Difference between revisions of "Phosphatase Subfamily Laforin"
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=== Domain === | === Domain === | ||
| − | Laforin | + | 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>. |
=== Function === | === Function === | ||
| − | Laforin is a glucan phosphatase. | + | 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 === | === References === | ||
| − | |||
<biblio> | <biblio> | ||
| + | #Ganesh04 pmid=14706656 | ||
| + | #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> | </biblio> | ||
Revision as of 02:03, 28 February 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily Laforin
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 [1, 2]. The phosphatase domain can directly dephosphorylates glycogen [3, 4].
Function
Laforin is a glucan phosphatase [3, 4].
laforin is also a phosphatase of muscle glycogen synthase (GS1) in polyglucosan bodies (PBs). In Lafora disease (LD), the deficiency of either laforin or E3 ligase malin causes massive accumulation of less-branched glycogen inclusions, known as 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 [5]. Laforin also dephosphorylates Ser 9 of Glycogen synthase kinase 3 [6].
Laforin also as an adaptor protein involved in several physiological pathways [7]. For instance, the complex of laforin and malin modules protein phosphatase 1 regulatory subunit PPP1R3D via ubiquitination [8]. See [7] for details.
References
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Error fetching PMID 22364389:
Error fetching PMID 16971387:
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Error fetching PMID 23624058:
Error fetching PMID 11739371:
Error fetching PMID 16901901:
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- Error fetching PMID 14706656:
- Error fetching PMID 16901901:
- Error fetching PMID 17646401:
- Error fetching PMID 24068615:
- Error fetching PMID 16115820:
- Error fetching PMID 22364389:
- Error fetching PMID 23624058:
- Error fetching PMID 16971387:
