PMID- 10652325
OWN - NLM
STAT- MEDLINE
DCOM- 20000302
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 275
IP  - 5
DP  - 2000 Feb 4
TI  - Differential regulation of sentrinized proteins by a novel sentrin-specific
      protease.
PG  - 3355-9
AB  - Sentrin-1, also called SUMO-1, is a protein of 101 residues that is distantly
      related to ubiquitin and another ubiquitin-like protein, NEDD8. Here we report
      the cloning of a novel sentrin-specific protease, SENP1, which has no homology to
      the known de-ubiquitinating enzymes or ubiquitin C-terminal hydrolases. However, 
      SENP1 is distantly related to the yeast Smt3-specific protease, Ulp1. A COS cell 
      expression system was used to demonstrate the activity of SENP1 in vivo. When
      HA-tagged sentrin-1 was co-expressed with SENP1, the higher molecular weight
      sentrin-1 conjugates were completely removed. Surprisingly, the major sentrinized
      band at 90 kDa remained intact. The disappearance of the high molecular weight
      sentrin-1 conjugates also coincided with an increase in free sentrin-1 monomers. 
      SENP1 is also active against proteins modified by sentrin-2, but not those
      modified by ubiquitin or NEDD8. In addition, sentrinized PML, a tumor suppressor 
      protein that resides in the nucleus, was selectively affected by SENP1, whereas
      sentrinized RanGAP1, which is associated with the cytoplasmic fibrils of the
      nuclear pore complex, remained intact. The inability of SENP1 to process
      sentrinized RanGAP1 in vivo is most likely due to its nuclear localization
      because SENP1 is active against sentrinized RanGAP1 in vitro. The identification 
      of a nuclear-localized, sentrin-specific protease will provide a unique tool to
      study the role of sentrinization in the biological function of PML and in the
      pathogenesis of acute promyelocytic leukemia.
FAU - Gong, L
AU  - Gong L
AD  - Research Center for Cardiovascular Diseases, Institute of Molecular Medicine for 
      the Prevention of Human Diseases, Division of Molecular Medicine, The University 
      of Texas-Houston Health Science, Houston, USA.
FAU - Millas, S
AU  - Millas S
FAU - Maul, G G
AU  - Maul GG
FAU - Yeh, E T
AU  - Yeh ET
LA  - eng
SI  - GENBANK/AF149770
GR  - GM-57502/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA, Complementary)
RN  - 0 (Repressor Proteins)
RN  - 0 (SUMO-1 Protein)
RN  - 0 (Ubiquitins)
RN  - EC 3.4.- (Endopeptidases)
RN  - EC 3.4.- (SENP1 protein, human)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - COS Cells
MH  - Cloning, Molecular
MH  - Cysteine Endopeptidases
MH  - DNA, Complementary/genetics/isolation & purification
MH  - Endopeptidases/*genetics/*metabolism
MH  - Molecular Sequence Data
MH  - Repressor Proteins
MH  - SUMO-1 Protein
MH  - Sequence Alignment
MH  - Substrate Specificity
MH  - Ubiquitins/*metabolism
EDAT- 2000/02/01 09:00
MHDA- 2000/05/20 09:00
CRDT- 2000/02/01 09:00
PHST- 2000/02/01 09:00 [pubmed]
PHST- 2000/05/20 09:00 [medline]
PHST- 2000/02/01 09:00 [entrez]
AID - 10.1074/jbc.275.5.3355 [doi]
PST - ppublish
SO  - J Biol Chem. 2000 Feb 4;275(5):3355-9. doi: 10.1074/jbc.275.5.3355.