A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that Is important for enzymatic regulation
Sumoylation affects many cellular processes by regulating the interactions of modified targets with downstream effectors. Here we identified the cytosolic dipeptidyl peptidase 9 (DPP9) as a SUMO1 interacting protein. Surprisingly, DPP9 binds to SUMO1 independent of the well known SUMO interacting mo...
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| Hauptverfasser: | , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
November 14, 2012
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| In: |
The journal of biological chemistry
Year: 2012, Jahrgang: 287, Heft: 53, Pages: 44320-44329 |
| ISSN: | 1083-351X |
| DOI: | 10.1074/jbc.M112.397224 |
| Online-Zugang: | Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1074/jbc.M112.397224 Verlag, kostenfrei, Volltext: http://www.jbc.org/content/287/53/44320 
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| Verfasserangaben: | Esther Pilla, Ulrike Möller, Guido Sauer, Francesca Mattiroli, Frauke Melchior, and Ruth Geiss-Friedlander |
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| 245 | 1 | 2 | |a A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that Is important for enzymatic regulation |c Esther Pilla, Ulrike Möller, Guido Sauer, Francesca Mattiroli, Frauke Melchior, and Ruth Geiss-Friedlander |
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| 520 | |a Sumoylation affects many cellular processes by regulating the interactions of modified targets with downstream effectors. Here we identified the cytosolic dipeptidyl peptidase 9 (DPP9) as a SUMO1 interacting protein. Surprisingly, DPP9 binds to SUMO1 independent of the well known SUMO interacting motif, but instead interacts with a loop involving Glu67 of SUMO1. Intriguingly, DPP9 selectively associates with SUMO1 and not SUMO2, due to a more positive charge in the SUMO1-loop. We mapped the SUMO-binding site of DPP9 to an extended arm structure, predicted to directly flank the substrate entry site. Importantly, whereas mutants in the SUMO1-binding arm are less active compared with wild-type DPP9, SUMO1 stimulates DPP9 activity. Consistent with this, silencing of SUMO1 leads to a reduced cytosolic prolyl-peptidase activity. Taken together, these results suggest that SUMO1, or more likely, a sumoylated protein, acts as an allosteric regulator of DPP9. | ||
| 650 | 4 | |a Dipeptidyl Peptidase | |
| 650 | 4 | |a Peptidases | |
| 650 | 4 | |a Post-translational Modification | |
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| 650 | 4 | |a SUMO-interacting Motif (SIM) | |
| 650 | 4 | |a Sumoylation | |
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