Evidence map›Paper›PMID 35417087›Full record

ArticleEMBO reports2022

Phosphorylation by casein kinase 2 enhances the interaction between ER-phagy receptor TEX264 and ATG8 proteins.

Haruka Chino, Akinori Yamasaki, Koji L Ode, Hiroki R Ueda, Nobuo N Noda, Noboru Mizushima

Open access · greenAbstract read
In one paragraph

Article in EMBO reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

33 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
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  5. Core principles of autophagy initiation mechanisms.Nature structural & molecular biology · 2026
    Review
  6. ER membrane receptors engage core autophagy machinery to initiate ER-phagy.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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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 4 institutions in 1 country.

Haruka ChinoDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0003-3328-2211
Akinori YamasakiInstitute of Microbial Chemistry (BIKAKEN), Shinagawa-ku, Tokyo, Japan.ORCID 0000-0002-5820-5549
Koji L OdeDepartment of Systems Pharmacology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.
Hiroki R UedaDepartment of Systems Pharmacology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0001-8342-9176
Nobuo N NodaInstitute of Microbial Chemistry (BIKAKEN), Shinagawa-ku, Tokyo, Japan.ORCID 0000-0002-6940-8069
Noboru MizushimaDepartment of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, Japan.ORCID 0000-0002-6258-6444
The University of Tokyo · JPHokkaido University · JPMicrobial Chemistry Research Foundation · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Selective autophagy cargos are recruited to autophagosomes primarily by interacting with autophagosomal ATG8 family proteins via the LC3-interacting region (LIR). The upstream sequence of most LIRs contains negatively charged residues such as Asp, Glu, and phosphorylated Ser and Thr. However, the significance of LIR phosphorylation (compared with having acidic amino acids) and the structural basis of phosphorylated LIR-ATG8 binding are not entirely understood. Here, we show that the serine residues upstream of the core LIR of the endoplasmic reticulum (ER)-phagy receptor TEX264 are phosphorylated by casein kinase 2, which is critical for its interaction with ATG8s, autophagosomal localization, and ER-phagy. Structural analysis shows that phosphorylation of these serine residues increases binding affinity by producing multiple hydrogen bonds with ATG8s that cannot be mimicked by acidic residues. This binding mode is different from those of other ER-phagy receptors that utilize a downstream helix, which is absent from TEX264, to increase affinity. These results suggest that phosphorylation of the LIR is critically important for strong LIR-ATG8 interactions, even in the absence of auxiliary interactions.

Indexed as

Casein Kinase IIMicrotubule-Associated ProteinsAutophagyAutophagy-Related Protein 8 FamilyCarrier ProteinsEndoplasmic ReticulumPhosphorylationSerineAutophagy-Related Protein 8 FamilyCarrier ProteinsCasein Kinase IIMicrotubule-Associated ProteinsSerinecrystal structureER-phagyLC3-interacting regionphosphorylationselective autophagy

Identifiers

PMID35417087
PMCPMC9171416
OpenAlexW4223510002

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.