PMID- 20302916
OWN - NLM
STAT- MEDLINE
DCOM- 20100817
LR  - 20200109
IS  - 0006-3002 (Print)
IS  - 0006-3002 (Linking)
VI  - 1806
IP  - 1
DP  - 2010 Aug
TI  - The potential role of ubiquitin c-terminal hydrolases in oncogenesis.
PG  - 1-6
LID - 10.1016/j.bbcan.2010.03.001 [doi]
AB  - Deubiquitinating enzymes (DUBs), capable of removing ubiquitin (Ub) from protein 
      substrates, are involved in numerous biological processes. The ubiquitin 
      C-terminal hydrolases (UCHs) subfamily of DUBs consists of four members: UCH-L1, 
      UCH-L3, UCH37 and BRCA1-associated protein-1 (BAP1). UCH-L1 possesses 
      deubiquitinating activity and dimerization-dependent ubiquitin ligase activity, 
      and functions as a mono-ubiquitin stabilizer; UCH-L3 does both deubiquitinating 
      and deneddylating activity, except dimerization or ligase activity, and unlike 
      UCH-L1, can interact with Lys48-linked Ub dimers to protect it from degradation 
      and in the meanwhile to inhibit its hydrolase activity; UCH37 is responsible for 
      the deubiquitinating activity in the 19S proteasome regulatory complex, and as 
      indicated by the recent study, UCH37 is also associated with the human Ino80 
      chromatin-remodeling complex (hINO80) in the nucleus and can be activated via 
      transient association of 19S regulatory particle- or proteasome-bound hRpn13 with 
      hINO80; BAP1, binding to the wild-type BRCA1 RING finger domain, is regarded as a 
      tumor suppressor, but for such suppressing activity, as demonstrated otherwise, 
      both deubiquitinating activity and nucleus localization are required. There is 
      growing evidence that UCH enzymes and human malignancies are closely correlated. 
      Previous studies have shown that UCH enzymes play a crucial role in some 
      signalings and cell-cycle regulation. In this review, we provided an insight into 
      the relation between UCH enzymes and oncogenesis.
CI  - Copyright 2010 Elsevier B.V. All rights reserved.
FAU - Fang, Ying
AU  - Fang Y
AD  - Department of Gastroenterology of Zhongshan Hospital, Fudan University, Shanghai, 
      200032, PR China.
FAU - Fu, Da
AU  - Fu D
FAU - Shen, Xi-Zhong
AU  - Shen XZ
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20100317
PL  - Netherlands
TA  - Biochim Biophys Acta
JT  - Biochimica et biophysica acta
JID - 0217513
RN  - 0 (BAP1 protein, human)
RN  - 0 (Tumor Suppressor Proteins)
RN  - 0 (Ubiquitin carboxyl-Terminal Hydrolase L-1, human)
RN  - EC 3.4.- (Carboxypeptidases)
RN  - EC 3.4.19.12 (UCHL3 protein, human)
RN  - EC 3.4.19.12 (UCHL5 protein, human)
RN  - EC 3.4.19.12 (Ubiquitin Thiolesterase)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
SB  - IM
MH  - Animals
MH  - Carboxypeptidases/physiology
MH  - Cysteine Endopeptidases/physiology
MH  - Humans
MH  - Neoplasms/*etiology
MH  - Tumor Suppressor Proteins/physiology
MH  - Ubiquitin Thiolesterase/chemistry/*physiology
RF  - 70
EDAT- 2010/03/23 06:00
MHDA- 2010/08/18 06:00
CRDT- 2010/03/23 06:00
PHST- 2009/10/22 00:00 [received]
PHST- 2010/03/01 00:00 [revised]
PHST- 2010/03/08 00:00 [accepted]
PHST- 2010/03/23 06:00 [entrez]
PHST- 2010/03/23 06:00 [pubmed]
PHST- 2010/08/18 06:00 [medline]
AID - S0304-419X(10)00026-0 [pii]
AID - 10.1016/j.bbcan.2010.03.001 [doi]
PST - ppublish
SO  - Biochim Biophys Acta. 2010 Aug;1806(1):1-6. doi: 10.1016/j.bbcan.2010.03.001. 
      Epub 2010 Mar 17.