Evidence map›Paper›PMID 17030088›Full record

ArticleMolecular and cellular endocrinology2007

APPL1, APPL2, Akt2 and FOXO1a interact with FSHR in a potential signaling complex.

Cheryl A Nechamen, Richard M Thomas, James A Dias

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular endocrinology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

49 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
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  11. Glycosylation Pattern andFrontiers in endocrinology · 2019
    Article
  12. Review
  13. Endocytosis is required for CThe Journal of biological chemistry · 2018
    Article
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  19. Experimental verification of a predicted novel microRNA located in human PIK3CA gene with a potential oncogenic function in colorectal cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  20. Adiponectin signaling and function in insulin target tissues.Journal of molecular cell biology · 2016
    Review
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

3 authors at 1 institution in 1 country.

Cheryl A NechamenWadsworth Center, David Axelrod Institute for Public Health, New York State Department of Health, 120 New Scotland Avenue, Albany, NY 12208, United States.
Richard M Thomas
James A Dias
New York State Department of Health · 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

A number of signaling proteins have been demonstrated to interact with follicle stimulating hormone (FSH) receptor (FSHR), including APPL1, 14-3-3tau and Akt2. To further define the repertoire of proteins involved in FSH-induced signal transduction, several signaling and adapter proteins were examined for the ability to associate with FSHR. This report shows that, in addition to APPL1, FSHR interacts with FOXO1a and APPL2. Moreover, APPL1 and APPL2 associate with one another via the N-terminus of APPL1, presumably via the Bin-Amphiphysin-Rvs (BAR) domain. The interactions between FSHR and APPL2 and between FSHR and FOXO1a evidently are distinct since FOXO1a does not associate with either APPL1 or with APPL2. Though APPL1 and APPL2 show some similarity in primary sequence, APPL1 associates with Akt2, whereas APPL2 does not. This is the first documented difference in function between APPL1 and APPL2. These results suggest that FSHR, APPL1, APPL2, Akt2 and FOXO1a are organized into distinct scaffolding networks in the cell. Accordingly, the spatial organization of signaling and adapter proteins with FSHR likely facilitates and finely regulates the signal transduction induced by FSH.

Indexed as

Signal TransductionAdaptor Proteins, Signal TransducingCarrier ProteinsFollicle Stimulating HormoneForkhead Transcription FactorsHumansImmediate-Early ProteinsImmunoprecipitationMutant ProteinsPhosphorylationProtein BindingProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktReceptors, FSHSerum-Glucocorticoid Regulated KinasesAdaptor Proteins, Signal TransducingCarrier ProteinsFollicle Stimulating HormoneForkhead Transcription FactorsImmediate-Early ProteinsMutant ProteinsProtein Serine-Threonine KinasesProto-Oncogene Proteins c-aktReceptors, FSHSerum-Glucocorticoid Regulated Kinases

Identifiers

PMID17030088
PMCPMC1782224
OpenAlexW2092321734

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.