TRIM33

Last update 08 May 2025

Basic Info

Synonyms

E3 ubiquitin-protein ligase TRIM33, Ectodermin homolog, FLJ11429

+ [18]

Introduction

Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF-beta/BMP signaling cascade).

100 Clinical Results associated with TRIM33

100 Translational Medicine associated with TRIM33

0 Patents (Medical) associated with TRIM33

307

Literatures (Medical) associated with TRIM33

01 Aug 2025·Tissue and Cell

Trim33 inhibited the growth and relieved the fibrosis of mesangial cells through inducing the ubiquitination degradation of Smad2

Article

Author: Zhang, Yong ; Liu, Zhiyuan ; Li, Hongzhou

BACKGROUNDDiabetic nephropathy (DN) poses a significant global health burden due to its progressive nature leading to end-stage renal disease and increased mortality rates. Here, we explored the effects of Tripartite Motif Containing 33 (Trim33) on cell viability and fibrosis of mesangial cells (MCs).METHODSMCs were treated with 30 mM D-glucose (HG) and mice were injected with 50 mg/kg STZ to establish the DN model. Cell growth were detected by CCK-8 and EdU staining. The protein levels of fibronectin (FN), Collagen IV (Col-IV), α-SMA, Smad2, Smad3 and Smad4 were tested by western blot. Furthermore, the interaction between Trim33 and Smad2 were tested by Immunoprecipitation. Wild-type and mutation type of ubiquitin was used to analyze the ubiquitination levels of Smad2. Finally, the injury of kidneys in DN mice were observed by HE staining.RESULTSTrim33 was down regulated in HG treated MCs and DN mice. Trim33 verexpression decreased the cell viability and proliferation of MCs. Besides, the protein levels of FN, Col-IV, α-SMA, Smad2, Smad3 and Smad4 were decreased after Trim33 overexpression in vivo and in vitro. Furthermore, CO-IP assay confirmed that Trim33 interacted with Smad2. Trim33 regulated the Smad2 ubiquitination through the K48 site of Ub. Trim33 overexpression induced the protein degradation of Smad2. Additionally, Smad2 overexpression reversed the effects of Trim33 on the growth and fibrosis of HG treated MCs.CONCLUSIONThis study demonstrated that Trim33 overexpression inhibited the growth and fibrosis progression in HG treated MCs through inducing the ubiquitination degradation of Smad2 protein.

01 Apr 2025·Seminars in Arthritis and Rheumatism

Established and novel insights to guide cancer assessment in patients with idiopathic inflammatory myopathies

Article

Author: Selmi, Carlo ; Isailovic, Natasa ; Tonutti, Antonio ; Ceribelli, Angela ; De Santis, Maria

OBJECTIVEOlder age, dermatomyositis, and specific serum autoantibodies such as anti-TIF1-γ are associated with higher cancer risk in patients with myositis. We evaluated a vast cohort of patients with myositis for the prevalence of cancer, the association to disease features, and the performance of the recent IMACS guidelines.METHODSA retrospective cohort analysis was performed and in all cases serum autoantibodies were tested using HEp-2, immunoassays, RNA- and protein-immunoprecipitation. Myositis was defined as cancer-associated if malignancy occurred within 3 years prior to or after the onset of myositis.RESULTSNinety-five patients with IIM were followed-up for a median of 6 years (interquartile range 3-11), the majority were classified as 'high-risk' or 'intermediate-risk' of cancer based on IMACS guidelines. A diagnosis of cancer was made in 22/95 (23 %) of cases and, based on the timing of the diagnosis, 14 % patients were cancer-associated myositis, with no significant differences compared to patients without cancer. Both groups of patients with overall cancer and cancer-associated myositis had more respiratory comorbidities, anemia, and hypergammaglobulinemia, and dermatomyositis phenotype. Anti-TIF1-γ antibody positivity predicted cancer-associated myositis but not the overall cancer rate; malignancy was observed in particular in patients with isolated anti-TIF1-γ antibodies, while a lower prevalence occurred in case of additional specificities identified by immunoprecipitation.CONCLUSIONSRecent IMACS guidelines perform well in the interception of cancer, yet adjunctive history and laboratory features should be considered. Patients with anti-TIF1-γ antibodies are at risk of cancer-associated myositis, but concurrent autoantibodies negatively correlate with malignancy and warrant characterization.

01 Mar 2025·Biochemical and Biophysical Research Communications

Discovery of myeloid zinc finger (MZF) 1 nuclear bodies

Article

Author: Calderwood, Stuart K ; Eguchi, Takanori

Myeloid zinc finger 1 (MZF1) is a multifaceted transcription factor that can act either as a transcriptional activator or a gene repressor. We examined its production of nuclear bodies (NBs) and subcellular localization. Proteomic and protein-protein interaction analysis were used to identify its cofactors and interactions. These revealed the presence of MZF1-NBs (intranuclear oligomers containing MZF1). MZF-NBs are similar to some other nuclear bodies, notably promyelocytic leukemia (PML) -NBs in terms of size and morphology. However the two structures appear to be different. MZF-NBs and PML-NBs were found to associate in the nucleus. Both MZF1 and PML are SUMO1-SUMOylated in PC-3 cells. Sumoylated MZF1 can interact with proteins containing SUMO-interaction motifs (SIM) through SUMO-SIM interaction. Interactome analysis revealed that its NBs participate in the stress response (TPR and UBAP2L), protein folding (CALR and ANKRD40), transcription, post-translational modification (TRIM33, ACOT7, CAMK2D, and CAMK2G), and RNA binding (ALURBP and CPSF5).

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TRIM33

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