Evidence map›Paper›PMID 27375556›Full record

ReviewFrontiers in endocrinology2016

Role of Protein Phosphorylation and Tyrosine Phosphatases in the Adrenal Regulation of Steroid Synthesis and Mitochondrial Function.

Cristina Paz, Fabiana Cornejo Maciel, Alejandra Gorostizaga, Ana F Castillo, M Mercedes Mori Sequeiros García, Paula M Maloberti, Ulises D Orlando, Pablo G Mele, Cecilia Poderoso, Ernesto J Podesta

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in endocrinology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

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  16. ACTH Action on StAR Biology.Frontiers in neuroscience · 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

10 authors at 2 institutions in 1 country.

Cristina PazDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Fabiana Cornejo MacielDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Alejandra GorostizagaDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Ana F CastilloDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
M Mercedes Mori Sequeiros GarcíaDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Paula M MalobertiDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Ulises D OrlandoDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Pablo G MeleDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Cecilia PoderosoDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Ernesto J PodestaDepartamento de Bioquímica Humana, Facultad de Medicina, Instituto de Investigaciones Biomédicas (INBIOMED), Universidad de Buenos Aires (UBA-CONICET) , Ciudad Autónoma de Buenos Aires , Argentina.
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of Buenos Aires · AR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In adrenocortical cells, adrenocorticotropin (ACTH) promotes the activation of several protein kinases. The action of these kinases is linked to steroid production, mainly through steroidogenic acute regulatory protein (StAR), whose expression and activity are dependent on protein phosphorylation events at genomic and non-genomic levels. Hormone-dependent mitochondrial dynamics and cell proliferation are functions also associated with protein kinases. On the other hand, protein tyrosine dephosphorylation is an additional component of the ACTH signaling pathway, which involves the "classical" protein tyrosine phosphatases (PTPs), such as Src homology domain (SH) 2-containing PTP (SHP2c), and members of the MAP kinase phosphatase (MKP) family, such as MKP-1. PTPs are rapidly activated by posttranslational mechanisms and participate in hormone-stimulated steroid production. In this process, the SHP2 tyrosine phosphatase plays a crucial role in a mechanism that includes an acyl-CoA synthetase-4 (Acsl4), arachidonic acid (AA) release and StAR induction. In contrast, MKPs in steroidogenic cells have a role in the turn-off of the hormonal signal in ERK-dependent processes such as steroid synthesis and, perhaps, cell proliferation. This review analyzes the participation of these tyrosine phosphates in the ACTH signaling pathway and the action of kinases and phosphatases in the regulation of mitochondrial dynamics and steroid production. In addition, the participation of kinases and phosphatases in the signal cascade triggered by different stimuli in other steroidogenic tissues is also compared to adrenocortical cell/ACTH and discussed.

Indexed as

Acsl4ERK1/2mitochondrial dynamicsMKP-1PKAPTPsSHP2

Identifiers

PMID27375556
PMCPMC4899475
OpenAlexW2409750388

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.