Reactome | EPM2A dimer dephosphorylates phosphoglycogen-GYG2

EPM2A dimer dephosphorylates phosphoglycogen-GYG2

Stable Identifier

R-HSA-3781011

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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EPM2A dimer dephosphorylates phosphoglycogen-GYG2

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EPM2A (laforin), associated with PPP1R3C (protein phosphatase 1 regulatory subunit 3C, PTG) and phosphoglycogen-GYG2 in a cytosolic glycogen particle, catalyzes the dephosphorylation of phosphoglycogen (Tagliabracci et al. 2007). This reaction is inferred from the activity of EPM2A on phosphoglycogen-GYG1, and from the fact that in the absence of normal EPM2A activity, abnormally phosphorylated forms of both glycogen-GYG1 and glycogen-GYG2 accumulate in cells. The catalytically active form of EPM2A has been shown to be a homodimer (Raththagala et al. 2015; Sankhala et al. 2015).

Literature References

PubMed ID	Title	Journal	Year
25544560	Structural mechanism of laforin function in glycogen dephosphorylation and lafora disease Parker, MW, Husodo, S, Bridges, TM, Auger, KD, Hellman, LM, Turner, BD, Li, S, Hsu, S, Gentry, MS, Meekins, DA, Chakravarthy, S, Vander Kooi, CW, Brewer, MK, Paasch, BC, Woods, VL, Sherwood, AR, Wong, BK, Taylor, AO, Dukhande, VV, Raththagala, M, Sanz, P	Mol. Cell	2015
18040046	Laforin is a glycogen phosphatase, deficiency of which leads to elevated phosphorylation of glycogen in vivo Girard, JM, Roach, PJ, Delgado-Escueta, AV, Tagliabracci, VS, Zhao, X, Skurat, AV, DePaoli-Roach, AA, Wang, W, Turnbull, J, Minassian, BA	Proc. Natl. Acad. Sci. U.S.A.	2007
25538239	Dimeric quaternary structure of human laforin Cingolani, G, Sankhala, RS, Nitschke, F, Ho, L, Minassian, BA, Koksal, AC	J. Biol. Chem.	2015