Evidence map›Paper›PMID 20554852›Full record

ArticleNucleic acids research2010

Phosphorylation of the RNase III enzyme Drosha at Serine300 or Serine302 is required for its nuclear localization.

Xiaoli Tang, Yingjie Zhang, Lynne Tucker, Bharat Ramratnam

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

56 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
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  4. Regulation of the microprocessor by post-translational modifications.Frontiers in cell and developmental biology · 2025
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  13. Trans-acting regulators of ribonuclease activity.Journal of microbiology (Seoul, Korea) · 2021
    Review
  14. Evolution of MicroRNA Biogenesis Genes in the Sterlet (International journal of molecular sciences · 2020
    Article
  15. Review
  16. Article
  17. Review
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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

4 authors at 1 institution in 1 country.

Xiaoli TangLaboratory of Retrovirology, Division of Infectious Diseases, Department of Medicine, Warren Alpert Medical School of Brown University, Providence, RI 02903, USA.
Yingjie Zhang
Lynne Tucker
Bharat Ramratnam
Brown University · US

Funding

Translational ScienceP30AI042853 · NIAID · MIRIAM HOSPITAL · PI LARRY K BROWN · 1998 to 2026
$51.7M
HIV and Other Infectious Consequences of Substance UseT32DA013911 · NIDA · MIRIAM HOSPITAL · PI TRACI C GREEN, JOSIAH D RICH · 2001 to 2026
$9.6M
TYORISINE PHOSPHATASE SHP2 IN HEMATOPOIETIC STEM CELL PROPERTY MAINTENANCEP20RR025179 · NCRR · RHODE ISLAND HOSPITAL · PI ALIOTTA, JASON M · 2009 to 2011
$6.4M
Overcoming HIV-1 resistance to RNA InterferenceR01AI058697 · NIAID · RHODE ISLAND HOSPITAL · PI RAMRATNAM, BHARAT · 2005 to 2009
$1.6M
NCRR NIH HHS P20 RR025179NCRR NIH HHS P20RR025179NIAID NIH HHS P30AI042853NIAID NIH HHS R01 AI058697NIAID NIH HHS R01AI058697NIDA NIH HHS T32 DA013911NIDA NIH HHS T32DA013911
6 · The paper itself

Abstract

The RNaseIII enzyme Drosha plays a pivotal role in microRNA (miRNA) biogenesis by cleaving primary miRNA transcripts to generate precursor miRNA in the nucleus. The RNA binding and enzymatic domains of Drosha have been characterized and are on its C-terminus. Its N-terminus harbors a nuclear localization signal. Using a series of truncated Drosha constructs, we narrowed down the segment responsible for nuclear translocation to a domain between aa 270 and aa 390. We further identified two phosphorylation sites at Serine300 (S300) and Serine302 (S302) by mass spectrometric analysis. Double mutations of S→A at S300 and S302 completely disrupted nuclear localization. Single mutation of S→A at S300 or S302, however, had no effect on nuclear localization indicating that phosphorylation at either site is sufficient to locate Drosha to the nucleus. Furthermore, mimicking phosphorylation status by mutating S→E at S300 and/or S→D at S302 restored nuclear localization. Our findings add a further layer of complexity to the molecular anatomy of Drosha as it relates to miRNA biogenesis.

Indexed as

Cell LineCell NucleusHumansMass SpectrometryMicroRNAsNuclear Localization SignalsPhosphorylationRibonuclease IIIRNA Processing, Post-TranscriptionalSequence DeletionSerineDROSHA protein, humanMicroRNAsNuclear Localization SignalsRibonuclease IIISerine

Identifiers

PMID20554852
PMCPMC2965249
OpenAlexW2054356425

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.