Phosphatase Subfamily Laforin - Revision history

Gerard at 04:34, 30 April 2015

2015-04-30T04:34:43Z

Gerard at 04:34, 30 April 2015

2015-04-30T04:34:29Z

Gerard at 04:34, 30 April 2015

2015-04-30T04:34:07Z

Gerard at 04:15, 30 April 2015

2015-04-30T04:15:10Z

Mark: /* Function */

2015-04-22T17:19:06Z

‎Function

Mark at 19:31, 2 March 2015

2015-03-02T19:31:57Z

Mark at 02:03, 28 February 2015

2015-02-28T02:03:01Z

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

2015-02-27T05:15:51Z

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_Laforin|Subfamily Laforin]]

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

=== Domain ===
Laforin

=== Function ===
Laforin is a glucan phosphatase. Laforin mutations have been associated with myoclonic epilepsy of [http://en.wikipedia.org/wiki/Lafora_disease Lafora].

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

@@ Line 19: / Line 19: @@
 Laforin also serves 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.
-DSP4/SEX4 is one of several plant Laforins, and is implicated in breakdown of starch in the chloroplast <cite>Kotting<cite>, as is another family member, LSF2 <cite>Santelia</cite>, while LSF1 is predicted to be an inactive scaffold <cite>Silver</cite>
+DSP4/SEX4 is one of several plant Laforins, and is implicated in breakdown of starch in the chloroplast <cite>Kotting</cite>, as is another family member, LSF2 <cite>Santelia</cite>, while LSF1 is predicted to be an inactive scaffold <cite>Silver</cite>
 === References ===

@@ Line 19: / Line 19: @@
 Laforin also serves 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.
-DSP4/SEX4 is one of several plant Laforins, and is implicated in breakdown of starch in the chloroplast <cite>Kotting<cite>, as is another family member, LSF2 <cite>Santelia<cite>, while LSF1 is predicted to be an inactive scaffold <cite>Silver</cite>
+DSP4/SEX4 is one of several plant Laforins, and is implicated in breakdown of starch in the chloroplast <cite>Kotting<cite>, as is another family member, LSF2 <cite>Santelia</cite>, while LSF1 is predicted to be an inactive scaffold <cite>Silver</cite>
 === References ===

@@ 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_Laforin|Subfamily Laforin]]
-Laforin is a subfamily found in vertebrates and scattered among other species. It's not only a phosphatase, but also acts as an adaptor protein involved in different physiological pathways.
+Laforin is a [http://en.wikipedia.org/wiki/Glucan glucan] phosphatase and an adaptor protein.
 === Evolution ===
-Laforin found in vertebrates, ciliates, alveolates and plants as well as a few additional species including the animals Trichinella (nematode), Branchiostoma (lancelet) and Nematostella (anemone). It has a single human member, EPM2A.
+Laforin found in vertebrates, ciliates, alveolates and plants as well as a few scattered additional species including the animals Trichinella (nematode), Branchiostoma (lancelet) and Nematostella (anemone). It has a single human member, EPM2A.
 === Domain ===
@@ Line 12: / Line 12: @@
 === Function ===
-Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite>.
+Laforin is a glucan phosphatase <cite>Worby06, Gentry07</cite> and 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 the 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 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.
+Laforin also serves 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 ===
@@ Line 26: / Line 26: @@
 #Gentry07 pmid=17646401
 #Gentry13 pmid=22364389
 #Liu06 pmid=16971387
 #Liu14 pmid=24068615
 #Lohi05 pmid=16115820
 #Rubio-Villena13 pmid=23624058
 #Wang02 pmid=11739371
 #Worby06 pmid=16901901
 </biblio>

@@ Line 5: / Line 5: @@
 === Evolution ===
-Laforin found in vertebrates and scattered other species. It has a single human member, EPM2A.
+Laforin found in vertebrates, ciliates, alveolates and plants as well as a few additional species including the animals Trichinella (nematode), Branchiostoma (lancelet) and Nematostella (anemone). 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>.
+Laforin typically has an N-terminal CBM20 carbohydrate-binding module and a C-terminal phosphatase domain. The carbohydrate-binding module targets laforin to Lafora inclusion bodies <cite>Wang02, Ganesh04</cite>. The phosphatase domain directly dephosphorylates glycogen <cite>Worby06, Gentry07</cite>. Multiple plant homologs lack the CBM20 domain.
 [http://www.omim.org/allelicVariant/607566 Epilepsy-caused mutations] are found on both domains.

@@ Line 15: / Line 15: @@
 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>.
+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 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.

Phosphatase Subfamily Laforin - Revision history

Gerard at 04:34, 30 April 2015

Gerard at 04:34, 30 April 2015

Gerard at 04:34, 30 April 2015

Gerard at 04:15, 30 April 2015

Mark: /* Function */

Mark at 19:31, 2 March 2015

Mark at 02:03, 28 February 2015

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_..."