TRIM60

Last update 08 May 2025

Basic Info

Synonyms

FLJ35882, RING finger protein 129, RING finger protein 33

+ [5]

Introduction

E3 SUMO-protein ligase that mediates SUMOylation of TAB2 leading to inhibition of NF-kappa-B and MAPK pathways by suppressing the TRAF6/TAB2/TAK1 complex.

100 Clinical Results associated with TRIM60

100 Translational Medicine associated with TRIM60

0 Patents (Medical) associated with TRIM60

Literatures (Medical) associated with TRIM60

01 Aug 2021·Cellular & Molecular ImmunologyQ1 · MEDICINE

The SUMOylation of TAB2 mediated by TRIM60 inhibits MAPK/NF-κB activation and the innate immune response

Q1 · MEDICINE

Article

Author: Wang, Xiaomeng ; Yang, Wenyong ; Dai, Lunzhi ; Yu, Hui ; Zhang, Zhiqiang ; Chen, Xueying ; Chen, Qianqian ; Zhong, Bo ; Qi, Yu ; Gu, Zhiwen ; Hu, Hongbo ; Qi, Shiqian ; Gong, Yanqiu ; Zhang, Huiyuan

AbstractActivation of the TAK1 signalosome is crucial for mediating the innate immune response to pathogen invasion and is regulated by multiple layers of posttranslational modifications, including ubiquitination, SUMOylation, and phosphorylation; however, the underlying molecular mechanism is not fully understood. In this study, TRIM60 negatively regulated the formation and activation of the TAK1 signalosome. Deficiency of TRIM60 in macrophages led to enhanced MAPK and NF-κB activation, accompanied by elevated levels of proinflammatory cytokines but not IFN-I. Immunoprecipitation-mass spectrometry assays identified TAB2 as the target of TRIM60 for SUMOylation rather than ubiquitination, resulting in impaired formation of the TRAF6/TAB2/TAK1 complex and downstream MAPK and NF-κB pathways. The SUMOylation sites of TAB2 mediated by TRIM60 were identified as K329 and K562; substitution of these lysines with arginines abolished the SUMOylation of TAB2. In vivo experiments showed that TRIM60-deficient mice showed an elevated immune response to LPS-induced septic shock andL. monocytogenesinfection. Our data reveal that SUMOylation of TAB2 mediated by TRIM60 is a novel mechanism for regulating the innate immune response, potentially paving the way for a new strategy to control antibacterial immune responses.

01 Jan 2012·Molecular and Cellular BiochemistryQ3 · BIOLOGY

Association of the testis-specific TRIM/RBCC protein RNF33/TRIM60 with the cytoplasmic motor proteins KIF3A and KIF3B

Q3 · BIOLOGY

Article

Author: Chih-Chun Chang ; Chih-Cheng Huang ; Chiu-Jung Huang

The Rnf33/Trim60 gene is temporally transcribed in the preimplantation embryo before being silenced at the blastocyst stage but Rnf33 expression is detected in adult testis of the mouse. The putative RNF33 protein is a tripartite motif (TRIM)/RBCC protein composed of a typical RING zinc finger, a B-box 2, two α-helical coiled-coil segments, and a B30.2 domain. As a first step towards the elucidation of the biologic function of RNF33, we aimed in this study to elucidate proteins that associate with RNF33. RNF33-interacting proteins were first derived by the yeast two-hybrid system followed by co-immunoprecipitation assays. Interacting domains were determined by deletion mapping in genetic and biochemical analyzes. RNF33 was shown to interact with the kinesin-2 family members 3A (KIF3A) and 3B (KIF3B) motor proteins in the heterodimeric form known to transport cargos along the microtubule. Domain mapping showed that the RB and B30.2 domains of RNF33 interacted with the respective carboxyl non-motor domains of KIF3A and KIF3B. Since RNF33 interacted with the carboxyl-terminal tail of the KIF3A-KIF3B heterodimer, the motor head section of KIF3A-KIF3B was free and available for association with designated cargo(s) and movement along the microtubule. Data also suggest that RNF33 most likely interacted with KIF3A-KIF3B independent of the adaptor kinesin-associated protein KAP3. This study is a first demonstration of a TRIM protein, namely RNF33, that interacts with the kinesin molecular motors possibly contributing to kinesin-dependent mobilization of specific cargo(s) along the microtubule in the testis of the mouse.

01 Mar 2011·The FEBS JournalQ3 · BIOLOGY

Nuclear factor kappa B and tumor necrosis factor‐alpha modulation of transcription of the mouse testis‐ and pre‐implantation development‐specific Rnf33/Trim60 gene

Q3 · BIOLOGY

Article

Author: Kong-Bung Choo ; Wan-Yi Lin ; Yao-Hui Tsai ; Min-Chuan Hsu ; Chiu-Jung Huang

We have previously reported a mouse Rnf33/Trim60 gene that is temporally expressed in the pre‐implantation embryo. The Rnf33 structural gene is composed of a short noncoding exon 1 and an intronless coding exon 2. In the present work, Rnf33 was shown to be expressed in the mouse testis and in the testicular cell lines TM3 and TM4. To elucidate Rnf33 transcriptional modulation, a 2.5‐kb Rnf33 sequence, inclusive of the upstream regulatory region, exon 1 and the associated intronic sequence, was dissected in transient transfection and luciferase assays. An initiator and an atypical TATA‐box were shown to act as the core promoter elements of the gene. Deletion and mutagenesis of the 2.5‐kb sequence in luciferase constructs further demonstrated that an intronic and palindromic kappa B (κB) sequence was an important cis element targeted by the nuclear factor‐κB (NF‐κB) subunits p65/RELA and p50/NFκB1, and also through modulation by tumor necrosis factor α. Transcriptional up‐regulation of Rnf33 by NF‐κB and tumor necrosis factor‐α was directly demonstrated in TM3 and TM4 cells by real‐time PCR quantification of the Rnf33 mRNA levels. Small interfering RNA knockdown of p65 and p50 confirmed Rnf33 down‐regulation by p65/p50. Spermatogenesis is regulated by a wide range of stimuli, including NF‐κB, which, in turn, is regulated by other signals. Hence, demonstration of NF‐κB‐regulated Rnf33 expression in testicular cells, particularly in Sertoli cells, implicates functional involvement of the putative RNF33 protein in spermatogenesis through association of the RNF33 protein with the microtubule via interaction with kinesin motor proteins, as previously demonstrated [Huang et al., submitted].

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TRIM60

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