Structural plasticity allows UCH37 to be primed by RPN13 or locked down by INO80G.
Two studies in this issue of Molecular Cell,VanderLinden et al. (2015) and Sahtoe et al. (2015),report crystal structures that define how deubiquitinating enzyme UCH37 is switched on or off by proteasome ubiquitin receptor RPN13 or chromatin remodeler component INO80G.
Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA.
Xiang
X
Chen
Protein Processing Section, Structural Biophysics Laboratory, Center for Cancer Research, National Cancer Institute, Frederick, MD 21702, USA. Electronic address: kylie.walters@nih.gov.
Kylie J
KJ
Walters
D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D043222:Ubiquitin Thiolesterase / Q000737:chemistry*
C500781:ADRM1 protein, human; D004268:DNA-Binding Proteins; D047908:Intracellular Signaling Peptides and Proteins; D008562:Membrane Glycoproteins; C072725:NFRKB protein, human; C421245:UCHL5 protein, human; D043222:Ubiquitin Thiolesterase