Difference between revisions of "Phosphatase Subfamily Laforin"
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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_Laforin|Subfamily Laforin]] | [[Phosphatase classification|Phosphatase Classification]]: [[Phosphatase_Fold_CC1|Fold CC1]]: [[Phosphatase_Superfamily_CC1|Superfamily CC1]]: [[Phosphatase_Family_DSP|Family DSP]]: [[Phosphatase_Subfamily_Laforin|Subfamily Laforin]] | ||
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| + | 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. | ||
=== Evolution === | === Evolution === | ||
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=== Domain === | === 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 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 === | === Function === | ||
Revision as of 19:31, 2 March 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: 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.
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]. Epilepsy-caused mutations are found on both domains.
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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