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J. Biol. Chem., Vol. 276, Issue 42, 39060-39066, October 19, 2001
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From the School of Life Science, Tokyo University of Pharmacy and
Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392 and the
A novel SUMO-1/Smt3-specific isopeptidase,
SMT3IP2/Axam2 (Smt3-specific isopeptidase 2), was cloned and
characterized. The catalytic domains in the carboxyl-terminal region
were very much similar to those of other SUMO-1/Smt3-specific
proteases, but the amino-terminal part was quite different. The enzyme
specifically bound to Smt3a and Smt3b but not to SUMO-1. The SMT3IP2
expressed by Escherichia coli could cleave SUMO-1, Smt3a,
or Smt3b from a SUMO-1/RanGAP1, Smt3a/RanGAP1, or Smt3b/RanGAP1
conjugate, respectively, and had the activity of a carboxyl-terminal
hydrolase to produce a glycine residue in the carboxyl terminus of
these ubiquitin-like proteins. The sequence data indicated that the
amino acid sequence of SMT3IP2 was mostly identical to that of rat
Axam, which binds to Axin and promotes the degradation of The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF368904, AF151697, AF260129, AI390987, AI152880, and
AI664083.
Characterization of a Novel Mammalian
SUMO-1/Smt3-specific Isopeptidase, a Homologue of Rat Axam, Which Is an
Axin-binding Protein Promoting
-Catenin Degradation*
, and Department of Biochemistry 1, Hamamatsu University School
of Medicine, 1-20-1 Handayama, Hamamatsu 431-3192, Japan
-catenin,
although its amino-terminal region was much shorter than that of Axam.
Therefore, we designated this isopeptidase SMT3IP2/Axam2. When human
SW480 cells were transfected with wild-type SMT3IP2/Axam2, the
-catenin disappeared. When the cells were transfected with the
SMT3IP2/Axam2 C500A mutant, which had neither isopeptidase nor
carboxyl-terminal hydrolase activity, or with the 1-352 mutant, which
lacked the catalytic domain of the enzyme, again the -catenin
disappeared, indicating that the enzyme activities were not necessary
for the instability of -catenin in this transfection assay system
and that its competition with Dvl for binding to Axin may be important for the instability of -catenin as suggested previously for Axam (Kadoya, T., Kishida, S., Fukui, A., Hinoi, T., Michiue, T.,
Asashima, M., and Kikuchi, A. (2000) J. Biol.
Chem. 275, 37030-37037). The involvement of its enzyme
activities in the Wnt signaling pathway remains to be elucidated.
*
This work was supported in part by the Scientific Grant from
the Ministry of Education, Science, Sports and Technology, Japan. This
work was also supported by the Uehara Memorial Foundation and Sagawa
Cancer Research Fund (to H. Y.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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