Reactome | The C-terminal extension of UCHL5 (UCH37) binds to ADRM1, pa...

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created	[InstanceEdit:5665927] Jupe, Steve, 2015-01-20
dbId	5665929
displayName	The C-terminal extension of UCHL5 (UCH37) binds to ADRM1, pa...
literatureReference	[LiteratureReference:5665938] hRpn13/ADRM1/GP110 is a novel proteasome subunit that binds the deubiquitinating enzyme, UCH37 [LiteratureReference:5665836] Mechanism of the Rpn13-induced activation of Uch37 [LiteratureReference:5689577] Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome [LiteratureReference:5689596] A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
modified	[InstanceEdit:8868786] Jupe, Steve, 2016-04-25
schemaClass	Summation
text	The C-terminal extension of UCHL5 (UCH37) binds to ADRM1, part of the proteasomal 19S regulatory subunit which is itself a subunit of the 26S proteasome. Binding of UCHL5 enhances its DUB activity (Qiu et al. 2006). UCHL5 forms oligomers in solution that have very low DUB activity. Binding with ADRM1 is 1:1, preventing oligomerization of UCHL5 while making the active site of UCHL5 accessible to Ubiquitin (Jiao et al. 2014). When associated with the proteasome, UCHL5 disassembles poly-Ub chains by hydrolyzing the distal ubiquitin from a chain. This dissassembly of the degradation signal from only the distal end of polyubiquitin chains may selectively rescue poorly ubiquitinated or slowly degraded Ub-protein conjugates from proteolysis (Lam et al. 1997).

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