000309651 001__ 309651
000309651 005__ 20260205152448.0
000309651 0247_ $$2doi$$a10.1007/s00018-025-06021-z
000309651 0247_ $$2pmid$$apmid:41636814
000309651 0247_ $$2ISSN$$a1420-682X
000309651 0247_ $$2ISSN$$a0014-4754
000309651 0247_ $$2ISSN$$a1420-9071
000309651 037__ $$aDKFZ-2026-00283
000309651 041__ $$aEnglish
000309651 082__ $$a610
000309651 1001_ $$aWirtgen, Valentina Elena$$b0
000309651 245__ $$aProximity labeling reveals non-catalytic interactions between DPP9 and ubiquitin signaling complexes.
000309651 260__ $$aCham (ZG)$$bSpringer International Publishing AG$$c2026
000309651 3367_ $$2DRIVER$$aarticle
000309651 3367_ $$2DataCite$$aOutput Types/Journal article
000309651 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$bjournal$$mjournal$$s1770301372_2391615
000309651 3367_ $$2BibTeX$$aARTICLE
000309651 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000309651 3367_ $$00$$2EndNote$$aJournal Article
000309651 500__ $$a#DKTKZFB26#
000309651 520__ $$aDipeptidyl peptidase 9 (DPP9) is an amino-peptidase with roles in immunity, DNA-repair, cell signaling, memory and neonatal survival; its dysregulation is linked to cancer and immune-related disorders. While many studies focus on its catalytic activity, scaffolding functions of DPP9 are emerging. Here, we mapped the DPP9 interactome using TurboID-based proximity labeling in DPP9 knock-out HEK293 cells reconstituted with doxycycline-inducible miniTurboID-DPP9, allowing fine-tuned expression that approximates physiological levels. Besides known partners, proteins involved in autophagy, mRNA decay and ubiquitin signaling along with DPP8, were strongly enriched among the identified DPP9 binding partners. Notably, we validated DPP8, the E3 ligase CBL, the deubiquitinase complex CYLD-SPATA2 and the BRISC complex components BRCC36/BRCC3 and ABRO1/ABRAXAS2 as novel DPP9 interactors. Furthermore, NanoBRET assays in living cells demonstrated that DPP9 disrupts the binding between BRCC36/BRCC3 and ABRO1/ABRAXAS2, and the interaction of CYLD with SPATA2, thereby compromising these protein-protein interactions. Mechanistically, these findings reveal physical and potentially regulatory interactions between DPP9 and components of the ubiquitin system and provide a basis for dissecting the non-catalytic functions of DPP9.
000309651 536__ $$0G:(DE-HGF)POF4-899$$a899 - ohne Topic (POF4-899)$$cPOF4-899$$fPOF IV$$x0
000309651 588__ $$aDataset connected to CrossRef, PubMed, , Journals: inrepo02.dkfz.de
000309651 650_7 $$2Other$$aAutophagy
000309651 650_7 $$2Other$$aBRISC complex
000309651 650_7 $$2Other$$aCBL
000309651 650_7 $$2Other$$aCYLD
000309651 650_7 $$2Other$$aDPP8
000309651 650_7 $$2Other$$aMRNA decay
000309651 650_7 $$2Other$$aProximity labeling
000309651 650_7 $$2Other$$aXIAP
000309651 7001_ $$aSaied, Layla$$b1
000309651 7001_ $$aZolg, Samuel$$b2
000309651 7001_ $$aAlonso, Marta Campos$$b3
000309651 7001_ $$aMayer, Bettina$$b4
000309651 7001_ $$aDonzelli, Laura$$b5
000309651 7001_ $$aMaurer, Ulrich$$b6
000309651 7001_ $$0P:(DE-He78)a77f61c7d4ca6aa1f9adc620eed66f3d$$aTimmers, H T Marc$$b7$$udkfz
000309651 7001_ $$aKnobeloch, Klaus-Peter$$b8
000309651 7001_ $$aKleifeld, Oded$$b9
000309651 7001_ $$00000-0002-1720-3440$$aGeiss-Friedlander, Ruth$$b10
000309651 773__ $$0PERI:(DE-600)1458497-9$$a10.1007/s00018-025-06021-z$$gVol. 83, no. 1, p. 93$$n1$$p93$$tCellular and molecular life sciences$$v83$$x1420-682X$$y2026
000309651 9101_ $$0I:(DE-588b)2036810-0$$6P:(DE-He78)a77f61c7d4ca6aa1f9adc620eed66f3d$$aDeutsches Krebsforschungszentrum$$b7$$kDKFZ
000309651 9131_ $$0G:(DE-HGF)POF4-899$$1G:(DE-HGF)POF4-890$$2G:(DE-HGF)POF4-800$$3G:(DE-HGF)POF4$$4G:(DE-HGF)POF$$aDE-HGF$$bProgrammungebundene Forschung$$lohne Programm$$vohne Topic$$x0
000309651 9141_ $$y2026
000309651 915__ $$0StatID:(DE-HGF)3002$$2StatID$$aDEAL Springer$$d2025-11-06$$wger
000309651 915__ $$0StatID:(DE-HGF)3002$$2StatID$$aDEAL Springer$$d2025-11-06$$wger
000309651 915__ $$0StatID:(DE-HGF)0200$$2StatID$$aDBCoverage$$bSCOPUS$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0300$$2StatID$$aDBCoverage$$bMedline$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0320$$2StatID$$aDBCoverage$$bPubMed Central$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0600$$2StatID$$aDBCoverage$$bEbsco Academic Search$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bASC$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0199$$2StatID$$aDBCoverage$$bClarivate Analytics Master Journal List$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)1120$$2StatID$$aDBCoverage$$bBIOSIS Reviews Reports And Meetings$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0160$$2StatID$$aDBCoverage$$bEssential Science Indicators$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0113$$2StatID$$aWoS$$bScience Citation Index Expanded$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0150$$2StatID$$aDBCoverage$$bWeb of Science Core Collection$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)1030$$2StatID$$aDBCoverage$$bCurrent Contents - Life Sciences$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)1050$$2StatID$$aDBCoverage$$bBIOSIS Previews$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0501$$2StatID$$aDBCoverage$$bDOAJ Seal$$d2025-06-06T08:03:23Z
000309651 915__ $$0StatID:(DE-HGF)0500$$2StatID$$aDBCoverage$$bDOAJ$$d2025-06-06T08:03:23Z
000309651 915__ $$0StatID:(DE-HGF)0030$$2StatID$$aPeer Review$$bDOAJ : Anonymous peer review$$d2025-06-06T08:03:23Z
000309651 915__ $$0StatID:(DE-HGF)0561$$2StatID$$aArticle Processing Charges$$d2025-11-06
000309651 915__ $$0StatID:(DE-HGF)0700$$2StatID$$aFees$$d2025-11-06
000309651 9201_ $$0I:(DE-He78)FR01-20160331$$kFR01$$lDKTK Koordinierungsstelle Freiburg$$x0
000309651 980__ $$ajournal
000309651 980__ $$aVDB
000309651 980__ $$aI:(DE-He78)FR01-20160331
000309651 980__ $$aUNRESTRICTED