Different nuclear/cytoplasmic distributions of RET finger protein in different cell types

Tezel, Gaye Güler; Nagasaka, Tetsuro; Iwahashi, Naoko; Asai, Naoya; Iwashita, Toshihide; Sakata, Kazuki; Takahashi, Masahide

doi:10.1046/j.1440-1827.1999.00957.x

Cited by 40 publications

(50 citation statements)

References 17 publications

(30 reference statements)

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“…Interestingly, several lines of evidence have also implicated RFP to be involved in tumorigenesis. RFP mRNA is highly expressed in many human and mouse cancer cell lines [39], and high levels of RFP are observed in the solitary plasmacytoma and multiple myeloma [40]. In addition, positive RFP expression usually predicts a poor clinical outcome in patients with endometrial cancer and colon carcinoma [41,42], and RFP expression is found in 41.4% of invasive breast carcinomas and in none of the non-neoplastic breast tissues [43].…”

Section: Discussionmentioning

confidence: 99%

RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation

et al. 2013

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The PTEN tumor suppressor is a lipid phosphatase that has a central role in regulating the phosphatidylinositol-3-kinase (PI3K) signal transduction cascade. Nevertheless, the mechanism by which the PTEN activity is regulated in cells needs further elucidation. Although previous studies have shown that ubiquitination of PTEN can modulate its stability and subcellular localization, the role of ubiquitination in the most critical aspect of PTEN function, its phosphatase activity, has not been fully addressed. Here, we identify a novel E3 ubiquitin ligase of PTEN, Ret finger protein (RFP), that is able to promote atypical polyubiquitinations of PTEN. These ubiquitinations do not lead to PTEN instability or relocalization, but rather significantly inhibit PTEN phosphatase activity and therefore modulate its ability to regulate the PI3K signal transduction cascade. Indeed, RFP overexpression relieves PTEN-mediated inhibitory effects on AKT activation; in contrast, RNAi-mediated knockdown of endogenous RFP enhances the ability of PTEN to suppress AKT activation. Moreover, RFP-mediated ubiquitination of PTEN inhibits PTEN-dependent activation of TRAIL expression and also suppresses its ability to induce apoptosis. Our findings demonstrate a crucial role of RFP-mediated ubiquitination in controlling PTEN activity.

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Section: Discussionmentioning

confidence: 99%

RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation

et al. 2013

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“…5 It has been reported that TRIM27 is detectable in male germ cells, peripheral and central neurons, hepatocytes and adrenal chromaffin cells. [6][7][8] However, it is highly expressed in various tumor cells and tissues, such as endometrial cancer, breast cancer and lung cancer. Furthermore, high-level expression of TRIM27 correlates with the proliferation, migration and chemosensitivity of some tumor cells and could act as a potential prognostic indicator in some cancers.…”

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confidence: 99%

Downregulation of TRIM27 expression inhibits the proliferation of ovarian cancer cells in vitro and in vivo

Wei

Bast

et al. 2016

Laboratory Investigation

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(tripartite motif-containing 27) was originally identified as a fusion partner with the RET (REarranged during transfection) proto-oncogene and is highly expressed in various tumor cells and tissues. However, the level of expression and function of TRIM27 in ovarian cancer remain unclear. Here we have measured the expression of TRIM27 in normal ovarian and fallopian tube epithelial cells and in ovarian serous carcinoma cells and correlated TRIM27 expression with clinical and pathological parameters. In addition, we detected the effect of TRIM27 knockdown on proliferation of ovarian cancer cells in cell culture and xenografts. The results demonstrated that TRIM27 was highly expressed in ovarian serous carcinoma cells, and TRIM27 expression was significantly correlated with metastasis and FIGO stage in ovarian serous carcinoma patients. Downregulation of TRIM27 expression suppressed the proliferation of ovarian cancer cells in cell culture and inhibited the growth of xenografts in nude mice. TRIM27 knockdown induced cell cycle arrest and apoptosis in ovarian cancer cells by upregulating the expression of p-P38 and downregulating the expression of p-AKT. Thus the present study suggests that TRIM27 could have important roles as an oncogene during the development of ovarian cancer and could serve as a diagnostic and therapeutic target.

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“…RFP is a component of PML nuclear bodies and interacts with other protein family members of PML, other B-box family members, 11,20,21 and other diverse proteins. [22][23][24][25][26][27] RFP even interacts with itself for homodimerization.…”

Section: Discussionmentioning

confidence: 99%

Ret finger protein inhibits muscle differentiation by modulating serum response factor and enhancer of polycomb1

et al. 2011

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Skeletal myogenesis is precisely regulated by multiple transcription factors. Previously, we demonstrated that enhancer of polycomb 1 (Epc1) induces skeletal muscle differentiation by potentiating serum response factor (SRF)-dependent muscle gene activation. Here, we report that an interacting partner of Epc1, ret finger protein (RFP), blocks skeletal muscle differentiation. Our findings show that RFP was highly expressed in skeletal muscles and was downregulated during myoblast differentiation. Forced expression of RFP delayed myoblast differentiation, whereas knockdown enhanced it. Epc1-induced enhancements of SRF-dependent multinucleation, transactivation of the skeletal a-actin promoter, binding of SRF to the serum response element, and muscle-specific gene induction were blocked by RFP. RFP interfered with the physical interaction between Epc1 and SRF. Muscles from rfp knockout mice (Rfp À/À ) mice were bigger than those from wild-type mice, and the expression of SRF-dependent muscle-specific genes was upregulated. Myotube formation and myoblast differentiation were enhanced in Rfp À/À mice. Taken together, our findings highlight RFP as a novel regulator of muscle differentiation that acts by modulating the expression of SRFdependent skeletal muscle-specific genes. Skeletal muscle is critical for the generation of active force, the maintenance of posture, and body shape. Muscle regeneration from myoblasts is important for the repair and maintenance of skeletal muscles after muscle injury or dystrophy. Myogenesis from the precursor cells to the skeletal muscle lineage consists of multiple steps, and each of these steps is tightly organized by extrinsic and intrinsic signaling pathways. Thus, not only for understanding the regeneration of injured skeletal muscles, but also for furthering therapeutic approaches to muscle atrophy, a hot issue in current research is how the proliferation and differentiation of myoblasts are regulated. To ultimately provide important clues for therapeutics, a comprehensive understanding of how various signaling mechanisms collaborate to regulate the gene expression and epigenetic programs for myoblast differentiation is needed.The TRIM (tripartite motif) protein family (also known as the RBCC protein family) has the common structures of three zinc-binding domains, a RING, a B-box type 1, and a B-box type 2, followed by a coiled-coil region.

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Different nuclear/cytoplasmic distributions of RET finger protein in different cell types

Cited by 40 publications

References 17 publications

RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation

RFP-mediated ubiquitination of PTEN modulates its effect on AKT activation

Downregulation of TRIM27 expression inhibits the proliferation of ovarian cancer cells in vitro and in vivo

Ret finger protein inhibits muscle differentiation by modulating serum response factor and enhancer of polycomb1

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