Evidence map›Paper›PMID 19220816›Full record

ArticleTraffic (Copenhagen, Denmark)2009

Interdependent nucleocytoplasmic trafficking and interactions of Dis3 with Rrp6, the core exosome and importin-alpha3.

Amy C Graham, Stephanie M Davis, Erik D Andrulis

Open access · bronzeAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Threading the barrel of the RNA exosome.Trends in biochemical sciences · 2013
    Review
  7. Article
  8. Article
  9. Dis3- and exosome subunit-responsive 3' mRNA instability elements.Biochemical and biophysical research communications · 2012
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Characterization of the Drosophila melanogaster Dis3 ribonuclease.Biochemical and biophysical research communications · 2009
    Article
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 1 institution in 1 country.

Amy C GrahamDepartment of Molecular Biology and Microbiology, Case Western Reserve University School of Medicine, Cleveland, OH, USA.
Stephanie M Davis
Erik D Andrulis
Case Western Reserve University · US

Funding

Compartmentalized Exosome Structure and FunctionR01GM072820 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI ANDRULIS, ERIK D · 2006 to 2010
$1.4M
NIGMS NIH HHS GM072820NIGMS NIH HHS R01 GM072820
6 · The paper itself

Abstract

Subcellular compartmentalization of exoribonucleases (RNAses) is an important control mechanism in the temporal and spatial regulation of RNA processing and decay. Despite much progress towards understanding RNAse substrates and functions, we know little of how RNAses are transported and assembled into functional, subcellularly restricted complexes. To gain insight into this issue, we are studying the exosome-binding protein Dis3, a processive 3' to 5' exoribonuclease. Here, we examine the interactions and subcellular localization of the Drosophila melanogaster Dis3 (dDis3) protein. N-terminal domain mutants of dDis3 abolish associations with the 'core' exosome, yet only reduce binding to the 'nuclear' exosome-associated factor dRrp6. We show that nuclear localization of dDis3 requires a C-terminal classic nuclear localization signal (NLS). Consistent with this, dDis3 specifically co-precipitates the NLS-binding protein importin-alpha3. Surprisingly, dDis3 constructs that lack or mutate the C-terminal NLS retain importin-alpha3 binding, suggesting that the interaction is indirect. Finally, we find that endogenous dDis3 and dRrp6 exhibit coordinated nuclear enrichment or exclusion, suggesting that dDis3, Rrp6 and importin-alpha3 interact in a complex independent of the core. We propose that the movement and deposition of this complex is important for the subcellular compartmentalization and regulation of the exosome core.

Indexed as

AnimalsCarrier ProteinsCell NucleusDrosophila melanogasterEndoribonucleasesExoribonucleasesExosomesKaryopherinsMutationNuclear Localization SignalsProtein BindingProtein TransportRibonucleasesCarrier ProteinsEndoribonucleasesExoribonucleasesKaryopherinsNuclear Localization SignalsRibonucleases

Identifiers

PMID19220816
PMCPMC2852473
OpenAlexW1991803961

What OpenQuestion holds

Textmetadata
LicenceTDM
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.