Evidence map›Paper›PMID 27185895›Full record

ArticleNucleic acids research2016

Alternative splicing affects the subcellular localization of Drosha.

Steffen Link, Stefanie E Grund, Sven Diederichs

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.7field-weighted citation impact, top 7% 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

40 citing papers in PubMed, 56 citations in OpenAlex.

  1. Subcellular localization as a driver of protein function.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
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  5. Molecular therapy. Nucleic acids · 2024
    Article
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  10. Review
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  17. Frontiers in endocrinology · 2022
    Article
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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

3 authors at 2 institutions in 1 country.

Steffen LinkDivision of RNA Biology and Cancer (B150), German Cancer Research Center (DKFZ), Heidelberg, Germany Institute of Pathology, University of Heidelberg, Heidelberg, Germany.
Stefanie E GrundDivision of RNA Biology and Cancer (B150), German Cancer Research Center (DKFZ), Heidelberg, Germany Institute of Pathology, University of Heidelberg, Heidelberg, Germany.
Sven DiederichsDivision of Cancer Research, Dept. of Thoracic Surgery, Medical Center-University of Freiburg, Freiburg, Germany Faculty of Medicine, University of Freiburg, Freiburg, Germany Division of RNA Biology and Cancer (B150), German Cancer Research Center (DKFZ), Heidelberg, Germany German Cancer Consortium (DKTK), Freiburg, Germany Institute of Pathology, University of Heidelberg, Heidelberg, Germany Spemann Graduate School of Biology and Medicine (SGBM), University of Freiburg, Freiburg, Germany s.diederichs@dkfz.de.
German Cancer Research Center · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The RNase III enzyme Drosha is a key factor in microRNA (miRNA) biogenesis and as such indispensable for cellular homeostasis and developmental processes. Together with its co-factor DGCR8, it converts the primary transcript (pri-miRNA) into the precursor hairpin (pre-miRNA) in the nucleus. While the middle and the C-terminal domain are crucial for pri-miRNA processing and DGCR8 binding, the function of the N-terminus remains cryptic. Different studies have linked this region to the subcellular localization of Drosha, stabilization and response to stress. In this study, we identify alternatively spliced Drosha transcripts that are devoid of a part of the arginine/serine-rich (RS-rich) domain and expressed in a large set of human cells. In contrast to their expected habitation, we find two isoforms also present in the cytoplasm, while the other two isoforms reside exclusively in the nucleus. Their processing activity for pri-miRNAs and the binding to co-factors remains unaltered. In multiple cell lines, the endogenous mRNA expression of the Drosha isoforms correlates with the localization of endogenous Drosha proteins. The pri-miRNA processing efficiency is not significantly different between groups of cells with or without cytoplasmic Drosha expression. In summary, we discovered novel isoforms of Drosha with differential subcellular localization pointing toward additional layers of complexity in the regulation of its activity.

Indexed as

Alternative SplicingAmino Acid SequenceAnimalsCell LineGene Expression RegulationHumansMicroRNAsNuclear Localization SignalsOrgan SpecificityProtein BindingProtein TransportRibonuclease IIIRNA-Binding ProteinsRNA InterferenceRNA TransportSubstrate SpecificityMicroRNAsNuclear Localization SignalsRibonuclease IIIRNA-Binding Proteins

Identifiers

PMID27185895
PMCPMC4914122
OpenAlexW2396839178

What OpenQuestion holds

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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.