Reactome | EPM2A dimer dephosphorylates phosphoglycogen-GYG1

EPM2A dimer dephosphorylates phosphoglycogen-GYG1

Stable Identifier

R-HSA-3781018

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

ReviewStatus

5/5

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EPM2A dimer dephosphorylates phosphoglycogen-GYG1

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EPM2A (laforin), associated with PPP1R3C (protein phosphatase 1 regulatory subunit 3C, PTG) and phosphoglycogen-GYG1 in a cytosolic glycogen particle, catalyzes the dephosphorylation of phosphoglycogen (Tagliabracci et al. 2007). 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