Evidence map›Paper›PMID 31101736›Full record

ArticleLife science alliance2019

An N-terminal-truncated isoform of FAM134B (FAM134B-2) regulates starvation-induced hepatic selective ER-phagy.

Shohei Kohno, Yuji Shiozaki, Audrey L Keenan, Shinobu Miyazaki-Anzai, Makoto Miyazaki

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
4.3field-weighted citation impact, top 5% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.

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  7. FAM134B controls collagen I dynamics in hepatic stellate cell-driven fibrosis.American journal of physiology. Gastrointestinal and liver physiology · 2026
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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

5 authors at 1 institution in 1 country.

Shohei KohnoDivision of Renal Diseases and Hypertension, Department of Medicine, University of Colorado Denver, Aurora, CO, USA.
Yuji ShiozakiDivision of Renal Diseases and Hypertension, Department of Medicine, University of Colorado Denver, Aurora, CO, USA.
Audrey L KeenanDivision of Renal Diseases and Hypertension, Department of Medicine, University of Colorado Denver, Aurora, CO, USA.
Shinobu Miyazaki-AnzaiDivision of Renal Diseases and Hypertension, Department of Medicine, University of Colorado Denver, Aurora, CO, USA.
Makoto MiyazakiDivision of Renal Diseases and Hypertension, Department of Medicine, University of Colorado Denver, Aurora, CO, USA makoto.miyazaki@ucdenver.edu.ORCID 0000-0002-8704-8511
University of Colorado Denver · US

Funding

The role of MLKL in the regulation of vascular calcification in CKDR01HL132318 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI MIYAZAKI, MAKOTO · 2016 to 2025
$3.8M
Molecular Pathogenesis of Chronic Kidney Disease-Dependent Vascular CalcificationR01DK096030 · NIDDK · UNIVERSITY OF COLORADO DENVER · PI MIYAZAKI, MAKOTO · 2013 to 2017
$2.2M
The contributory role of microbial metabolite in the pathogenesis of CKD-dependent vascular calcificationR01HL133545 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI MIYAZAKI, MAKOTO · 2018 to 2021
$1.9M
The Role of Stearate in The Regulation of Vascular Calcification in Chronic Kidney DiseaseR01HL117062 · NHLBI · UNIVERSITY OF COLORADO DENVER · PI MIYAZAKI, MAKOTO · 2013 to 2016
$1.5M
NHLBI NIH HHS R01 HL117062NHLBI NIH HHS R01 HL132318NHLBI NIH HHS R01 HL133545NIDDK NIH HHS R01 DK096030
6 · The paper itself

Abstract

Autophagy is a conserved system that adapts to nutrient starvation, after which proteins and organelles are degraded to recycle amino acids in response to starvation. Recently, the ER was added to the list of targets of autophagic degradation. Autophagic degradation pathways of bulk ER and the specific proteins sorted through the ER are considered key mechanisms in maintaining ER homeostasis. Four ER-resident proteins (FAM134B, CCPG1, SEC62, and RTN3) have been identified as ER-resident cargo receptors, which contain LC3-interacting regions. In this study, we identified an N-terminal-truncated isoform of FAM134B (FAM134B-2) that contributes to starvation-induced ER-related autophagy. Hepatic FAM134B-2 but not full-length FAM134B (FAM134B-1) is expressed in a fed state. Starvation drastically induces FAM134B-2 but no other ER-resident cargo receptors through transcriptional activation by C/EBPβ. C/EBPβ overexpression increases FAM134B-2 recruitment into autophagosomes and lysosomal degradation. FAM134B-2 regulates lysosomal degradation of ER-retained secretory proteins such as ApoCIII. This study demonstrates that the C/EBPβ-FAM134B-2 axis regulates starvation-induced selective ER-phagy.

Indexed as

AutophagyAmino Acid SequenceAnimalsCCAAT-Enhancer-Binding Protein-betaEndoplasmic ReticulumGene Expression ProfilingGene Expression RegulationHumansIntracellular Signaling Peptides and ProteinsLiverLysosomesMembrane ProteinsMiceProtein IsoformsStarvationTranscription, GeneticCCAAT-Enhancer-Binding Protein-betaIntracellular Signaling Peptides and ProteinsMembrane ProteinsProtein IsoformsRETREG1 protein, human

Identifiers

PMID31101736
PMCPMC6526285
OpenAlexW2946728370

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.