Evidence map›Paper›PMID 10454563›Full record

ArticleMolecular and cellular biology1999

Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins.

H Ma, H Hong, S M Huang, R A Irvine, P Webb, P J Kushner, G A Coetzee, M R Stallcup

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
15.1field-weighted citation impact, top 1% 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

75 citing papers in PubMed, 255 citations in OpenAlex.

  1. A Spatiotemporal Atlas of the Androgen Receptor Proximal Interactome.bioRxiv : the preprint server for biology · 2026
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15 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

H MaDepartments of Pathology, University of Southern California, Los Angeles, California 90033, USA.
H Hong
S M Huang
R A Irvine
P Webb
P J Kushner
G A Coetzee
M R Stallcup
University of California, San Francisco · USUniversity of Southern California · US

Funding

Transcription activation by nuclear coactivatorsR01DK043093 · NIDDK · UNIVERSITY OF SOUTHERN CALIFORNIA · PI STALLCUP, MICHAEL R · 1990 to 2019
$6.5M
Mechanisms of Bladder Cancer ProgressionR01CA072821 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LOKESHWAR, VINATA B · 2003 to 2014
$2.4M
MODULATION OF ESTROGEN RECEPTOR FUNCTION BY COREPRESSORSR01DK051083 · NIDDK · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KUSHNER, PETER J · 1996 to 2003
$878k
MECHANISIMS OF BLADDER CANCER PROGRESSIONR29CA072821 · NCI · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI LOKESHWAR, VINATA B · 1997 to 2001
$214k
NCI NIH HHS CA/OD72821NIDDK NIH HHS DK43093NIDDK NIH HHS DK51083NIDDK NIH HHS R01 DK043093NIDDK NIH HHS R01 DK051083
6 · The paper itself

Abstract

Members of the 160-kDa nuclear receptor coactivator family (p160 coactivators) bind to the conserved AF-2 activation function found in the hormone binding domains of nuclear receptors (NR) and are potent transcriptional coactivators for NRs. Here we report that the C-terminal region of p160 coactivators glucocorticoid receptor interacting protein 1 (GRIP1), steroid receptor coactivator 1 (SRC-1a), and SRC-1e binds the N-terminal AF-1 activation function of the androgen receptor (AR), and p160 coactivators can thereby enhance transcriptional activation by AR. While they all interact efficiently with AR AF-1, these same coactivators have vastly different binding strengths with and coactivator effects on AR AF-2. p160 activation domain AD1, which binds secondary coactivators CREB binding protein (CBP) and p300, was previously implicated as the principal domain for transmitting the activating signal to the transcription machinery. We identified a new highly conserved motif in the AD1 region which is important for CBP/p300 binding. Deletion of AD1 only partially reduced p160 coactivator function, due to signaling through AD2, another activation domain located at the C-terminal end of p160 coactivators. C-terminal coactivator fragments lacking AD1 but containing AD2 and the AR AF-1 binding site served as efficient coactivators for full-length AR and AR AF-1. The two signal input domains (one that binds NR AF-2 domains and one that binds AF-1 domains of some but not all NRs) and the two signal output domains (AD1 and AD2) of p160 coactivators played different relative roles for two different NRs: AR and thyroid hormone receptor.

Indexed as

AnimalsBinding SitesCell LineHistone AcetyltransferasesHumansMolecular WeightNuclear ProteinsNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 2Receptors, AndrogenReceptors, Cytoplasmic and NuclearReceptors, SteroidReceptors, Thyroid HormoneRecombinant Fusion ProteinsSignal TransductionTrans-ActivatorsHistone AcetyltransferasesNCOA1 protein, humanNCOA2 protein, humanNuclear ProteinsNuclear Receptor Coactivator 1Nuclear Receptor Coactivator 2Receptors, AndrogenReceptors, Cytoplasmic and NuclearReceptors, SteroidReceptors, Thyroid HormoneRecombinant Fusion ProteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID10454563
PMCPMC84548
OpenAlexW2124174146

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.