Regulation of <scp>BC</scp>200 <scp>RNA</scp>‐mediated translation inhibition by hn<scp>RNP</scp> E1 and E2

Jang, Seonghui; Shin, Heegwon; Lee, Jungmin; Kim, Youngmi; Bak, Geunu; Lee, Younghoon

doi:10.1002/1873-3468.12544

Cited by 19 publications

(20 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We recently identified a heterogeneous ribonucleoprotein E2 (hnRNP E2, also known as PCBP2) as a BC200 RNA-interacting protein (13). hnRNP E2 binds to BC200 RNA mainly through the unique 3′ C-rich domain (nts 162-200) of BC200 RNA (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…BC200 RNA is known to be targeted to dendrites by hnRNP A2/B1 in neuronal cells (19). Likewise, it is likely that BC200 RNA could be targeted to p-bodies by hnRNP E2 in HeLa cells because the p-body constituent (hnRNP E2) is a binding partner of BC200 RNA (13). …”

Section: Resultsmentioning

confidence: 99%

“…Recently, we identified heterologous nuclear ribonucleoprotein E2 (hnRNP E2) as a binding partner of BC200 RNA, as assessed using a yeast three-hybrid assay (13). hnRNP E2 is a multifunctional protein that participates in a variety of cellular processes, including RNA metabolism (14, 15) and translational enhancement (16).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identifying the cellular location of brain cytoplasmic 200 RNA using an RNA-recognizing antibody

et al. 2017

Self Cite

View full text Add to dashboard Cite

Brain cytoplasmic 200 RNA (BC200 RNA) is a neuron-specific non-coding RNA, implicated in the inhibition of local synaptodendritic protein synthesis, and is highly expressed in some cancer cells. Although BC200 RNA has been shown to inhibit translation in vitro, the cellular location of this inhibition is unknown. In this study, we used a BC200 RNA-recognizing antibody to identify the cellular locations of BC200 RNA in HeLa cervical carcinoma cells. We observed punctate signals in both the cytoplasm and nucleus, and further discovered that BC200 RNA co-localized with the p-body decapping enzyme, DCP1A, and the heterogeneous nuclear ribonucleoprotein E2 (hnRNP E2). The latter is a known BC200 RNA-binding partner protein and a constituent of p-bodies. This suggests that BC200 RNA is localized to p-bodies via hnRNP E2.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Identifying the cellular location of brain cytoplasmic 200 RNA using an RNA-recognizing antibody

et al. 2017

Self Cite

View full text Add to dashboard Cite

show abstract

“…In this latter context, it has been suggested that other BC200 RNA-binding proteins can hinder protein binding to a specific BC200 RNA motif (12). Notably, it has also been reported that hnRNP E1 and E2 restore BC200 RNA-inhibited translation by binding the C-rich domain (32). Therefore, it is possible that individual RNA motifs may be differently involved in BC 200 RNA-mediated translational regulation in a cell-type-specific and spatially distinct manner.…”

Section: Discussionmentioning

confidence: 99%

Functional Analysis of RNA Motifs Essential for BC200 RNA-mediated Translational Regulation

2020

Self Cite

View full text Add to dashboard Cite

Brain cytoplasmic 200 RNA (BC200 RNA) is proposed to act as a local translational modulator by inhibiting translation after being targeted to neuronal dendrites. However, the mechanism by which BC200 RNA inhibits translation is not fully understood. Although a detailed functional analysis of RNA motifs is essential for understanding the BC200 RNA-mediated translation-inhibition mechanism, there is little relevant research on the subject. Here, we performed a systematic domain-dissection analysis of BC200 RNA to identify functional RNA motifs responsible for its translationalinhibition activity. Various RNA variants were assayed for their ability to inhibit translation of luciferase mRNA in vitro. We found that the 111-200-nucleotide region consisting of part of the Alu domain as well as the A/C-rich domain (consisting of both the A-rich and C-rich domains) is most effective for translation inhibition. Surprisingly, we also found that individual A-rich, A/C-rich, and Alu domains can enhance translation but at different levels for each domain, and that these enhancing effects manifest as cap-dependent translation. [BMB Reports 2020; 53(2): 94-99] BMB Rep. 2020; 53(2): 94-99 www.bmbreports.org

show abstract

“…Other work has demonstrated a higher affinity of hnRNP E1 for hnRNP D than hnRNP E2 [17], and hnRNP E1 and hnRNP E2 have differential responses to hypoxic stress [39]. Both hnRNP E1 and hnRNP E2 can regulate BC200 RNA-mediated translation inhibition but not through the same control mechanism [16]. Therefore, despite the high degree of sequence similarities between hnRNP E1 and hnRNP E2 isoforms, they each have distinct non-redundant cellular functions.…”

Section: Discussionmentioning

confidence: 99%

Heterogeneous ribonuclear protein E2 (hnRNP E2) is associated with TDP-43-immunoreactive neurites in Semantic Dementia but not with other TDP-43 pathological subtypes of Frontotemporal Lobar Degeneration

Davidson

Robinson

Flood

et al. 2017

acta neuropathol commun

View full text Add to dashboard Cite

Frontotemporal Lobar Degeneration (FTLD) encompasses certain related neurodegenerative disorders which alter personality and cognition. Heterogeneous ribonuclear proteins (hnRNPs) maintain RNA metabolism and changes in their function may underpin the pathogenesis of FTLD. Immunostaining for hnRNP E2 was performed on sections of frontal and temporal cortex with hippocampus from 80 patients with FTLD, stratified by pathology into FTLD-tau and FTLD-TDP type A, B and C subtypes, and by genetics into patients with C9orf72 expansions, MAPT or GRN mutations, or those with no known mutation, and on 10 healthy controls. Semi-quantitative analysis assessed hnRNP staining in frontal and temporal cortex, and in dentate gyrus (DG) of hippocampus, in the different pathology and genetic groups. We find that hnRNP E2 immunostaining detects the TDP-43 positive dystrophic neurites (DN) within frontal and temporal cortex, and the neuronal cytoplasmic inclusions (NCI) seen in DG granule cells, characteristic of patients with Semantic Dementia (SD) and type C TDP-43 pathology, but did not detect TDP-43 or tau inclusions in any of the other pathological or genetic variants of FTLD. Double immunofluorescence for hnRNP E2 and TDP-43 showed most TDP-43 immunopositive DN to contain hnRNP E2. Present findings indicate an association between TDP-43 and hnRNP E2 which might underlie the pathogenetic mechanism of this form of FTLD.

show abstract

Regulation of BC200 RNA‐mediated translation inhibition by hnRNP E1 and E2

Cited by 19 publications

References 46 publications

Identifying the cellular location of brain cytoplasmic 200 RNA using an RNA-recognizing antibody

Identifying the cellular location of brain cytoplasmic 200 RNA using an RNA-recognizing antibody

Functional Analysis of RNA Motifs Essential for BC200 RNA-mediated Translational Regulation

Heterogeneous ribonuclear protein E2 (hnRNP E2) is associated with TDP-43-immunoreactive neurites in Semantic Dementia but not with other TDP-43 pathological subtypes of Frontotemporal Lobar Degeneration

Contact Info

Product

Resources

About