Evidence map›Paper›PMID 21768307›Full record

ArticleMolecular and cellular biology2011

Human GTPases associate with RNA polymerase II to mediate its nuclear import.

Clément Carré, Ramin Shiekhattar

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

31 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Structure of cytoplasmic RNA polymerase II.Nature communications · 2026
    Article
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  7. Article
  8. Article
  9. Biogenesis of RNA Polymerases in Yeast.Frontiers in molecular biosciences · 2021
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 2 institutions in 2 countries.

Clément CarréThe Wistar Institute, 3601 Spruce Street, Philadelphia, PA 19104, USA. ccarre@wistar.org
Ramin Shiekhattar
Pompeu Fabra University · ESThe Wistar Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Small GTPases share a biochemical mechanism and act as binary molecular switches. One important function of small GTPases in the cell is nucleocytoplasmic transport of both proteins and RNA. Here, we show the stable association of human GPN1 and GPN3, small GTPases related to Ran, with RNA polymerase II (RNAPII) isolated from either the cytoplasmic or nuclear fraction. GPN1 and GPN3 directly interact with RNAPII subunit 7 (RPB7)/RPB4 and the C-terminal domain (CTD) of RNAPII. Depletion of GPN1 or GPN3 using small interfering RNAs led to decreased RNAPII levels in the nucleus and an accumulation of this enzyme in the cytoplasm of human cells. Furthermore, isolation of a GPN1/GPN3/RNAPII complex from stable cell lines expressing a dominant negative GPN1 harboring mutations in the GTP-binding pocket demonstrated a role for these proteins in nuclear import of RNAPII. Thus, GPN1/GPN3 define a new family of small GTPases that are specialized for the transport of RNA polymerase II into the nucleus.

Indexed as

Active Transport, Cell NucleusAmino Acid SequenceGTP-Binding ProteinsGTP PhosphohydrolasesHEK293 CellsHeLa CellsHumansMolecular Sequence DataMultiprotein ComplexesProtein Structure, TertiaryProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase IIGPN1 protein, humanGPN3 protein, humanGTP-Binding ProteinsGTP PhosphohydrolasesMultiprotein ComplexesProtein SubunitsRecombinant Fusion ProteinsRNA Polymerase II

Identifiers

PMID21768307
PMCPMC3187354
OpenAlexW2004887075

What OpenQuestion holds

Textmetadata
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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.