383(Pt. 3):447-55. DOI:10.1042/BJ20040498 | PubMed ID:15281913 | HubMed [Takagaki04]
  4. Tang JP, Tan CP, Li J, Siddique MM, Guo K, Chan SW, Park JE, Tay WN, Huang ZY, Li WC, Chen J, and Zeng Q. VHZ is a novel centrosomal phosphatase associated with cell growth and human primary cancers. Mol Cancer. 2010 May 28;9:128. DOI:10.1186/1476-4598-9-128 | PubMed ID:20509867 | HubMed [Tang10]
All Medline abstracts: PubMed | HubMed
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