Evidence map›Paper›PMID 29642903›Full record

ArticleJournal of biomedical science2018

Functional domains of SP110 that modulate its transcriptional regulatory function and cellular translocation.

Jia-Shiun Leu, So-Yi Chang, Chia-Yu Mu, Mei-Ling Chen, Bo-Shiun Yan

Open access · diamondAbstract read
In one paragraph

Article in Journal of biomedical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
0.7field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 16 citations in OpenAlex.

  1. Pooled it
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  10. The Fate of Speckled Protein 100 (Sp100) During Herpesviruses Infection.Frontiers in cellular and infection microbiology · 2020
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Jia-Shiun LeuInstitute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan.
So-Yi ChangInstitute of Biochemistry and Molecular Biology, National Taiwan University Medical College, Taipei, Taiwan.
Chia-Yu MuInstitute of Biochemistry and Molecular Biology, National Taiwan University Medical College, Taipei, Taiwan.
Mei-Ling ChenGraduate Institute of Oncology, National Taiwan University Medical College, Taipei, Taiwan. meilingchen88@ntu.edu.tw.
Bo-Shiun YanInstitute of Biochemistry and Molecular Biology, National Taiwan University Medical College, Taipei, Taiwan. bsyan@ntu.edu.tw.ORCID http://orcid.org/0000-0002-9613-4788
National Taiwan University · TWNational Yang Ming Chiao Tung University · TW

Funding

Ministry of Science and Technology, Taiwan 104-2314-B-002-075-Ministry of Science and Technology, Taiwan 106-2320-B-002-020-Ministry of Science and Technology, Taiwan NSC 100-2320-B-002-106-Ministry of Science and Technology, Taiwan NSC 100-2321-B-002-009-Ministry of Science and Technology, Taiwan NSC 101-2320-B-002-022-Ministry of Science and Technology, Taiwan NSC 101-2321-B-002-001-Ministry of Science and Technology, Taiwan NSC 103-2314-B-002-083-Ministry of Science and Technology, Taiwan NSC 103-2320-B-002-044-MY3Ministry of Science and Technology, Taiwan NSC 97-2320-B-010-006-MY3Ministry of Science and Technology, Taiwan NSC 99- 2320-B-002-078-MY3Ministry of Science and Technology, Taiwan NSC 99-2321-B-002-022-
6 · The paper itself

Abstract

backgroundSP110, an interferon-induced nuclear protein, belongs to the SP100/SP140 protein family. Very recently, we showed that SP110b, an SP110 isoform, controls host innate immunity to Mycobacterium tuberculosis infection by regulating nuclear factor-κB (NF-κB) activity. However, it remains unclear how the structure of SP110 relates to its cellular functions. In this study, we provide experimental data illustrating the protein domains that are responsible for its functions.

methodsWe examined the effects of SP110 isoforms and a series of deletion mutants of SP110 on transcriptional regulation by luciferase reporter assays. We also employed confocal microscopy to determine the cellular distributions of enhanced green fluorescent protein-tagged SP110 isoforms and SP110 mutants. In addition, we performed immunoprecipitation and Western blotting analyses to identify the regions of SP110 that are responsible for protein interactions.

resultsUsing reporter assays, we first demonstrated that SP110 isoforms have different regulatory effects on NF-κB-mediated transcription, supporting the notion that SP110 isoforms may have distinct cellular functions. Analysis of deletion mutants of SP110 showed that the interaction of the N-terminal fragment (amino acids 1-276) of SP110 with p50, a subunit of NF-κB, in the cytoplasm plays a crucial role in the down-regulation of the p50-driven tumor necrosis factor-α (TNFα) promoter activity in the nucleus, while the middle and C-terminal regions of SP110 localize it to various cellular compartments. Surprisingly, a nucleolar localization signal (NoLS) that contains one monopartite nuclear localization signal (NLS) and one bipartite NLS was identified in the middle region of SP110. The identification of a cryptic NoLS in the SP110 suggests that although this protein forms nuclear speckles in the nucleoplasm, it may be directed into the nucleolus to carry out distinct functions under certain cellular conditions.

conclusionsThe findings from this study elucidating the multidomain structure of the SP110 not only identify functional domains of SP110 that are required for transcriptional regulation, cellular translocation, and protein interactions but also implicate that SP110 has additional functions through its unexpected activity in the nucleolus.

Indexed as

Gene Expression RegulationTranscription, GeneticCell Line, TumorHEK293 CellsHumansMinor Histocompatibility AntigensNF-kappa BNuclear ProteinsProtein DomainsProtein IsoformsMinor Histocompatibility AntigensNF-kappa BNuclear ProteinsProtein IsoformsSp110 protein, humanCellular translocationFunctional domainNuclear localization signalNucleolar localization signalTranscriptional regulation

Identifiers

PMID29642903
PMCPMC5894228
OpenAlexW2801344782

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.