Ask about this productRelated genes to: KIAA0157 antibody
- Gene:
- ABRAXAS2 NIH gene
- Name:
- abraxas 2, BRISC complex subunit
- Previous symbol:
- KIAA0157, FAM175B
- Synonyms:
- Em:AC068896.4, ABRO1
- Chromosome:
- 10q26.13
- Locus Type:
- gene with protein product
- Date approved:
- 2004-03-16
- Date modifiied:
- 2017-04-27
Related products to: KIAA0157 antibody
Related articles to: KIAA0157 antibody
- Dipeptidyl 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. - Source: PubMed
Publication date: 2026/02/04
Wirtgen Valentina ElenaSaied LaylaZolg SamuelAlonso Marta CamposMayer BettinaDonzelli LauraMaurer UlrichTimmers H T MarcKnobeloch Klaus-PeterKleifeld OdedGeiss-Friedlander Ruth - The Tumour Protein D52 (TPD52) family, including TPD52, TPD52L1, and TPD52L2, plays critical roles in membrane trafficking, lipid metabolism, and oncogenic signalling, with its overexpression linked to multiple cancers. Phosphorylation is a key regulator of their functions, yet their phosphoproteomic landscape remains underexplored. This study integrates over 3,825 public human phosphoproteomic datasets to map phosphorylation profiles of TPD52, TPD52L1, and TPD52L2, identifying dominant phosphosites like S171, S176, S149, and S12, S166 within conserved coiled-coil and PEST-like domains. CAMK2D was identified as a predominant shared kinase, alongside CDK2 and GRK5, associating these modifications with calcium signaling, cell cycle progression, and cytoskeletal remodeling. Co-phosphoregulation highlighted positive interactions with ABRAXAS2 and negative correlations with ABLIM3, implicating involvement in ubiquitin-mediated degradation, epithelial-mesenchymal transition (EMT), and cytokinesis. Notably, hypophosphorylation at TPD52_S171/S176 was observed in hepatocellular and lung carcinomas, whereas hyperphosphorylation at TPD52L2_S166 prevailed in ovarian and pancreatic cancers, underscoring biomarker utility. Phosphorylation-driven interactomes emphasized roles in vesicular trafficking and oncogenesis This study catalogues the phosphorylation events and explores the potential of TPD52 family as a phosphoregulated hub in cancer biology, with CAMK2D as a potential therapeutic target. - Source: PubMed
Publication date: 2025/12/09
Khan Noreen AFahma AmalMahin AlthafGopalakrishnan Athira PerunellyShivamurthy Prathik BasthikoppaRajeev Athira CRaju Rajesh - Numerous bacterial pathogens have evolved tactics to interfere with the host ubiquitination network to evade clearance by the innate immune system. Nevertheless, the subtle antagonism between a bacterial ubiquitinase and a host deubiquitinase, through which they modify their respective targets within a multifaceted network, has yet to be characterized. BRCC3 isopeptidase complex (BRISC) is a newly identified K63-specific deubiquitinase complex that plays a crucial role in cellular signaling pathways such as inflammation. NleG, a type III secretion system (T3SS) effector, contains a conserved RING E3 ubiquitin ligase domain that interacts with host ubiquitination machinery, along with a distinct substrate-recognition domain that targets host proteins. Here, one particular variant, NleG6, was identified as mediating K27- and K29-linked polyubiquitination at residues K89 and K114 of ABRAXAS2/FAM175B, a scaffolding protein within the BRISC complex, leading to its degradation through TOLLIP (toll interacting protein)-mediated selective autophagy. Further investigations elucidated that ABRAXAS2 degradation triggered the subsequent degradation of adjacent BRCC3, which in turn, hindered TNIP1/ABIN1 degradation, ultimately inhibiting NFKB/NF-κB (nuclear factor kappa B)-mediated inflammatory responses. This chain of events offers valuable insights into the NFKB activation by the K63-specific deubiquitinating role of BRISC, unveiling how bacteria manipulate ubiquitin regulation and selective autophagy within the BRISC network to inhibit the host's inflammatory response and thus dominate a pathogen-host tug-of-war. 3-MA: 3-methyladenine; A/E: attaching and effacing; ATG7: autophagy related 7; BafA1: bafilomycin A; BNIP3L/Nix: BCL2 interacting protein 3 like; BRISC: BRCC3 isopeptidase complex; Cas9: CRISPR-associated system 9; co-IP: co-immunoprecipitation; CQ: chloroquine; CRISPR: clustered regulatory interspaced short palindromic repeat; DAPI: 4',6-diamidino2-phenylindole; DMSO: dimethyl sulfoxide; DUB: deubiquitinating enzyme; : ; EHEC: enterohemorrhagic ; EPEC: enteropathogenic ; GFP: green fluorescent protein; LEE: locus of enterocyte effacement; MAP1LC3B/LC3: microtubule associated protein 1 light chain 3 beta; MG132: cbz-leu-leu-leucinal; MOI: multiplicity of infection; NBR1: NBR1 autophagy cargo receptor; NC: negative control; NFKB/NF-κB: nuclear factor kappa B; NHCl: ammonium chloride; OPTN: optineurin; SQSTM1/p62: sequestosome 1; sgRNAs: small guide RNAs; T3SS: type III secretion system; TNF: tumor necrosis factor; TOLLIP: toll interacting protein; TRAF: TNF receptor associated factor; TUBB: tubulin beta class I; WCL: whole cell lysate; WT: wide type. - Source: PubMed
Publication date: 2025/02/27
Pan XinmingSun YangyangLiu JiananChen RongZhang ZhenLi CaiyingYao HuochunMa Jiale - The aim of this study was to investigate the endometrial proteomic profiles of patients with polycystic ovary syndrome (PCOS) with and without insulin resistance (IR). We collected 40 endometrial samples, including PCOS-IR ( = 21), PCOS-non-IR ( = 12), and control ( = 7). Data-independent acquisition (DIA)-based proteomics method is used to identify the expressed proteins among the three groups. The correlation between pregnancy outcomes and identified proteins was analyzed by Lasso regression. A total of 5331 proteins were identified, while 275 proteins were differentially expressed in the PCOS vs. control group and 215 proteins were differentially expressed in the PCOS-IR vs. PCOS-non-IR group. Platelet degranulation, neutrophil degranulation, and very long-chain fatty acid catabolic processes have been found to play important roles in the endometrium of patients with PCOS-IR. Lasso regression analysis found that ACTR1A, TSC22D2, CKB, ABRAXAS2, and TAGLN2 were associated with miscarriage in patients with PCOS. ACTR1A and CKB were higher in the PCOS-IR group and were positively correlated with HOMA-IR ( < .05). In this study, a panel of proteins was found to be differently expressed in the endometrium. ACTR1A and CKB may be considered as PCOS-IR candidate biomarkers. - Source: PubMed
Publication date: 2023/02/07
Yang XinXiaoping WangNan DingJian ZhangXiaofeng LiLiwei YuanZhao MengniWang Fang - BRCA1/BRCA2-containing complex subunit 3 (BRCC3) is a lysine 63-specific deubiquitinase involved in multiple biological processes, such as DNA repair and immune responses. However, the regulation mechanism for BRCC3 protein stability is still unknown. Here, we demonstrate that BRCC3 is mainly degraded through the ubiquitin-proteasome pathway. The HECT-type E3 ubiquitin ligase WWP2 modulates BRCC3 ubiquitination and degradation. ABRO1, a subunit of the BRCC36 isopeptidase complex (BRISC), competes with WWP2 to bind to BRCC3, thereby preventing WWP2-mediated BRCC3 ubiquitination and enhancing BRCC3 stability. Functionally, we show that lentivirus-mediated overexpression of WWP2 in murine macrophages inhibits NLRP3 inflammasome activation by decreasing BRCC3 protein level. This study provides the first insights into the regulation of BRCC3 stability and expands our knowledge about the physiological function of WWP2. - Source: PubMed
Publication date: 2020/11/08
Zhang WenTao Shou-SongWang TingZhang JieLiu XianLi Ya-TingChen HuiZhan Yi-QunYu MiaoGe Chang-HuiLi Chang-YanRen Guang-MingYang Xiao-MingYin Rong-Hua