Evidence map›Paper›PMID 38077022›Full record

ArticlebioRxiv : the preprint server for biology2023

The formation of ubiquitin rich condensates triggers recruitment of the ATG9A lipid transfer complex to initiate basal autophagy.

D G Broadbent, C M McEwan, T M Tsang, D M Poole, B C Naylor, J C Price, J C Schmidt, J L Andersen

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

8 authors at 2 institutions in 1 country.

D G BroadbentInstitute for Quantitative Health Sciences and Engineering, Michigan State University, East Lansing, MI, USA.
C M McEwanDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
T M TsangInstitute for Quantitative Health Sciences and Engineering, Michigan State University, East Lansing, MI, USA.
D M PooleDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
B C NaylorDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
J C PriceDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
J C SchmidtInstitute for Quantitative Health Sciences and Engineering, Michigan State University, East Lansing, MI, USA.
J L AndersenDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
Brigham Young University · USMichigan State University · US

Funding

Biochemical Consequences of Regiospecific Metabolic Bias in the BrainR01AG066874 · NIA · BRIGHAM YOUNG UNIVERSITY · PI PRICE, JOHN C. · 2020 to 2024
$3.0M
Single-molecule Analysis of the DNA Damage Response in Living CellsDP2GM142307 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SCHMIDT, JENS CHRISTOPHER · 2020 to 2020
$2.1M
The Regulation and Function of the Ubiquitin-Sensing Kinase TNK1R01GM147310 · NIGMS · UNIVERSITY OF UTAH · PI ANDERSEN, JOSHUA LYON · 2022 to 2024
$957k
NIA NIH HHS R01 AG066874NIGMS NIH HHS DP2 GM142307NIGMS NIH HHS R01 GM147310
6 · The paper itself

Abstract

Autophagy is an essential cellular recycling process that maintains protein and organelle homeostasis. ATG9A vesicle recruitment is a critical early step in autophagy to initiate autophagosome biogenesis. The mechanisms of ATG9A vesicle recruitment are best understood in the context of starvation-induced non-selective autophagy, whereas less is known about the signals driving ATG9A vesicle recruitment to autophagy initiation sites in the absence of nutrient stress. Here we demonstrate that loss of ATG9A or the lipid transfer protein ATG2 leads to the accumulation of phosphorylated p62 aggregates in the context of basal autophagy. Furthermore, we show that p62 degradation requires the lipid scramblase activity of ATG9A. Lastly, we present evidence that poly-ubiquitin is an essential signal that recruits ATG9A and mediates autophagy foci assembly in nutrient replete cells. Together, our data support a ubiquitin-driven model of ATG9A recruitment and autophagosome formation during basal autophagy.

Indexed as

ATG2AATG9Aautophagycondensateproteomicsubiquitin

Identifiers

PMID38077022
PMCPMC10705457
OpenAlexW4389154944

What OpenQuestion holds

Textmetadata
LicenceCC BY-ND
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.