Evidence map›Paper›PMID 20600589›Full record

ArticleMolecular and cellular endocrinology2010

Emerging roles for the FSH receptor adapter protein APPL1 and overlap of a putative 14-3-3τ interaction domain with a canonical G-protein interaction site.

James A Dias, Smita D Mahale, Cheryl A Nechamen, Olga Davydenko, Richard M Thomas, Alfredo Ulloa-Aguirre

Abstract read
In one paragraph

Article in Molecular and cellular endocrinology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

19 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Review
  3. ERβ Regulation of Gonadotropin Responses during Folliculogenesis.International journal of molecular sciences · 2021
    Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Molecular Mechanisms of Action of FSH.Frontiers in endocrinology · 2019
    Review
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  10. Review
  11. Review
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  15. Article
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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

6 authors at 5 institutions in 3 countries.

James A DiasWadsworth Center, New York State Dept of Health, Albany, NY, United States. james.dias@wadsworth.org
Smita D Mahale
Cheryl A Nechamen
Olga Davydenko
Richard M Thomas
Alfredo Ulloa-Aguirre
Wadsworth Center · USMexican Social Security Institute · MXNational Institute for Research in Reproductive Health · INNew York State Department of Health · USUnion College · US

Funding

STRUCTURE AND CELLULAR BIOLOGY OF GPH RECEPTORSR01HD018407 · NICHD · WADSWORTH CENTER · PI A, DIAS JAMES · 1985 to 2010
$2.4M
NICHD NIH HHS HD18407NICHD NIH HHS R01 HD018407
6 · The paper itself

Abstract

The interaction of cytoplasmic proteins with intracellular domains of membrane receptors can occur at several opportunities, including: during biosynthesis, while in membrane residency and during internalization and recycling following ligand binding. Since the initial discovery that it interacts with the FSH receptor (FSHR) together with additional members of a potential signaling complex, APPL1 has been shown to interact with a variety of membrane receptors. Recent subcellular localizations of APPL1 place it in dynamic and varied venues in the cell, including at the cell membrane, the nucleus and the early endosomes. Another adapter protein family the 14-3-3 proteins, are largely recognized as binding to phosphorylation sites but recent work demonstrated that in the case of FSHR, the 14-3-3 site overlaps with the canonical G-protein binding site. G-proteins appear to sample the environment and exchange between the membrane and intracellular locales and this binding could be mediated by or modulated by receptor interactions at the 14-3-3 binding site. Observations that multiple proteins can interact with cytoplasmic domains of GPCRs leads to the inescapable conclusion that either the interactions occur via orderly replacement or exchange, or that receptors are simultaneously occupied by a variety of adapters and effectors or even that oligomers of dimeric GPCRs provide for platforms that can simultaneously interact with effectors and adaptors.

Indexed as

14-3-3 ProteinsAdaptor Proteins, Signal TransducingBinding SitesGTP-Binding ProteinsHumansProtein BindingReceptors, FSH14-3-3 ProteinsAdaptor Proteins, Signal TransducingAPPL1 protein, humanGTP-Binding ProteinsReceptors, FSH

Identifiers

PMID20600589
PMCPMC2946492
OpenAlexW2006970315

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.