Evidence map›Paper›PMID 10026152›Full record

ArticleThe Journal of biological chemistry1999

Oligomerization and scaffolding functions of the erythropoietin receptor cytoplasmic tail.

S S Watowich, K D Liu, X Xie, S Y Lai, A Mikami, G D Longmore, M A Goldsmith

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

12 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The erythropoietin receptor: molecular structure and hematopoietic signaling pathways.Journal of investigative medicine : the official publication of the American Federation for Clinical Research · 2011
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Erythropoietin receptors that signal through Stat5 or Stat3 support fetal liver and adult erythropoiesis: lack of specificity of stat signals during red blood cell development.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2000
    Article
  10. Article
  11. Article
  12. 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

7 authors at 3 institutions in 1 country.

S S WatowichDepartment of Immunology, M. D. Anderson Cancer Center, Houston, Texas 77030, USA.
K D Liu
X Xie
S Y Lai
A Mikami
G D Longmore
M A Goldsmith
University of California, San Francisco · USThe University of Texas MD Anderson Cancer Center · USWashington University in St. Louis · US

Funding

TRANSCRIPTION FACTOR GATA-1 IN TERMINAL ERYTHROID DEVELOPMENTP01HL032262 · NHLBI · CHILDREN'S HOSPITAL BOSTON · PI ORKIN, STUART H · 1985 to 2021
$38.9M
Signal Transduction by Cytokine Receptors in VivoR01GM054351 · NIGMS · J. DAVID GLADSTONE INSTITUTES · PI GREENE, WARNER C · 1995 to 2004
$1.3M
MOLECULAR MECHANISMS CYTOKINE RECEPTOR SIGNALINGR01CA077447 · NCI · UNIVERSITY OF TEXAS MD ANDERSON CAN CTR · PI WATOWICH, STEPHANIE S · 1998 to 2000
$250k
NCI NIH HHS CA-77447NCI NIH HHS R01 CA077447NHLBI NIH HHS HL32262NHLBI NIH HHS P01 HL032262NIGMS NIH HHS GM-54351NIGMS NIH HHS R01 GM054351
6 · The paper itself

Abstract

Signal transduction by the erythropoietin receptor (EPOR) is activated by ligand-mediated receptor homodimerization. However, the relationship between extracellular and intracellular domain oligomerization remains poorly understood. To assess the requirements for dimerization of receptor cytoplasmic sequences for signaling, we overexpressed mutant EPORs in combination with wild-type (WT) EPOR to drive formation of heterodimeric (i.e. WT-mutant) receptor complexes. Dimerization of the membrane-proximal portion of the EPOR cytoplasmic region was found to be critical for the initiation of mitogenic signaling. However, dimerization of the entire EPOR cytoplasmic region was not required. To examine this process more closely, we generated chimeras between the intracellular and transmembrane portions of the EPOR and the extracellular domains of the interleukin-2 receptor beta and gammac chains. These chimeras allowed us to assess more precisely the signaling role of each receptor chain because only heterodimers of WT and mutant receptor chimeras form in the presence of interleukin-2. Coexpression studies demonstrated that a functional receptor complex requires the membrane-proximal region of each receptor subunit in the oligomer to permit activation of JAK2 but only one membrane-distal tail to activate STAT5 and to support cell proliferation. Thus, this study defines key relationships involved in the assembly and activation of the EPOR signal transduction complex which may be applicable to other homodimeric cytokine receptors.

Indexed as

Base SequenceBiopolymersCell DivisionCell LineCytoplasmOligodeoxyribonucleotidesReceptors, ErythropoietinSignal TransductionBiopolymersOligodeoxyribonucleotidesReceptors, Erythropoietin

Identifiers

PMID10026152
PMCPMC2388248
OpenAlexW2005202995

What OpenQuestion holds

Texttitle and abstract
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.