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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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Bibliographic Details
Main Authors: Pilla, Esther (Author) , Melchior, Frauke (Author)
Format: Article (Journal)
Language:English
Published: November 14, 2012
In: The journal of biological chemistry
Year: 2012, Volume: 287, Issue: 53, Pages: 44320-44329
ISSN:1083-351X
DOI:10.1074/jbc.M112.397224
Online Access: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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Author Notes:Esther Pilla, Ulrike Möller, Guido Sauer, Francesca Mattiroli, Frauke Melchior, and Ruth Geiss-Friedlander
Description
Summary: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.
Item Description:Gesehen am 30.08.2018
Physical Description:Online Resource
ISSN:1083-351X
DOI:10.1074/jbc.M112.397224

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