Cloning and characterisation of the RBCC728/TRIM36 zinc-binding protein from the tumor suppressor gene region at chromosome 5q22.3

Bálint, Ildikó; Müller, Anke; Nagy, Anetta; Kovács, Gyula

doi:10.1016/j.gene.2004.02.045

Cited by 26 publications

(15 citation statements)

References 18 publications

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“…The third, TRIM36, had previously been reported by Reymond et al (2), but was represented as only possessing an N-terminal RBCC/TRIM domain. Validating our findings, two other groups identified and reported TRIM36 during the course of this study and also determined that it possesses a MID1/MID2-like domain architecture that includes both C-terminal FN3 and B30.2-like domains (14,31).…”

Section: Discussionsupporting

confidence: 75%

Subclassification of the RBCC/TRIM Superfamily Reveals a Novel Motif Necessary for Microtubule Binding

Short¹,

Cox²

2006

Journal of Biological Chemistry

299

358

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The biological significance of RBCC (N-terminal RING finger/Bbox/coiled coil) proteins is increasingly being appreciated following demonstrated roles in disease pathogenesis, tumorigenesis, and retroviral protective activity. Found in all multicellular eukaryotes, RBCC proteins are involved in a vast array of intracellular functions; but as a general rule, they appear to function as part of large protein complexes and possess ubiquitin-protein isopeptide ligase activity. Those members characterized to date have diverse C-terminal domain compositions and equally diverse subcellular localizations and functions. Using a bioinformatics approach, we have identified some new RBCC proteins that help define a subfamily that shares an identical domain arrangement (MID1, MID2, TRIM9, TNL, TRIM36, and TRIFIC). Significantly, we show that all analyzed members of this subfamily associate with the microtubule cytoskeleton, suggesting that subcellular compartmentalization is determined by the unique domain architecture, which may in turn reflect basic functional similarities. We also report a new motif called the COS box, which is found within these proteins, the MURF family, and a distantly related non-RBCC microtubule-binding protein. Notably, we demonstrate that mutations in the COS box abolish microtubule binding ability, whereas its incorporation into a nonmicrotubule-binding RBCC protein redirects it to microtubule structures. Further bioinformatics investigation permitted subclassification of the entire human RBCC complement into nine subfamilies based on their varied C-terminal domain compositions. This classification schema may aid the understanding of the molecular function of members of each subgroup and their potential involvement in both basic cellular processes and human disease.Members of the RBCC (N-terminal RING finger/B-box/coiled coil) or TRIM (tripartite motif) family of proteins perform a diverse array of cellular roles, yet are believed to share some functional properties: 1) act as a scaffold for the assembly of larger multiprotein complexes and 2) possess RING-dependent ubiquitin ligase activity (1, 2). The RBCC domain can be found in isolation or in combination with a variety of other C-terminal domains, including the NHL (NCL-1/HT2A/LIN-41 repeat), immunoglobulin, MATH (meprin and tumor necrosis factor receptor-associated factor homology), B30.2-like/RFP (Ret finger protein)/SPRY (SplA and ryanodine receptor) (the largest subgroup in humans), ARF (ADP-ribosylation factor), PHD (plant homeodomain finger), and BROMO domains (1, 2). As a family of proteins, their biological significance is perhaps best highlighted by the growing number that have a demonstrated role in disease pathogenesis, including immunological and developmental disorders, tumorigenesis, and retroviral protective activity (3-7).We have previously identified and characterized two RBCC proteins, MID1 and its closely related homolog, MID2. MID1 and MID2 contain a B30.2-like domain at their C terminus and a single fibronectin type III (FN3...

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Section: Discussionsupporting

confidence: 75%

Subclassification of the RBCC/TRIM Superfamily Reveals a Novel Motif Necessary for Microtubule Binding

Short¹,

Cox²

2006

Journal of Biological Chemistry

299

358

View full text Add to dashboard Cite

show abstract

“…Although the most of TRIM proteins are less characterized, some TRIM proteins play important roles in the cellular processes related to cancer. For example, TRIM3, TRIM16, TRIM29 and TRIM36 have been reported to function as tumor suppressors [ 18 – 21 ]. Interestingly, TRIM7 was identified as glycogenin-interacting protein and involved in the regulation of cellular glucose metabolism [ 22 ].…”

Section: Discussionmentioning

confidence: 99%

TRIM59 Promotes the Proliferation and Migration of Non-Small Cell Lung Cancer Cells by Upregulating Cell Cycle Related Proteins

et al. 2015

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TRIM protein family is an evolutionarily conserved gene family implicated in a number of critical processes including inflammation, immunity, antiviral and cancer. In an effort to profile the expression patterns of TRIM superfamily in several non-small cell lung cancer (NSCLC) cell lines, we found that the expression of 10 TRIM genes including TRIM3, TRIM7, TRIM14, TRIM16, TRIM21, TRIM22, TRIM29, TRIM59, TRIM66 and TRIM70 was significantly upregulated in NSCLC cell lines compared with the normal human bronchial epithelial (HBE) cell line, whereas the expression of 7 other TRIM genes including TRIM4, TRIM9, TRIM36, TRIM46, TRIM54, TRIM67 and TRIM76 was significantly down-regulated in NSCLC cell lines compared with that in HBE cells. As TRIM59 has been reported to act as a proto-oncogene that affects both Ras and RB signal pathways in prostate cancer models, we here focused on the role of TRIM59 in the regulation of NSCLC cell proliferation and migration. We reported that TRIM59 protein was significantly increased in various NSCLC cell lines. SiRNA-induced knocking down of TRIM59 significantly inhibited the proliferation and migration of NSCLC cell lines by arresting cell cycle in G2 phase. Moreover, TRIM59 knocking down affected the expression of a number of cell cycle proteins including CDC25C and CDK1. Finally, we knocked down TRIM59 and found that p53 protein expression levels did not upregulate, so we proposed that TRIM59 may promote NSCLC cell growth through other pathways but not the p53 signaling pathway.

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“…Among the 15 genes within the amplification locus, the major oncogenic-related cancer gene was TRIM36 that is overexpressed in prostate cancer. It has been hypothesized its overexpression leads to chromosomal instability [41,42]. …”

Section: Resultsmentioning

confidence: 99%

Metastatic tumor evolution and organoid modeling implicate TGFBR2as a cancer driver in diffuse gastric cancer

et al. 2014

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BackgroundGastric cancer is the second-leading cause of global cancer deaths, with metastatic disease representing the primary cause of mortality. To identify candidate drivers involved in oncogenesis and tumor evolution, we conduct an extensive genome sequencing analysis of metastatic progression in a diffuse gastric cancer. This involves a comparison between a primary tumor from a hereditary diffuse gastric cancer syndrome proband and its recurrence as an ovarian metastasis.ResultsBoth the primary tumor and ovarian metastasis have common biallelic loss-of-function of both the CDH1 and TP53 tumor suppressors, indicating a common genetic origin. While the primary tumor exhibits amplification of the Fibroblast growth factor receptor 2 (FGFR2) gene, the metastasis notably lacks FGFR2 amplification but rather possesses unique biallelic alterations of Transforming growth factor-beta receptor 2 (TGFBR2), indicating the divergent in vivo evolution of a TGFBR2-mutant metastatic clonal population in this patient. As TGFBR2 mutations have not previously been functionally validated in gastric cancer, we modeled the metastatic potential of TGFBR2 loss in a murine three-dimensional primary gastric organoid culture. The Tgfbr2 shRNA knockdown within Cdh1-/-; Tp53-/- organoids generates invasion in vitro and robust metastatic tumorigenicity in vivo, confirming Tgfbr2 metastasis suppressor activity.ConclusionsWe document the metastatic differentiation and genetic heterogeneity of diffuse gastric cancer and reveal the potential metastatic role of TGFBR2 loss-of-function. In support of this study, we apply a murine primary organoid culture method capable of recapitulating in vivo metastatic gastric cancer. Overall, we describe an integrated approach to identify and functionally validate putative cancer drivers involved in metastasis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13059-014-0428-9) contains supplementary material, which is available to authorized users.

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Cloning and characterisation of the RBCC728/TRIM36 zinc-binding protein from the tumor suppressor gene region at chromosome 5q22.3

Cited by 26 publications

References 18 publications

Subclassification of the RBCC/TRIM Superfamily Reveals a Novel Motif Necessary for Microtubule Binding

Subclassification of the RBCC/TRIM Superfamily Reveals a Novel Motif Necessary for Microtubule Binding

TRIM59 Promotes the Proliferation and Migration of Non-Small Cell Lung Cancer Cells by Upregulating Cell Cycle Related Proteins

Metastatic tumor evolution and organoid modeling implicate TGFBR2as a cancer driver in diffuse gastric cancer

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