EPM2A dimer dephosphorylates phosphoglycogen-GYG1

Stable Identifier
R-HSA-3781018
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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
Participants
Participates
Catalyst Activity

carbohydrate phosphatase activity of EPM2A:PPP1R3C:phosphoglycogen-GYG1:GYS1-a tetramer [cytosol]

Orthologous Events
Authored
Reviewed
Created
Cite Us!