A role for hnRNP C1/C2 and Unr in internal initiation of translation during mitosis

Schepens, Bert; Tinton, Sandrine A.; Bruynooghe, Yanik; Parthoens, Eef; Haegman, Mira; Beyaert, Rudi; Cornelis, Sigrid

doi:10.1038/sj.emboj.7601468

Cited by 98 publications

(134 citation statements)

References 29 publications

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“…0 -UTR (albeit tested with FLuc as the upstream cistron) and DAP5 5 0 -UTR met this criterion (Araud et al 2007;Schepens et al 2007), but in view of the ESTevidence for 3 0 -splice sites in both cases (Baranick et al 2008), independent confirmation of these findings is desirable. At the other extreme, the HIF-1a, VEGF, XIAP, and EGR-1 5 0 -UTRs comprehensively failed the siRNA test (Bert et al 2006).…”

Section: Discussionmentioning

confidence: 99%

The Current Status of Vertebrate Cellular mRNA IRESs

Jackson

2013

Cold Spring Harbor Perspectives in Biology

135

130

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Internal ribosome entry sites/segments (IRESs) were first discovered over 20 years ago in picornaviruses, followed by the discovery of two other types of IRES in hepatitis C virus (HCV), and the dicistroviruses, which infect invertebrates. In the meantime, reports of IRESs in eukaryotic cellular mRNAs started to appear, and the list of such putative IRESs continues to grow to the point in which it now stands at 100, 80% of them in vertebrate mRNAs. Despite initial skepticism from some quarters, there now seems universal agreement that there is genuine internal ribosome entry on the viral IRESs. However, the same cannot be said for cellular mRNA IRESs, which continue to be shrouded in controversy. The aim of this article is to explain why vertebrate mRNA IRESs remain controversial, and to discuss ways in which these controversies might be resolved.

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Section: Discussionmentioning

confidence: 99%

The Current Status of Vertebrate Cellular mRNA IRESs

Jackson

2013

Cold Spring Harbor Perspectives in Biology

135

130

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“…The RBP HNRNPC has attracted much attention in the recent years, for its multiplex functions in regulating pre‐mRNA splicing (Konig et al , 2010; Zarnack et al , 2013), mRNA stabilization (Shetty, 2005), length‐dependent exportation (McCloskey et al , 2012), stability and translation (Holcik et al , 2003; Kim et al , 2003; Schepens et al , 2007), etc. Although HNRNPC has been shown to regulate multiple cancer‐related genes, mostly through RNA‐related processes, understanding about the accountable machinery for the function of HNRNPC in tumors is still limited.…”

Section: Discussionmentioning

confidence: 99%

Function of HNRNPC in breast cancer cells by controlling the dsRNA‐induced interferon response

et al. 2018

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Elevated expression of RNA binding protein HNRNPC has been reported in cancer cells, while the essentialness and functions of HNRNPC in tumors were not clear. We showed that repression of HNRNPC in the breast cancer cells MCF7 and T47D inhibited cell proliferation and tumor growth. Our computational inference of the key pathways and extensive experimental investigations revealed that the cascade of interferon responses mediated by RIG‐I was responsible for such tumor‐inhibitory effect. Interestingly, repression of HNRNPC resulted in accumulation of endogenous double‐stranded RNA (dsRNA), the binding ligand of RIG‐I. These up‐regulated dsRNA species were highly enriched by Alu sequences and mostly originated from pre‐mRNA introns that harbor the known HNRNPC binding sites. Such source of dsRNA is different than the recently well‐characterized endogenous retroviruses that encode dsRNA. In summary, essentialness of HNRNPC in the breast cancer cells was attributed to its function in controlling the endogenous dsRNA and the down‐stream interferon response. This is a novel extension from the previous understandings about HNRNPC in binding with introns and regulating RNA splicing.

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“…HNRPC is a nuclear pre-mRNA binding protein that has also been implicated in cell proliferation (Kim et al 2003, Schepens et al 2007) and DPY30 is a protein involved in differentiation (Jiang et al 2011). All these K OLIVA and others .…”

Section: Proliferation and Differentiationmentioning

confidence: 99%

The effect of pre-existing maternal obesity on the placental proteome: two-dimensional difference gel electrophoresis coupled with mass spectrometry

Oliva¹,

Barker²,

Riley³

et al. 2012

Journal of Molecular Endocrinology

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Our aim was to study the protein expression profiles of placenta obtained from lean and obese pregnant women with normal glucose tolerance at the time of term Caesarean section. We used two-dimensional difference gel electrophoresis (2D-DIGE), utilising narrow-range immobilised pH gradient strips that encompassed the broad pH range of 4–5 and 5–6, followed by MALDI-TOF mass spectrometry of selected protein spots. Western blot and quantitative RT-PCR (qRT-PCR) analyses were performed to validate representative findings from the 2D-DIGE analysis. Eight proteins were altered (six down-regulated and two up-regulated on obese placentas). Annexin A5 (ANXA5), ATP synthase subunit beta, mitochondria (ATPB), brain acid soluble protein 1 (BASP1), ferritin light chain (FTL), heterogeneous nuclear ribonucleoprotein C (HNRPC) and vimentin (VIME) were all lower in obese patients. Alpha-1-antitrypsin (A1AT) and stress-70 protein, mitochondrial (GRP75) were higher in obese patients. Western blot analysis of ANXA5, ATPB, FTL, VIME, A1AT and GRP75 confirmed the findings from the 2D-DIGE analysis. For brain acid soluble protein 1 and HNRPC, qRT-PCR analysis also confirmed the findings from the 2D-DIGE analysis. Immunohistochemical analysis was also used to determine the localisation of the proteins in human placenta. In conclusion, proteomic analysis of placenta reveals differential expression of several proteins in patients with pre-existing obesity. These proteins are implicated in a variety of cellular functions such as regulation of growth, cytoskeletal structure, oxidative stress, inflammation, coagulation and apoptosis. These disturbances may have significant implications for fetal growth and development.

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A role for hnRNP C1/C2 and Unr in internal initiation of translation during mitosis

Cited by 98 publications

References 29 publications

The Current Status of Vertebrate Cellular mRNA IRESs

The Current Status of Vertebrate Cellular mRNA IRESs

Function of HNRNPC in breast cancer cells by controlling the dsRNA‐induced interferon response

The effect of pre-existing maternal obesity on the placental proteome: two-dimensional difference gel electrophoresis coupled with mass spectrometry

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