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Characterization of SENP7, a SUMO-2/3-specific isopeptidase.
| Content Provider | Semantic Scholar |
|---|---|
| Author | Shen, Lin Nan Geoffroy, Marie-Claude Jaffray, Ellis G. Hay, Ronald Thomas |
| Copyright Year | 2009 |
| Abstract | The modification of proteins by SUMO (small ubiquitin-related modifier) plays important roles in regulating the activity, stability and cellular localization of target proteins. Similar to ubiquitination, SUMO modification is a dynamic process that can be reversed by SENPs [SUMO-1/sentrin/SMT3 (suppressor of mif two 3 homologue 1)-specific peptidases]. To date, six SENPs have been discovered in humans, although knowledge of their regulation, specificity and biological functions is limited. In the present study, we report that SENP7 has a restricted substrate specificity, being unable to process SUMO precursors and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 efficiently depolymerized poly-SUMO-2 chains but had undetectable activity against poly-SUMO-1 chains. SENP7 also displayed isopeptidase activity against di-SUMO-2- and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1. in vivo, full-length SENP7 was localized to the nucleoplasm and preferentially reduced the accumulation of high-molecular-mass conjugates of SUMO-2 and SUMO-3 compared with SUMO-1. Small interfering RNA-mediated ablation of SENP7 expression led to the accumulation of high-molecular-mass SUMO-2 species and to the accumulation of promyelocytic leukaemia protein in subnuclear bodies. These findings suggest that SENP7 acts as a SUMO-2/3-specific protease that is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo. |
| Starting Page | 70 |
| Ending Page | 77 |
| Page Count | 8 |
| File Format | PDF HTM / HTML |
| Alternate Webpage(s) | http://www.biochemj.org/content/ppbiochemj/421/2/223.full.pdf |
| Alternate Webpage(s) | http://gre.lifesci.dundee.ac.uk/publications/Ron%20Hay%202008%202009%202010%202011/2009_characterization..biochemical_journal.pdf |
| Alternate Webpage(s) | http://gre.lifesci.dundee.ac.uk/publications/2009/PMID_19392659_Shen_Hay_2009.pdf |
| PubMed reference number | 19392659v1 |
| Alternate Webpage(s) | https://doi.org/10.1042/BJ20090246 |
| DOI | 10.1042/bj20090246 |
| Journal | The Biochemical journal |
| Volume Number | 421 |
| Issue Number | 2 |
| Language | English |
| Access Restriction | Open |
| Subject Keyword | Catalytic Domain Chemical Modifier Endopeptidases Homologous Gene Immunostimulating conjugate (antigen) Nucleoplasm Peptide Hydrolases Poly A Poly Adenosine Diphosphate Ribose RAN GTPase Activating Protein 1 RNA SENP7 gene SUMO-1 Protein USP13 gene Ubiquitination Undetectable cellular localization isopeptidase activity leukemia |
| Content Type | Text |
| Resource Type | Article |
