Evidence map›Paper›PMID 36717938›Full record

ArticleCell & bioscience2023

14-3-3 proteins regulate cullin 7-mediated Eag1 degradation.

Chang-Heng Hsieh, Chia-Cheng Chou, Ya-Ching Fang, Po-Hao Hsu, Yi-Hung Chiu, Chi-Sheng Yang, Guey-Mei Jow, Chih-Yung Tang, Chung-Jiuan Jeng

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell & bioscience, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 99% 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

1 citing paper in PubMed, 0 citations in OpenAlex.

  1. Article
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

9 authors at 4 institutions in 1 country.

Chang-Heng HsiehInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan.
Chia-Cheng ChouNational Laboratory Animal Center, National Applied Research Laboratories, Taipei, Taiwan.
Ya-Ching FangInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan.
Po-Hao HsuInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan.
Yi-Hung ChiuInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan.
Chi-Sheng YangInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan.
Guey-Mei JowSchool of Medicine, Fu-Jen Catholic University, New Taipei City, Taiwan.
Chih-Yung TangDepartment of Physiology, College of Medicine, National Taiwan University, Taipei, 100, Taiwan. tang@ntu.edu.tw.
Chung-Jiuan JengInstitute of Anatomy and Cell Biology, College of Medicine, National Yang Ming Chiao Tung University, Taipei, 112, Taiwan. cjjeng@nycu.edu.tw.ORCID http://orcid.org/0000-0001-6271-5704
National Yang Ming Chiao Tung University · TWFu Jen Catholic University · TWNational Institutes of Applied Research · TWNational Taiwan University · TW

Funding

National Science and Technology Council, Taiwan 108-2320-B-010-039-MY3National Science and Technology Council, Taiwan 111-2320-B-A49-014-MY3
6 · The paper itself

Abstract

backgroundMutations in the human gene encoding the neuron-specific Eag1 (K

resultsIn human cell line and native rat neurons, disruptions of endogenous 14-3-3 function with the peptide inhibitor difopein or specific RNA interference up-regulated Eag1 protein level in a transcription-independent manner. Difopein hindered Eag1 protein ubiquitination at the endoplasmic reticulum and the plasma membrane, effectively promoting the stability of both immature and mature Eag1 proteins. Suppression of endogenous 14-3-3 function also reduced excitotoxicity-associated Eag1 degradation in neurons. Difopein diminished Cul7-mediated Eag1 degradation, and Cul7 knock-down abolished the effect of difopein on Eag1. Inhibition of endogenous 14-3-3 function substantially perturbed the interaction of Eag1 with Cul7. Further structural analyses suggested that the intracellular Per-Arnt-Sim (PAS) domain and cyclic nucleotide-binding homology domain (CNBHD) of Eag1 are essential for the regulatory effect of 14-3-3 proteins. Significantly, suppression of endogenous 14-3-3 function reduced Cul7-mediated degradation of disease-associated Eag1 mutant proteins.

conclusionOverall these results highlight a chaperone-like role of endogenous 14-3-3 proteins in regulating Eag1 protein homeostasis, as well as a therapeutic potential of 14-3-3 modulators in correcting defective protein expression of disease-causing Eag1 mutants.

Indexed as

Lysosomal degradationPotassium channelProteasomal degradationProtein interactionProtein stabilityUbiquitin ligase

Identifiers

PMID36717938
PMCPMC9885684
OpenAlexW4318462523

What Socratic holds

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LicenceCC BY
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Registered trials

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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 Socratic graph.