Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm

Kim, Jong Heon; Hahm, Bumsuk; Kim, Yoon Ki; Choi, Min-Hyeok; Jang, Sung Key

doi:10.1006/jmbi.2000.3687

Cited by 176 publications

(143 citation statements)

References 54 publications

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“…hnRNP-U then binds to the same site to further activate OPN promoter activation (Gao et al, 2005), indicating that an interaction among hnRNP proteins might be important for their in vivo functions (Kim et al, 2000). Here we also found that two hnRNP proteins bind to the upstream of the same gene at similar regions (Fig.…”

Section: Gnrh1 Transcriptional Regulationsupporting

confidence: 65%

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Zhao

Korzan

Chen

et al. 2008

Molecular and Cellular Neuroscience

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Gonadotropin-releasing hormone 1 (GnRH1) causes the release of gonadotropins from the pituitary to control reproduction. Here we report that two heterogeneous nuclear ribonucleoproteins (hnRNP-A/B and hnRNP-G) bind to the GnRH-I upstream promoter region in a cichlid fish Astatotilapia burtoni. We identified these binding proteins using a newly developed homology based method of mass spectrometric peptide mapping. We show that both hnRNP-A/B and hnRNP-G colocalize with GnRH1 in the pre-optic area of the hypothalamus in the brain. We also demonstrated that these ribonucleoproteins exhibit similar binding capacity in vivo, using immortalized mouse GT1-7 cells where overexpression of either hnRNP-A/B or hnRNP-G significantly down-regulates GnRH1 mRNA levels in GT1-7 cells, suggesting that both act as repressors in GnRH1 transcriptional regulation.

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Section: Gnrh1 Transcriptional Regulationsupporting

confidence: 65%

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Zhao

Korzan

Chen

et al. 2008

Molecular and Cellular Neuroscience

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“…HnRNP L may enhance the translation of some IRES-dependent mRNAs. 64 HnRNP E2 enhances poliovirus mRNA translation. 64 HnRNP C, also identified here, may modulate c-myc IRES translation in a cell cycle-dependent fashion.…”

Section: Discussionmentioning

confidence: 99%

Riboproteomics of the Hepatitis C Virus Internal Ribosomal Entry Site

Noble

et al. 2004

J. Proteome Res.

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Hepatitis C virus (HCV) protein translation is mediated by a cis-acting RNA, an internal ribosomal entry site (IRES), located in the 5′ nontranslated region of the viral RNA. To examine proteins bound to the IRES, which could include proteins important for its function as well as potential drug targets, we used shotgun peptide sequencing to identify proteins in quadruplicate protein affinity extracts of lysed Huh7 cells, obtained using a biotinylated IRES. Twenty-six proteins bound the HCV IRES but not a reversed complementary sequence RNA or vector RNA controls. These included five ribosomal subunits, nine eukaryotic initiation factor 3 subunits, and novel interacting proteins such as the cytoskeletal-related proteins actin, FHOS (formin homologue overexpressed in spleen) and MIP-T3 (microtubule interacting protein that associates with TRAF3). Other novel HCV IRES-binding proteins included UNR (upstream of N-ras), UNR-interacting protein, and the RNA-binding proteins PAI-1 (plasminogen activator inhibitor-1) mRNA binding protein and Ewing sarcoma breakpoint 1 region protein EWS. A large set of additional proteins bound both the HCV IRES and a reversed complementary IRES sequence control, including the known HCV interactors PTB (polypyrimidine tract binding protein), the La autoantigen, and nucleolin. The discovery of these novel HCV IRES-binding proteins suggests links between IRES biology and the cytoskeleton, signal transduction, and other cellular functions.

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“…Electrophoretic mobility shift assays show that hnRNPK, PCBP1 and PCBP2 interact differently with the c-myc IRES It has been shown previously that members of the poly (rC) binding protein family contribute to many proteinprotein interactions, and that PCBP1, PCBP2 and hnRNPK can form homodimers (Kim et al, 2000). Thus, to investigate further the interactions of c-myc IRES RNA with PCBP1, PCBP2 and hnRNPK, electrophorectic mobility shift assays (EMSAs) were performed.…”

Section: Uv Crosslinking Analysis Shows That the C-myc Ires Interactsmentioning

confidence: 99%

Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo

et al. 2003

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The 5 0 untranslated region of the proto-oncogene c-myc contains an internal ribosome entry segment and c-Myc translation can be initiated by cap-independent as well as cap-dependent mechanisms. In contrast to the process of cap-dependent initiation, the trans-acting factor requirements for cellular internal ribosome entry are poorly understood. Here, we show that members of the poly (rC) binding protein family, poly (rC) binding protein 1 (PCBP1), poly (rC) binding protein 2 (PCBP2) and hnRNPK were able to activate the IRES in vitro up to threefold when added in combination with upstream of N-ras and unr-interacting protein. The interactions of PCBP1, PCBP2 and hnRNPK with c-myc-IRES-RNA were shown to be specific by ultraviolet crosslinking analysis and electrophoretic mobility shift assays, while immunoprecipitation of the three proteins using specific antibodies followed by reverse transcriptase-polymerase chain reaction showed that they were able to bind c-myc mRNA. c-myc-IRES-mediated translation from the reporter vector was stimulated by cotransfection of plasmids encoding PCBP1, PCBP2 and hnRNPK. Interestingly, the mutated version of the c-myc IRES that is prevalent in patients with multiple myeloma bound hnRNPK more efficiently in vitro and was stimulated by hnRNPK to a greater extent in vivo.

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Protein-protein interaction among hnRNPs shuttling between nucleus and cytoplasm

Cited by 176 publications

References 54 publications

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Riboproteomics of the Hepatitis C Virus Internal Ribosomal Entry Site

Members of the poly (rC) binding protein family stimulate the activity of the c-myc internal ribosome entry segment in vitro and in vivo

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