TY - JOUR
T1 - A SIM-ultaneous role for SUMO and ubiquitin
AU - Perry, J. Jefferson P.
AU - Tainer, John A.
AU - Boddy, Michael N.
N1 - Funding Information:
We thank The Scripps Research Cell Cycle and Structural Biology groups for their support. Work in the laboratory of M.N.B. is supported by NIH grant GM068608 and research on DNA-damage responses, replication stress and the RecQ helicases in the laboratory of J.A.T. is supported by NIH grant CA104660.
PY - 2008/5
Y1 - 2008/5
N2 - Ubiquitin and ubiquitin-like proteins (Ubls) share a β-GRASP fold and have key roles in cellular growth and suppression of genome instability. Despite their common fold, SUMO and ubiquitin are classically portrayed as distinct, and they can have antagonistic roles. Recently, a new family of proteins, the small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs), which directly connect sumoylation and ubiquitylation, has been discovered. Uniquely, STUbLs use SUMO-interaction motifs (SIMs) to recognize their sumoylated targets. STUbLs are global regulators of protein sumoylation levels, and cells lacking STUbLs display genomic instability and hypersensitivity to genotoxic stress. The human STUbL, RNF4, is implicated in several diseases including cancer, highlighting the importance of characterizing the cellular functions of STUbLs.
AB - Ubiquitin and ubiquitin-like proteins (Ubls) share a β-GRASP fold and have key roles in cellular growth and suppression of genome instability. Despite their common fold, SUMO and ubiquitin are classically portrayed as distinct, and they can have antagonistic roles. Recently, a new family of proteins, the small ubiquitin-related modifier (SUMO)-targeted ubiquitin ligases (STUbLs), which directly connect sumoylation and ubiquitylation, has been discovered. Uniquely, STUbLs use SUMO-interaction motifs (SIMs) to recognize their sumoylated targets. STUbLs are global regulators of protein sumoylation levels, and cells lacking STUbLs display genomic instability and hypersensitivity to genotoxic stress. The human STUbL, RNF4, is implicated in several diseases including cancer, highlighting the importance of characterizing the cellular functions of STUbLs.
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U2 - 10.1016/j.tibs.2008.02.001
DO - 10.1016/j.tibs.2008.02.001
M3 - Review article
C2 - 18403209
AN - SCOPUS:43849093519
SN - 0968-0004
VL - 33
SP - 201
EP - 208
JO - Trends in Biochemical Sciences
JF - Trends in Biochemical Sciences
IS - 5
ER -