A Novel RING Finger-B Box-Coiled-Coil Protein, GERP

Vincent, Steven R.; Kwasnicka, Dorota A.; Fretier, Pascale

doi:10.1006/bbrc.2000.3984

Cited by 32 publications

(28 citation statements)

References 27 publications

(28 reference statements)

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“…Sequencing of the genomic locus further confirmed the sequence and structure of the gene (data not shown). The sequence of this gene turned out to be identical to that of the TRIM8/GERP gene, independently identified by two groups using a functional genomic approach, based on systematic data gathered from screening the dbEST data base, with oligonucleotides derived from conserved RING domain sequences (29,30).…”

Section: Trim8/gerp a Ring Finger Protein That Interacts With Socs-1mentioning

confidence: 99%

“…Comparison of murine, rat, and human sequences (obtained by scanning the NCBI data base) revealed a 90% identity at the protein level. The carboxyl end of the protein contained a consensus nuclear localization motif (30), whereas the amino terminus of the predicted polypeptide sequence contained a canonical RING motif. The TRIM8/GERP RING domain spanned 41 amino acids with canonical consensus residues, along with cysteine/ histidine contrapositions similar to other C2H2 category RING fingers (29,30) (Fig.…”

Section: Trim8/gerp a Ring Finger Protein That Interacts With Socs-1mentioning

confidence: 99%

“…One of these proteins, termed TRIM8/ GERP, is a RING finger protein. TRIM8/GERP is a newly described member of the so-called tripartite motif family (also known as the RBCC subclass of the RING family containing proteins) (29,30). The RBCC proteins, which include members implicated in a variety of processes, such as development and cell-growth regulation, possess two zinc-binding domains between an amino-terminal RING finger and a coiled-coil region that is immediately amino-terminal to a variable carboxylterminal region.…”

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confidence: 99%

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TRIM8/GERP RING Finger Protein Interacts with SOCS-1

Toniato¹,

Chen

Losman

et al. 2002

Journal of Biological Chemistry

102

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Members of the suppressor of cytokine signaling (SOCS) family of signaling molecules regulate the activation of cytokine signaling. Experimental evidence indicates that SOCS expression is induced by cytokines and pro-inflammatory stimuli and is controlled at both the transcriptional and post-transcriptional levels. SOCS proteins are unstable and seem to be rapidly degraded by proteasomal pathways. However, the mechanisms by which SOCS protein levels are regulated remain unclear. Here, we show that TRIM8/GERP, a RING finger protein, interacts with SOCS-1 in vitro and in vivo. TRIM8/GERP, previously identified as a new member of the family of proteins containing a tripartite motif (TRIM), is a 551-amino acid RING finger protein conserved across species. TRIM8/GERP expression can be induced by interferon-␥ in epithelial and lymphoid cells. Coexpression of TRIM8/GERP with SOCS-1 decreases SOCS-1 protein stability and levels. Functionally, expression of TRIM8/GERP decreases the repression of interferon-␥ signaling mediated by SOCS-1. These data suggest that TRIM8/GERP may be a regulator of SOCS-1 function.Cytokines control many different cellular functions, including proliferation, differentiation, and gene expression (1, 2). Moreover, they participate in the pathophysiology of viral infections, play a central role in the development of the hematopoietic system, and have been implicated in the pathogenesis of autoimmune diseases (3, 4). The biological response of a cell to cytokines involves a complex network of signal transduction machinery. Signaling is initiated by the oligomerization of cognate cytokine receptors expressed on the surface of target cells (5), which triggers the activation of members of the JAK 1 family of protein-tyrosine kinases that constitutively associate with the cytokine receptor. Subsequently, JAKs can phosphorylate tyrosine residues present in the cytoplasmic regions of the receptors. These phosphorylated tyrosines then act as docking sites for signaling molecules, such as members of the STAT family of transcription factors (6).The intensity and duration of cytokine signaling seems to be regulated by several mechanisms. It is now known that at least three different classes of negative regulators contribute to cytokine inhibition: (i) the SH2-containing protein-tyrosine phosphatases 1 and 2 (7, 8), (ii) the protein inhibitors of activated STATs, and (iii) the suppressor of cytokine signaling (SOCS protein) (9 -13). Experimental data suggest that (i) SOCS genes are induced by cytokines; (ii) SOCS molecules can inhibit cytokine signaling by binding to downstream signaling molecules such as JAK kinases (14 -16); (iii) deregulated expression of SOCS proteins perturbs cytokine-related cellular proliferation and hematopoietic differentiation in murine tissues (17). Mice lacking SOCS-1 die shortly after birth from hepatic necrosis (18 -20). Data suggest that this lethality is due, at least in part, to hypersensitivity to IFN-␥ signaling. SOCS-2-deficient mice seem healthy after birth but develop a...

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Section: Trim8/gerp a Ring Finger Protein That Interacts With Socs-1mentioning

confidence: 99%

Section: Trim8/gerp a Ring Finger Protein That Interacts With Socs-1mentioning

confidence: 99%

mentioning

confidence: 99%

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TRIM8/GERP RING Finger Protein Interacts with SOCS-1

Toniato¹,

Chen

Losman

et al. 2002

Journal of Biological Chemistry

102

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“…We examined the effect of variations in the number of different models. With four models, we found that (Aicher et al 1999;Tsai et al 2000) NM_001964 NM_007913 2.3854e+09 CSNK1E NM_001894 NM_013767 4.5797e+04 ACTG2 (Carson et al 2000) NM_001615 NM_009610 3.9155e+04 RXRG (Downes et al 1994;Georgiades and Brickell 1997;Rebhan et al 1997 (Rebhan et al 1997;Valle et al 1997) NM_003673 NM_011540 2.2401e+02 LZTR1 NM_006767 NM_025808 2.0356e+02 TRIM8 (Vincent et al 2000) NM_030912 NM_053100 1.9458e+02…”

Section: Discussionmentioning

confidence: 90%

Decoding Human Regulatory Circuits

Thompson¹,

Palumbo²,

Wasserman³

et al. 2004

Genome Res.

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Clusters of transcription factor binding sites (TFBSs) which direct gene expression constitute cis-regulatory modules (CRMs). We present a novel algorithm, based on Gibbs sampling, which locates, de novo, the cis features of these CRMs, their component TFBSs, and the properties of their spatial distribution. The algorithm finds 69% of experimentally reported TFBSs and 85% of the CRMs in a reference data set of regions upstream of genes differentially expressed in skeletal muscle cells. A discriminant procedure based on the output of the model specifically discriminated regulatory sequences in muscle-specific genes in an independent test set. Application of the method to the analysis of 2710 10-kb fragments upstream of annotated human genes identified 17 novel candidate modules with a false discovery rate ≤0.05, demonstrating the applicability of the method to genome-scale data

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“…Because all TRIM proteins share the RBCC moiety, which this study has identified as a potent inducer of apoptosis, we propose that a large majority of TRIM family members might have apoptotic roles in a variety of processes such as development and cell growth. We speculate that the putative tumor-suppressing activities of glioblastoma expressed RING finger protein/TRIM8 and LEU5/TRIM13 (deleted in glioblastoma and B-cell lymphocytic leukemia, respectively (51,52)) may result from their pro-apoptotic effects. Further studies will be required to clarify the roles of potentially apoptotic TRIM proteins in many biological processes.…”

Section: Discussionmentioning

confidence: 99%

The Ret Finger Protein Induces Apoptosis via Its RING Finger-B Box-Coiled-coil Motif

Dho

Kwon

2003

Journal of Biological Chemistry

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The Ret finger protein (RFP) is a member of the tripartite motif family, which is characterized by a conserved RING finger, a B-box, and a coiled-coil domain (together called RBCC). Although RFP is known to become oncogenic when its RBCC moiety is connected to a tyrosine kinase domain by DNA rearrangement, its biological function is not well defined. Here we show that ectopic expression of RFP in human embryonic kidney 293 cells causes extensive apoptosis, as assessed by multiple criteria. RFP expression activates Jun N-terminal kinase and p38 kinase and also increases caspase-3-like activity. However, RFP failed to release cytochrome c and, therefore, to increase caspase-9-like activity. RFPinduced apoptosis could be blocked by the caspase-8 inhibitor crmA and dominant negative ASK1 but not by Bcl-2. These results reveal a novel RFP death pathway that recruits mitogen-activated protein kinase and caspases independently of mitochondrial events. Domain mapping showed that the intact RBCC moiety is necessary for the pro-apoptotic function of RFP. Moreover, expression of the RBCC moiety further potentiated the pro-apoptotic activity and resulted in a 7-fold increase of caspase activation compared with that induced by full-length RFP. This suggests that a large number of tripartite motif family members sharing the RBCC moiety may participate in the control of cell survival.

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A Novel RING Finger-B Box-Coiled-Coil Protein, GERP

Cited by 32 publications

References 27 publications

TRIM8/GERP RING Finger Protein Interacts with SOCS-1

TRIM8/GERP RING Finger Protein Interacts with SOCS-1

Decoding Human Regulatory Circuits

The Ret Finger Protein Induces Apoptosis via Its RING Finger-B Box-Coiled-coil Motif

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