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A novel SUMO1-specific interacting motif in dipeptidyl peptidase 9 (DPP9) that is important for enzymatic regulation.
Pilla, Esther; Möller, Ulrike; Sauer, Guido; Mattiroli, Francesca; Melchior, Frauke; Geiss-Friedlander, Ruth.
Afiliação
  • Pilla E; Department of Biochemistry I, Faculty of Medicine, Georg-August-University of Goettingen, Humboldtallee 23, 37073 Goettingen, Germany.
J Biol Chem ; 287(53): 44320-9, 2012 Dec 28.
Article em En | MEDLINE | ID: mdl-23152501
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 Glu(67) 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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteína SUMO-1 / Dipeptidil Peptidases e Tripeptidil Peptidases Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Alemanha

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteína SUMO-1 / Dipeptidil Peptidases e Tripeptidil Peptidases Limite: Humans Idioma: En Revista: J Biol Chem Ano de publicação: 2012 Tipo de documento: Article País de afiliação: Alemanha