The cytoplasmic peptidase DPP9 Is rate-limiting for degradation of proline-containing peptides

• Verfasst von: Geiss-Friedlander, Ruth [VerfasserIn]
• Verfasst von: Parmentier, Nicolas [VerfasserIn]
• Verfasst von: Möller, Ulrike [VerfasserIn]
• Verfasst von: Urlaub, Henning [VerfasserIn]
• Verfasst von: Eynde, Benoit van den [VerfasserIn]
• Verfasst von: Melchior, Frauke [VerfasserIn]
• Titel: The cytoplasmic peptidase DPP9 Is rate-limiting for degradation of proline-containing peptides
• Verf.angabe: Ruth Geiss-Friedlander, Nicolas Parmentier, Ulrike Möller, Henning Urlaub, Benoit J. Van den Eynde, and Frauke Melchior
• E-Jahr: 2009
• Jahr: October 2009
• Umfang: 9 S.
• Fussnoten: Gesehen am 04.09.2023
• Titel Quelle: Enthalten in: The journal of biological chemistry
• Ort Quelle: Bethesda, Md. : ASBMB Publications, 1905
• Jahr Quelle: 2009
• Band/Heft Quelle: 284(2009), 40 vom: Okt., Seite 27211-27219
• ISSN Quelle: 1083-351X
• DOI: doi:10.1074/jbc.M109.041871
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1858760763

Abstract

Protein degradation is an essential process that continuously takes place in all living cells. Regulated degradation of most cellular proteins is initiated by proteasomes, which produce peptides of varying length. These peptides are rapidly cleaved to single amino acids by cytoplasmic peptidases. Proline-containing peptides pose a specific problem due to structural constrains imposed by the pyrrolidine ring that prevents most peptidases from cleavage. Here we show that DPP9, a poorly characterized cytoplasmic prolyl-peptidase, is rate-limiting for destruction of proline-containing substrates both in cell extracts and in intact cells. We identified the first natural substrate for DPP9, the RU134-42 antigenic peptide (VPYGSFKHV). RU134-42 is degraded in vitro by DPP9, and down-regulation of DPP9 in intact cells results in increased presentation of this antigen. Together our findings demonstrate an important role for DPP9 in peptide turnover and antigen presentation.