Phosphatase Subfamily DSP23 - Revision history

Gerard at 05:57, 22 March 2017

2017-03-22T05:57:36Z

Gerard at 05:30, 22 March 2017

2017-03-22T05:30:41Z

Mark at 20:53, 2 March 2015

2015-03-02T20:53:10Z

Mark: /* Domain */

2015-03-02T19:51:33Z

‎Domain

Mark: /* Domain */

2015-03-02T19:48:14Z

‎Domain

Mark at 19:46, 2 March 2015

2015-03-02T19:46:23Z

Mark: /* Evolution */

2015-03-02T19:41:43Z

‎Evolution

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

2015-03-02T19:40:49Z

Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

New page

__NOTOC__
[[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]

summary...

=== Evolution ===
Laforin found in vertebrates and scattered other species. It has a single human member, EPM2A.

=== Domain ===
Laforin has two domains: carbohydrate-binding module and phosphatase domain. The carbohydrate-binding module targets laforin to Lafora inclusion bodies <cite>Wang02, Ganesh04</cite>. The phosphatase domain can directly dephosphorylates glycogen <cite>Worby06, Gentry07</cite>.
[http://www.omim.org/allelicVariant/607566 Epilepsy-caused mutations] are found on both domains.

=== Function ===
Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite>.

laforin is also a phosphatase of muscle glycogen synthase (GS1) in polyglucosan bodies (PBs).
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>.

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.

=== References ===
<biblio>
</biblio>

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
-DSP23 is a nuclear phosphatase found in metazoan but lost in most ecdysozoa.
+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 ([http://resdev.gene.com/gOrtholog/view/cluster/MC0006453/overview unpublished data from gOrtholog]). It has a single human member, DUSP23.
+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 ===
-DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family <cite>Alonso04</cite>.
+DSP23 has a single domain, the phosphatase domain. Sequence and structure show that it is the shortest known DSP <cite>Alonso04</cite>.
 === Function ===

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
-DSP23 is a nuclear phosphatase found in metazoan but lost in ecdysozoan.
+DSP23 is a nuclear phosphatase found in metazoan but lost in most ecdysozoa.
 === Evolution ===
-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.
+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.
 === Domain ===
@@ Line 11: / Line 11: @@
 === Function ===
-Human DUSP23 dephosphorylates Ser322 on Glial cells missing homolog 1 (GCM1), which is a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation <cite>Lin11</cite>.
+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>.
 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>.

@@ Line 8: / Line 8: @@
 === Domain ===
-DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family.
+DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family <cite>Alonso04</cite>.
 === Function ===

@@ Line 2: / Line 2: @@
 [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]:  [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_DSP23|Subfamily DSP23]]
-summary...
+DSP23 is a nuclear phosphatase found in metazoan but lost in ecdysozoan.
 === Evolution ===
@@ Line 11: / Line 11: @@
 === Function ===
-Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite>.
+Human DUSP23 dephosphorylates Ser322 on Glial cells missing homolog 1 (GCM1), which is a transcription factor essential for placental development. The dephosphorylation promotes GCM1 acetylation <cite>Lin11</cite>.
-laforin is also a phosphatase of muscle glycogen synthase (GS1) in polyglucosan bodies (PBs).
+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>.
-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>.
-−
-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.
-−
-=== Links ===
-[http://phosphatome.net/3.0/database/gene/uid/HsapP023 Human DUSP23 page] in Phosphatome.Net database.
 === References ===
 <biblio>
 </biblio>

Phosphatase Subfamily DSP23 - Revision history

Gerard at 05:57, 22 March 2017

Gerard at 05:30, 22 March 2017

Mark at 20:53, 2 March 2015

Mark: /* Domain */

Mark: /* Domain */

Mark at 19:46, 2 March 2015

Mark: /* Evolution */

Mark: Created page with "__NOTOC__ Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."

Mark: Created page with "NOTOC Phosphatase Classification: Fold CC1: Superfamily CC1: Phosphatase_Family_..."