SNCAIP is ubiquitinated by several different E3 ubiquitin-ligases, including Parkin (PARK2). PARK2 overexpression with SNCAIP in cell culture leads to the formation of protein aggregates (Chung et al. 2001). PARK2 preferentially mediates the addition of lysine-63 (K63)-linked polyubiquitination of SNCAIP (Lim et al. 2005). This leads to SNCAIP degradation only at an unusually high PARK2 to SNCAIP ratio (Lim et al. 2005). K63-linked ubiquitination may be a signal that leads to the degradation of inclusions by autophagy when the ubiquitin-proteasome system is dysfunctional (Lim et al. 2005, Tan et al. 2008).
Zhang, Y, Dawson, TM, Ross, CA, Dawson, VL, Lim, KL, Gao, J, Huang, H, Chung, KK, Tanaka, Y
ubiquitin-protein transferase activity of PARK2:SNCAIP [cytosol]
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