Ask about this productRelated genes to: TRIM37 antibody
- Gene:
- TRIM37 NIH gene
- Name:
- tripartite motif containing 37
- Previous symbol:
- MUL
- Synonyms:
- KIAA0898, POB1, TEF3
- Chromosome:
- 17q22
- Locus Type:
- gene with protein product
- Date approved:
- 1995-09-08
- Date modifiied:
- 2016-01-15
Related products to: TRIM37 antibody
Related articles to: TRIM37 antibody
- Polo-like kinase 4 (PLK4) is a key regulator of centriole duplication and contributes to mitotic spindle organization during cell division. PLK4 has been implicated as pharmacological target in a subset of breast cancers and neuroblastomas harboring 17q chromosomal gains and overexpression of the E3 ubiquitin-protein ligase TRIM37. Here, we investigated factors that influence sensitivity of cancer cells to PLK4 inhibition. - Source: PubMed
Publication date: 2026/06/18
Stoyanov MiroslavAquino-Perez CeciliaMazumder ShreyasiSalcakova DominikaPetrezselyova SilviaMacurek Libor - Tripartite motif-containing 37 protein (TRIM37), a member of the TRIM protein family, functions as an E3 ubiquitin ligase. It was implicated in the pathogenesis of numerous malignancies. Nonetheless, its precise function in hepatocellular carcinoma (HCC) is still insufficiently understood. This study aims to elucidate the regulatory function of TRIM37 in HCC progression and to explore the underlying molecular mechanisms. - Source: PubMed
Publication date: 2026/05/27
Wang QingqingZhang XiaojianZhang Jie - It was recently shown that inhibition of polo-like kinase 4 (PLK4) induces synthetic lethality in cancers with chromosome 17q-encoded TRIM37 copy number gain due to cooperative regulation of centriole duplication and mitotic spindle nucleation. We show here that chromosome 17q/TRIM37 gain is a defining feature of high-risk neuroblastoma and renders patient-derived cell lines hypersensitive to the novel PLK4 inhibitor RP-1664. We demonstrate that centriole amplification at low doses of RP-1664 contributes to this sensitivity in a TRIM37-independent fashion. CRISPR screens and live cell imaging reveal that upon centriole amplification, neuroblastoma cells succumb to multipolar mitoses due to an inability to cluster or inactivate supernumerary centrosomes. RP-1664 monotherapy showed robust anti-tumor activity in 14/15 human neuroblastoma-derived xenograft models, and significantly extended survival in a transgenic MYCN-driven murine model of neuroblastoma. RP-1664 combined with GD2-directed chemoimmunotherapy resulted in maintained complete responses in 6/9 mice with established MYCN-driven murine neuroblastomas. These data support clinical development of PLK4 inhibitors for high-risk neuroblastoma and other cancers with somatically acquired TRIM37 overexpression. - Source: PubMed
Publication date: 2026/06/13
Soria-Bretones IsabelCasás-Selves MatiasSamanta MinuGroff DavidMurray JayneFletcher Jamie IFarrel AlvinPastor StevenPatel KhushbuGoodfellow ElliotLi LiCaron CathyShiwram AriyaKim HyeyeonHenry DanielleLaterreur NancyBowlan JulianKrytska KaterynaNeuhauser Steven BStearns Timothy MSchubert Jeffrey AWu JinhuaSurrey Lea FMartinez DanielMak CrystalBrand JenniferWesley CaitlinSomers KlaartjeÁlvarez-Quilón AlejandroVallée FrédéricNejad ParhamSchonhoft Joseph DLi JoannaVeloso ArturYoung Jordan T FHyer Marc LMorris Stephen JMossé Yael PMarshall C GaryHaber MichelleZimmermann MichalMaris John M - Kaposi sarcoma-associated herpesvirus (KSHV), an oncogenic virus associated with several malignancies, including Kaposi sarcoma (KS), primary effusion lymphoma (PEL), and multicentric Castleman disease, harbors a DNA replication helicase encoded by ORF44 that is crucial for viral replication and pathogenesis. In this study, we identified the host PFN1 (profilin 1), a well-known actin-binding factor, as an inhibitor of KSHV lytic replication functioning via the macroautophagy/autophagy-lysosomal degradation pathway targeting ORF44. Mechanistic analyses revealed that PFN1 interacts with ORF44, leading to enhanced polyubiquitination of PFN1. Notably, the E3 ubiquitin ligase TRIM37 (tripartite motif containing 37) facilitates the polyubiquitination of lysine residues at position 116 of PFN1, which serves as a critical recognition motif for the cargo receptor SQSTM1/p62 (sequestosome 1), which is pivotal for the subsequent autophagic degradation of ORF44. Overall, our findings revealed a previously uncharacterized antiviral function of PFN1, highlighting its potential as a novel therapeutic avenue for the treatment of KSHV-associated malignancies. ALS: amyotrophic lateral sclerosis; Baf A1: bafilomycin A; co-IP: co-immunoprecipitation; KSHV: Kaposi sarcoma-associated herpes virus; LIR: LC3-interacting region; PFN1: profilin 1; SQSTM1/p62: sequestosome 1; TRIM37: tripartite motif containing 37; UBA: ubiquitin-associated domain. - Source: PubMed
Publication date: 2026/06/14
Sun XiaoyiDong JiazhenLiang XiaoweiPeng JiangweiChen YuncaiYin RuiTan TaoBai LeiLan Ke - Centrosomes are key microtubule-organizing centers required for accurate spindle assembly and chromosome segregation, and their dysfunction in cancer creates therapeutic vulnerabilities. Prior work identified a synthetic lethal interaction between TRIM37 overexpression and Polo-like kinase 4 inhibition (PLK4i) in 17q23-amplified tumors, motivating the clinical development of centrosome-depleting PLK4 inhibitors. However, the broader determinants of sensitivity and resistance to PLK4 inhibition remain poorly defined. Using genome-wide CRISPR-Cas9 screening, we identify multiple genetic suppressors of sensitivity to centrosome depletion, including loss of as a general escape mechanism, mediated by enhanced activation of Aurora kinase A (AURKA) on the spindle. This process requires NuMA, which scaffolds robust acentrosomal spindle assembly, and operates independently of the TRIM37-regulated pathway that restores pericentriolar material (PCM) foci to reconstitute microtubule-organizing center activity. We further show that centrosome depletion creates a dependence on the AURKA-TPX2 axis for spindle assembly, such that modulation of this pathway shapes cellular responses to PLK4 inhibition. Loss of PPP6C elevates AURKA activity and confers resistance, whereas disruption of the AURKA-TPX2 axis sensitizes cells to centrosome depletion. Together, these findings reveal how centrosome depletion rewires mitotic organization, rendering cells dependent on distinct adaptive spindle assembly pathways. - Source: PubMed
Publication date: 2026/05/06
Yeow Zhong YChang Fang-ChiXu Lance YHolland Andrew J