Evidence map›Paper›PMID 25691244›Full record

ArticleThe EMBO journal2015

PI3P binding by Atg21 organises Atg8 lipidation.

Lisa Juris, Marco Montino, Peter Rube, Petra Schlotterhose, Michael Thumm, Roswitha Krick

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

56 citing papers in PubMed, 97 citations in OpenAlex.

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  6. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
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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

6 authors at 1 institution in 1 country.

Lisa JurisGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany.
Marco MontinoGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany.
Peter RubeGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany.
Petra SchlotterhoseGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany.
Michael ThummGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany mthumm@uni-goettingen.de.
Roswitha KrickGeorg-August-University, University Medicine, Institute of Cellular Biochemistry, Goettingen, Germany.
University of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagosome biogenesis requires two ubiquitin-like conjugation systems. One couples ubiquitin-like Atg8 to phosphatidylethanolamine, and the other couples ubiquitin-like Atg12 to Atg5. Atg12~Atg5 then forms a heterodimer with Atg16. Membrane recruitment of the Atg12~Atg5/Atg16 complex defines the Atg8 lipidation site. Lipidation requires a PI3P-containing precursor. How PI3P is sensed and used to coordinate the conjugation systems remained unclear. Here, we show that Atg21, a WD40 β-propeller, binds via PI3P to the preautophagosomal structure (PAS). Atg21 directly interacts with the coiled-coil domain of Atg16 and with Atg8. This latter interaction requires the conserved F5K6-motif in the N-terminal helical domain of Atg8, but not its AIM-binding site. Accordingly, the Atg8 AIM-binding site remains free to mediate interaction with its E2 enzyme Atg3. Atg21 thus defines PI3P-dependently the lipidation site by linking and organising the E3 ligase complex and Atg8 at the PAS.

Indexed as

Amino Acid MotifsAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEndopeptidasesInositol PhosphatesLipoylationMicrotubule-Associated ProteinsMultiprotein ComplexesProtein BindingProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesATG21 protein, S cerevisiaeATG3 protein, S cerevisiaeATG8 protein, S cerevisiaeAutophagy-Related Protein 8 FamilyAutophagy-Related ProteinsEndopeptidasesInositol PhosphatesMicrotubule-Associated ProteinsMultiprotein ComplexesSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesautophagyPROPPINubiquitin‐like conjugationWIPI

Identifiers

PMID25691244
PMCPMC4388602
OpenAlexW2118210524

What OpenQuestion holds

Textmetadata
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.