Evidence map›Paper›PMID 9256445›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

mRNA binding protein mrnp 41 localizes to both nucleus and cytoplasm.

D Kraemer, G Blobel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Virus Infection and mRNA Nuclear Export.International journal of molecular sciences · 2023
    Review
  6. Structure and Function of the Nuclear Pore Complex.Cold Spring Harbor perspectives in biology · 2022
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Vesiculoviral matrix (M) protein occupies nucleic acid binding site at nucleoporin pair (Rae1 • Nup98).Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  14. Viral subversion of nucleocytoplasmic trafficking.Traffic (Copenhagen, Denmark) · 2014
    Review
  15. Article
  16. Review
  17. Article
  18. Nuclear transport and the mitotic apparatus: an evolving relationship.Cellular and molecular life sciences : CMLS · 2010
    Review
  19. Structural and functional analysis of the interaction between the nucleoporin Nup98 and the mRNA export factor Rae1.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  20. Cohesin subunit SMC1 associates with mitotic microtubules at the spindle pole.Proceedings of the National Academy of Sciences of the United States of America · 2008
    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

2 authors at 2 institutions in 1 country.

D KraemerLaboratory of Cell Biology, Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021, USA.
G Blobel
Howard Hughes Medical Institute · USRockefeller University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have identified and molecularly characterized a human protein with a Mr of 40,880 Da. After UV irradiation of HeLa cells, this protein was cross-linked to poly(A)-containing mRNA and was therefore designated mrnp 41 (for mRNA binding protein of 41 kDa). Cell fractionation and immunoblotting showed mrnp 41 in both the cytoplasm and the nucleus and particularly in the nuclear envelope. Immunofluorescence microscopy localized mrnp 41 to distinct foci in the nucleoplasm, to the nuclear rim, and to meshwork-like structures throughout the cytoplasm. The cytoplasmic meshwork staining was disrupted by prior treatment of cells with the actin filament- or microtubule-disrupting drugs cytochalasin or nocodazole, respectively, suggesting association of mrnp 41 with the cytoskeleton. Double immunofluorescence with antibodies against mrnp 41 and the cytoplasmic poly(A) binding protein showed colocalization to the cytoplasmic meshwork. Immunogold electronmicroscopy confirmed mrnp 41's cytoplasmic and nucleoplasmic localization and revealed a striking labeling of nuclear pore complexes. Together these data suggest that mrnp 41 may function in nuclear export of mRNPs and/or in cytoplasmic transport on, or attachment to, the cytoskeleton. Consistent with a role of mrnp 41 in nuclear export are previous reports that mutations in homologs of mrnp 41 in Schizosaccharomyces pombe, designated Rae1p, or in Saccharomyces cerevisiae, designated Gle2p, result in mRNA accumulation in the nucleus although it is presently not known whether these homologs are mRNA binding proteins as well.

Indexed as

Nuclear Matrix-Associated ProteinsNucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsAmino Acid SequenceAnimalsCell NucleusCytoplasmFluorescent Antibody Technique, IndirectHeLa CellsHumansImmunohistochemistryLiverMolecular Sequence DataNuclear Pore Complex ProteinsRatsRNA-Binding ProteinsGLE2 protein, S cerevisiaeNuclear Matrix-Associated ProteinsNuclear Pore Complex ProteinsNucleocytoplasmic Transport ProteinsRAE1 protein, humanRNA-Binding ProteinsRNA, MessengerSaccharomyces cerevisiae Proteins

Identifiers

PMID9256445
PMCPMC23064
OpenAlexW2033680770

What OpenQuestion holds

Textmetadata
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.