Organization of the Human tarbp2 Gene Reveals Two Promoters That Are Repressed in an Astrocytic Cell Line

Bannwarth, Sylvie; Talakoub, Lily; Letourneur, Franck; Duarte, Márcia do Rocio; Purcell, Damian F. J.; Hiscott, John; Gatignol, Anne

doi:10.1074/jbc.m104645200

Cited by 32 publications

(35 citation statements)

References 40 publications

(16 reference statements)

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“…The two proteins are identical except that TRBP2 has 21 additional amino acids at the N-terminal end due to the translation of an alternative first exon (4,53) (Fig. 1A).…”

Section: Trbp As a Dsrna Binding Protein Identificationmentioning

confidence: 98%

“…For the human gene, two adjacent promoters initiate the transcription of alternative first exons for TRBP1 and TRBP2 mRNAs. The TRBP1 promoter is upregulated by NF-Y transcription factors, which influences the expression of both isoforms, as observed by the low expression levels of the proteins in astrocytic cells (3,4). The knockout of the tarbp2 gene in mice results in a growth defect, and males are sterile, displaying severe oligospermia.…”

Section: Tarbp2 Gene Characterizationmentioning

confidence: 99%

“…The TRBP expression level in astrocytes is low because of the weak induction of its promoter. In turn, the poor stimulation of the TRBP1 promoter in astrocytes compared to that in lymphocytes is due to the reduced amount of the NF-Y transcription factor in these cells (3,4,109) (Fig. 3A).…”

Section: Consequences Of Pkr Inhibition By Trbpmentioning

confidence: 99%

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The Multiple Functions of TRBP, at the Hub of Cell Responses to Viruses, Stress, and Cancer

Daniels

Gatignol

2012

Microbiol Mol Biol Rev

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100

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SUMMARY The TAR RNA binding protein (TRBP) has emerged as a key player in many cellular processes. First identified as a cellular protein that facilitates the replication of human immunodeficiency virus, TRBP has since been shown to inhibit the activation of protein kinase R (PKR), a protein involved in innate immune responses and the cellular response to stress. It also binds to the PKR activator PACT and regulates its function. TRBP also contributes to RNA interference as an integral part of the minimal RNA-induced silencing complex with Dicer and Argonaute proteins. Due to its multiple functions in the cell, TRBP is involved in oncogenesis when its sequence is mutated or its expression is deregulated. The depletion or overexpression of TRBP results in malignancy, suggesting that the balance of TRBP expression is key to normal cellular function. These studies show that TRBP is multifunctional and mediates cross talk between different pathways. Its activities at the molecular level impact the cellular function from normal development to cancer and the response to infections.

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“…The two proteins are identical except that TRBP2 has 21 additional amino acids at the N-terminal end due to the translation of an alternative first exon (4,53) (Fig. 1A).…”

Section: Trbp As a Dsrna Binding Protein Identificationmentioning

confidence: 98%

Section: Tarbp2 Gene Characterizationmentioning

confidence: 99%

See 1 more Smart Citation

The Multiple Functions of TRBP, at the Hub of Cell Responses to Viruses, Stress, and Cancer

Daniels

Gatignol

2012

Microbiol Mol Biol Rev

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100

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“…TRBP1 was the first of these proteins to be identified. TRBP2 contains a splice variant that adds 21 additional amino acids to its N terminus (6). Compared with TRBP1, TRBP3 is missing the C-terminal dsRNA-binding domain (7).…”

mentioning

confidence: 99%

TRBP Homolog Interacts with Eukaryotic Initiation Factor 6 (eIF6) in Fenneropenaeus chinensis

Wang

Liu

Chen

et al. 2009

The Journal of Immunology

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The HIV transactivating response RNA-binding protein (TRBP) plays an important role in many biological processes. We have cloned three cDNAs from newly identified genes in the TRBP family from Fenneropenaeus chinensis. These genes have been designated Fc-TRBP1-3. Recombinant Fc-TRBP1, which was produced in Escherichia coli, was used for panning of a T7 phage display library of the Chinese shrimp hemocytes. From this panning, Fc-eukaryotic initiation factor 6 (Fc-eIF6) was isolated and sequenced. Fc-eIF6 was then cloned, recombinantly expressed, and shown to interact with Fc-TRBP by the performance of pull-down assays and Far Western blot analysis. Expression of Fc-TRBP was detected in many tissues, with elevated expression in the heart, gill, and intestine in the early stages of infection by the white spot syndrome virus (WSSV), and enhanced expression in most tissues following challenge with Vibrio anguillarum. Western blot studies confirmed the increased expression of Fc-TRBP in the gill after WSSV infection. The expression pattern of eIF6 was also analyzed and its expression was also up-regulated in intestine of WSSV-challenged shrimp. The replication of WSSV was reduced after injection of Fc-TRBP. These results indicate that Fc-TRBP and Fc-eIF6 may be components of the RNA-induced silencing complex (RISC), and thereby play a crucial role in the antiviral defense response of shrimp.

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“…TRBP was originally cloned as an HIV-1 transactivation-response RNA-binding protein and belongs to the family of double-stranded RNA (dsRNA)-binding proteins with two clearly defined dsRNAbinding domains (dsRBDs) and a carboxyl-terminal basic region (17)(18)(19)(20)(21). TRBP dsRBD2 binds transactivation-response with higher affinity than dsRBD1, because of the presence of a KR helix motif (16,17).…”

mentioning

confidence: 99%

Merlin, a Tumor Suppressor, Interacts with Transactivation-responsive RNA-binding Protein and Inhibits Its Oncogenic Activity

Lee¹,

Kim²,

Ryu³

et al. 2004

Journal of Biological Chemistry

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The neurofibromatosis type 2 gene-encoded protein, merlin, is related to the ERM (ezrin, radixin, and moesin) family of membrane-cytoskeleton-associated proteins. Recent studies suggest that the loss of neurofibromatosis type 2 function contributes to tumor development and metastasis. Although the cellular functions of merlin as a tumor suppressor are relatively well characterized, the cellular mechanism whereby merlin controls cell proliferation from membrane locations is still poorly understood. During our efforts to find potential merlin modulators through protein-protein interactions, we identified transactivation-responsive RNAbinding protein (TRBP) as a merlin-binding protein in a yeast two-hybrid screen. The interaction between TRBP and merlin was confirmed by glutathione S-transferase pull-down assays, co-immunoprecipitation, and co-localization experiments. The carboxyl-terminal regions of each protein were responsible for their interaction. Cells overexpressing TRBP showed enhanced cell growth in cell proliferation assays and also exhibited transformed phenotypes, such as anchorage-independent cell growth and tumor development in mouse xenografts. Merlin efficiently inhibited these oncogenic activities of TRBP in our experiments. These results provide the first clue to the functional interaction between TRBP and merlin and suggest a novel mechanism for the tumor suppressor function of merlin both in vitro and in vivo.

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Organization of the Human tarbp2 Gene Reveals Two Promoters That Are Repressed in an Astrocytic Cell Line

Cited by 32 publications

References 40 publications

The Multiple Functions of TRBP, at the Hub of Cell Responses to Viruses, Stress, and Cancer

The Multiple Functions of TRBP, at the Hub of Cell Responses to Viruses, Stress, and Cancer

TRBP Homolog Interacts with Eukaryotic Initiation Factor 6 (eIF6) in Fenneropenaeus chinensis

Merlin, a Tumor Suppressor, Interacts with Transactivation-responsive RNA-binding Protein and Inhibits Its Oncogenic Activity

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