NHLRC1 mediated ubiquitination of EPM2A (laforin) and PPP1RC3 (PTG) associated with glycogen-GYG2
EPM2A:PPP1R3C:glycogen-GYG2:GYS2-a tetramer + 2 Ub → K48polyUb-PPP1R3C + glycogen-GYG2:GYS2-a tetramer + 2 K48polyUb-EPM2A
- Reactome
- R-HSA-3780995
- Compartment
- cytosol
- Rhea
- None recorded
Inputs
- EPM2A:PPP1R3C:glycogen-GYG2:GYS2-a tetramerR-HSA-3780991, cytosol
- 2 UbR-HSA-113595, cytosol
Outputs
- K48polyUb-PPP1R3CR-HSA-3781005, cytosol
- glycogen-GYG2:GYS2-a tetramerR-HSA-3322011, cytosol
- 2 K48polyUb-EPM2AR-HSA-3781004, cytosol
Catalysed by
- ubiquitin-protein transferase activity of NHLRC1 [cytosol]EC 6.3.2.19; UniProt Q6VVB1
Literature
- Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin J. Biol. Chem., 2010
- Insights into Lafora disease: malin is an E3 ubiquitin ligase that ubiquitinates and promotes the degradation of laforin Proc. Natl. Acad. Sci. U.S.A., 2005
- Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG) J. Biol. Chem., 2008