PMID- 18922472
OWN - NLM
STAT- MEDLINE
DCOM- 20081030
LR  - 20201209
IS  - 1097-4164 (Electronic)
IS  - 1097-2765 (Print)
IS  - 1097-2765 (Linking)
VI  - 31
IP  - 6
DP  - 2008 Sep 26
TI  - Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the 
      proteasome and in the Ino80 chromatin-remodeling complex.
PG  - 909-17
LID - 10.1016/j.molcel.2008.08.027 [doi]
AB  - Deubiquitinating enzymes (DUBs) are proteases that can antagonize 
      ubiquitin-mediated signaling by disassembling ubiquitin-protein conjugates. How 
      DUBs are regulated in vivo and how their substrate specificities are achieved are 
      largely unknown. The conserved DUB Uch37 is found on proteasomes in organisms 
      ranging from fission yeast to humans. Deubiquitination by Uch37 is activated by 
      proteasomal binding, which enables Uch37 to process polyubiquitin chains. Here we 
      show that in the nucleus Uch37 is also associated with the human Ino80 
      chromatin-remodeling complex (hINO80). In hINO80, Uch37 is held in an inactive 
      state; however, it can be activated by transient interaction of the Ino80 complex 
      with the proteasome. Thus, DUB activities can be modulated both positively and 
      negatively via dynamic interactions with partner proteins. In addition, our 
      findings suggest that the proteasome and the hINO80 chromatin-remodeling complex 
      may cooperate to regulate transcription or DNA repair, processes in which both 
      complexes have been implicated.
FAU - Yao, Tingting
AU  - Yao T
AD  - Stowers Institute for Medical Research, Kansas City, MO 64110, USA.
FAU - Song, Ling
AU  - Song L
FAU - Jin, Jingji
AU  - Jin J
FAU - Cai, Yong
AU  - Cai Y
FAU - Takahashi, Hidehisa
AU  - Takahashi H
FAU - Swanson, Selene K
AU  - Swanson SK
FAU - Washburn, Michael P
AU  - Washburn MP
FAU - Florens, Laurence
AU  - Florens L
FAU - Conaway, Ronald C
AU  - Conaway RC
FAU - Cohen, Robert E
AU  - Cohen RE
FAU - Conaway, Joan W
AU  - Conaway JW
LA  - eng
GR  - R01 GM037666-18/GM/NIGMS NIH HHS/United States
GR  - R01 GM37666/GM/NIGMS NIH HHS/United States
GR  - R01 GM037666/GM/NIGMS NIH HHS/United States
GR  - R37 GM41628/GM/NIGMS NIH HHS/United States
GR  - R37 GM041628-21/GM/NIGMS NIH HHS/United States
GR  - R37 GM041628/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PL  - United States
TA  - Mol Cell
JT  - Molecular cell
JID - 9802571
RN  - 0 (ADRM1 protein, human)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (NFRKB protein, human)
RN  - 0 (Protein Subunits)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.19.12 (UCHL5 protein, human)
RN  - EC 3.4.19.12 (Ubiquitin Thiolesterase)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - EC 3.6.4.- (ATPases Associated with Diverse Cellular Activities)
RN  - EC 3.6.4.- (DNA Helicases)
RN  - EC 3.6.4.- (INO80 protein, human)
SB  - IM
CIN - Mol Cell. 2008 Sep 26;31(6):773-4. PMID: 18922460
MH  - ATPases Associated with Diverse Cellular Activities
MH  - Carboxypeptidases/antagonists & inhibitors/chemistry/*metabolism
MH  - Cell Line
MH  - *Chromatin Assembly and Disassembly
MH  - DNA Helicases/*metabolism
MH  - DNA-Binding Proteins/metabolism
MH  - Enzyme Activation
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Membrane Glycoproteins/metabolism
MH  - Proteasome Endopeptidase Complex/*metabolism
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Protein Subunits/metabolism
MH  - Ubiquitin Thiolesterase
PMC - PMC2577292
MID - NIHMS71747
EDAT- 2008/10/17 09:00
MHDA- 2008/10/31 09:00
PMCR- 2009/09/26
CRDT- 2008/10/17 09:00
PHST- 2007/11/07 00:00 [received]
PHST- 2008/05/25 00:00 [revised]
PHST- 2008/08/13 00:00 [accepted]
PHST- 2008/10/17 09:00 [pubmed]
PHST- 2008/10/31 09:00 [medline]
PHST- 2008/10/17 09:00 [entrez]
PHST- 2009/09/26 00:00 [pmc-release]
AID - S1097-2765(08)00615-1 [pii]
AID - 10.1016/j.molcel.2008.08.027 [doi]
PST - ppublish
SO  - Mol Cell. 2008 Sep 26;31(6):909-17. doi: 10.1016/j.molcel.2008.08.027.