Evidence map›Paper›PMID 22590650›Full record

ArticlePloS one2012

Phosphorylation of nicastrin by SGK1 leads to its degradation through lysosomal and proteasomal pathways.

Jung-Soon Mo, Ji-Hye Yoon, Ji-Ae Hong, Mi-Yeon Kim, Eun-Jung Ann, Ji-Seon Ahn, Su-Man Kim, Hyeong-Jin Baek, Florian Lang, Eui-Ju Choi and 1 more

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In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
1.0field-weighted citation impact, top 25% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

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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

11 authors at 3 institutions in 2 countries.

Jung-Soon MoSchool of Biological Sciences and Technology, Hormone Research Center, Chonnam National University, Gwangju, Republic of Korea.
Ji-Hye Yoon
Ji-Ae Hong
Mi-Yeon Kim
Eun-Jung Ann
Ji-Seon Ahn
Su-Man Kim
Hyeong-Jin Baek
Florian Lang
Eui-Ju Choi
Hee-Sae Park
Chonnam National University · KRKorea University · KRUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The gamma-secretase complex is involved in the intramembranous proteolysis of a variety of substrates, including the amyloid precursor protein and the Notch receptor. Nicastrin (NCT) is an essential component of the gamma-secretase complex and functions as a receptor for gamma-secretase substrates. In this study, we determined that serum- and glucocorticoid-induced protein kinase 1 (SGK1) markedly reduced the protein stability of NCT. The SGK1 kinase activity was decisive for NCT degradation and endogenous SGK1 inhibited gamma-secretase activity. SGK1 downregulates NCT protein levels via proteasomal and lysosomal pathways. Furthermore, SGK1 directly bound to and phosphorylated NCT on Ser437, thereby promoting protein degradation. Collectively, our findings indicate that SGK1 is a gamma-secretase regulator presumably effective through phosphorylation and degradation of NCT.

Indexed as

ProteolysisAmyloid Precursor Protein SecretasesAnimalsHEK293 CellsHumansImmediate-Early ProteinsLysosomesMembrane GlycoproteinsMicePhosphorylationProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesProtein StabilitySerum-Glucocorticoid Regulated KinasesAmyloid Precursor Protein SecretasesImmediate-Early ProteinsMembrane Glycoproteinsnicastrin proteinProteasome Endopeptidase ComplexProtein Serine-Threonine KinasesSerum-Glucocorticoid Regulated Kinases

Identifiers

PMID22590650
PMCPMC3349648
OpenAlexW1984798065

What OpenQuestion holds

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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.