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NHLRC1 mediated ubiquitination of EPM2A and PPP1RC3 associated with glycogen-GYG1 (R-HSA-3781009) [Homo sapiens]

Black Box Event
Summation

NHLRC1 (malin) associates with the glycogen particle where it functions as a ubiquitin E3 ligase to mediate the polyubiquitination of EPM2A (laforin) and PPP1R3C (PTG). The two polyubiquitinated proteins are targeted for proteasome-mediated degradation, leaving a glycogen-GYG1 particle associated with GYS1 (Gentry et al. 2005, Worby et al. 2008). In NHLRC1 knockout mice, PPP1R3C levels are unchanged, rather than increased, suggesting that NHLRC1 does not target PPP1R3C for degradation. However, EPM2A protein levels are increased in this knockout consistent with NHLRC1's proposed role (DePaoli-Roach et al. 2010).

Locations in the PathwayBrowser
Additional Information
Compartment cytosol
Components of this entry
Input entries
Output entries
Catalyst Activity
PhysicalEntity Activity Active Units
NHLRC1 ubiquitin-protein transferase activity (0004842)  
Literature References
pubMedId Title Journal Year
20538597 Genetic depletion of the malin E3 ubiquitin ligase in mice leads to lafora bodies and the accumulation of insoluble laforin J. Biol. Chem. 2010
15930137 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
18070875 Malin decreases glycogen accumulation by promoting the degradation of protein targeting to glycogen (PTG) J. Biol. Chem. 2008
Inferred Entries
Orthologous events
 
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