Difference between revisions of "Phosphatase Subfamily DSP23"
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=== Domain === | === 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 === | === Function === | ||
Revision as of 19:51, 2 March 2015
Phosphatase Classification: Fold CC1: Superfamily CC1: Family DSP: Subfamily DSP23
summary...
Evolution
DSP23 is found in metazoan but lost in nematodes and most arthropods (unpublished data from gOrtholog) has a single member in human, DUSP23.
Domain
DSP23 has a single domain, the phosphatase domain. Actually, it is the shortest within DSP family [1].
Function
Laforin is a glucan phosphatase [2, 3].
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 [4]. Laforin also dephosphorylates Ser 9 of Glycogen synthase kinase 3 [5].
Laforin also as an adaptor protein involved in several physiological pathways [6]. For instance, the complex of laforin and malin modules protein phosphatase 1 regulatory subunit PPP1R3D via ubiquitination [7]. See [6] for details.
Links
Human DUSP23 page in Phosphatome.Net database.
