Evidence map›Paper›PMID 25092175›Full record

ArticleBlood2014

Histones to the cytosol: exportin 7 is essential for normal terminal erythroid nuclear maturation.

Shilpa M Hattangadi, Sandra Martinez-Morilla, Heide Christine Patterson, Jiahai Shi, Karly Burke, Amalia Avila-Figueroa, Srividhya Venkatesan, Junxia Wang, Katharina Paulsen, Dirk Görlich and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Erythroblast enucleation at a glance.Journal of cell science · 2024
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Extra-nuclear histones: origin, significance and perspectives.Molecular and cellular biochemistry · 2022
    Review
  16. Article
  17. Review
  18. Review
  19. Proteomic/transcriptomic analysis of erythropoiesis.Current opinion in hematology · 2021
    Review
  20. 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

12 authors at 6 institutions in 3 countries.

Shilpa M HattangadiWhitehead Institute for Biomedical Research, Cambridge, MA.
Sandra Martinez-Morilla
Heide Christine Patterson
Jiahai Shi
Karly Burke
Amalia Avila-Figueroa
Srividhya Venkatesan
Junxia Wang
Katharina Paulsen
Dirk Görlich
Maki Murata-Hori
Harvey F Lodish
Whitehead Institute for Biomedical Research · USMax Planck Institute for Biophysical Chemistry · DEBoston Children's Hospital · USMassachusetts Institute of Technology · USNational University of Singapore · SGTemasek Life Sciences Laboratory · SG

Funding

TRANSCRIPTION FACTOR GATA-1 IN TERMINAL ERYTHROID DEVELOPMENTP01HL032262 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI YIEN, YVETTE Y · 1985 to 2021
$38.9M
Yale University Clinical and Translational Science Award ProgramUL1TR000142 · NCATS · YALE UNIVERSITY · PI SHERWIN, ROBERT S · 2012 to 2015
$31.8M
Elucidating the Role of Nuclear Protein Export in Erythroid Nuclear CondensationR01DK102889 · NIDDK · YALE UNIVERSITY · PI HATTANGADI, SHILPA MANOHAR · 2014 to 2017
$1.3M
Syk in Mitochondrial Stress Signaling and Insulin ResistanceK08GM102718 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI PATTERSON, HEIDE CHRISTINE · 2012 to 2015
$800k
Transcriptional Regulatory Networks Active in Terminal Erythroid DifferentiationK08DK076848 · NIDDK · DANA-FARBER CANCER INST · PI HATTANGADI, SHILPA MANOHAR · 2007 to 2011
$723k
NCATS NIH HHS UL1 TR000142NHLBI NIH HHS P01 HL032262NHLBI NIH HHS P01 HL32262NIDDK NIH HHS K08 DK076848NIDDK NIH HHS R01 DK102889NIGMS NIH HHS K08 GM102718
6 · The paper itself

Abstract

Global nuclear condensation, culminating in enucleation during terminal erythropoiesis, is poorly understood. Proteomic examination of extruded erythroid nuclei from fetal liver revealed a striking depletion of most nuclear proteins, suggesting that nuclear protein export had occurred. Expression of the nuclear export protein, Exportin 7 (Xpo7), is highly erythroid-specific, induced during erythropoiesis, and abundant in very late erythroblasts. Knockdown of Xpo7 in primary mouse fetal liver erythroblasts resulted in severe inhibition of chromatin condensation and enucleation but otherwise had little effect on erythroid differentiation, including hemoglobin accumulation. Nuclei in Xpo7-knockdown cells were larger and less dense than normal and accumulated most nuclear proteins as measured by mass spectrometry. Strikingly,many DNA binding proteins such as histones H2A and H3 were found to have migrated into the cytoplasm of normal late erythroblasts prior to and during enucleation, but not in Xpo7-knockdown cells. Thus, terminal erythroid maturation involves migration of histones into the cytoplasm via a process likely facilitated by Xpo7.

Indexed as

AnimalsCell NucleusCytosolErythroblastsErythropoiesisGene Knockdown TechniquesHistonesKaryopherinsMiceMice, Inbred C57BLNuclear Proteinsran GTP-Binding ProteinHistonesKaryopherinsNuclear Proteinsran GTP-Binding ProteinRanGTP-binding protein 16

Identifiers

PMID25092175
PMCPMC4168348
OpenAlexW2141881890

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.