SUMO E3 ligase activity of TRIM proteins英文文献.pdfVIP

Oncogene (2010), 1–9 2010 Macmillan Publishers Limited All rights reserved 0950-9232/10 /onc ORIGINAL ARTICLE SUMO E3 ligase activity of TRIM proteins Y Chu1 and X Yang Department of Cancer Biology and Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, USA SUMOylation governs numerous cellular processes and SAE2), the SUMO-conjugating enzyme E2 (Ubc9) and is essential to most eukaryotic life. Despite increasing one of the SUMO ligases or E3s. SUMO E3s confer recognition of the importance of this process, an SUMOylation specificity and efficiency. However, in extremely limited number of small ubiquitin-like modifier contrast to the over 600 known ubiquitin E3s (Deshaies (SUMO) protein ligases (E3s) have been identified. Here and Joazeiro, 2009), only a handful of SUMO E3s we show that at least some members of the functionally have been reported. These include protein inhibitor of diverse tripartite motif (TRIM) superfamily are SUMO activated STAT proteins (PIAS proteins) (Hochstrasser, E3s. These TRIM proteins bind both the SUMO- 2001; Johnson and Gupta, 2001; Kahyo et al., 2001), the conjugating enzyme Ubc9 and substrates and strongly nuclear pore protein RanBP2 (Pichler et al., 2002) and enhance transfer of SUMOs from Ubc9 to these the polycomb group protein Pc2 (Kagey et al., 2003). substrates. Among the substrates of TRIM SUMO E3s With the identification of numerous SUMOylation targets are the tumor suppress