Evidence map›Paper›PMID 34169534›Full record

ArticleThe EMBO journal2021

Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.

Ying-Ying Wang, Jianxiu Zhang, Xiao-Man Liu, Yulu Li, Jianhua Sui, Meng-Qiu Dong, Keqiong Ye, Li-Lin Du

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Review
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  6. Review
  7. Autophagy genes in biology and disease.Nature reviews. Genetics · 2023
    Review
  8. Article
  9. Antibody screening reveals antigenic proteins involved inFrontiers in cellular and infection microbiology · 2023
    Article
  10. NBR1: The archetypal selective autophagy receptor.The Journal of cell biology · 2022
    Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 1 country.

Ying-Ying WangCollege of Life Sciences, Beijing Normal University, Beijing, China.ORCID 0000-0003-1838-8034
Jianxiu ZhangKey Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0002-1864-7510
Xiao-Man LiuNational Institute of Biological Sciences, Beijing, China.
Yulu LiNational Institute of Biological Sciences, Beijing, China.
Jianhua SuiNational Institute of Biological Sciences, Beijing, China.
Meng-Qiu DongNational Institute of Biological Sciences, Beijing, China.
Keqiong YeKey Laboratory of RNA Biology, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.ORCID 0000-0001-6169-7049
Li-Lin DuNational Institute of Biological Sciences, Beijing, China.ORCID 0000-0002-1028-7397
National Institute of Biological Sciences, Beijing · CNChinese Academy of Sciences · CNBeijing Normal University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In selective autophagy, cargo selectivity is determined by autophagy receptors. However, it remains scarcely understood how autophagy receptors recognize specific protein cargos. In the fission yeast Schizosaccharomyces pombe, a selective autophagy pathway termed Nbr1-mediated vacuolar targeting (NVT) employs Nbr1, an autophagy receptor conserved across eukaryotes including humans, to target cytosolic hydrolases into the vacuole. Here, we identify two new NVT cargos, the mannosidase Ams1 and the aminopeptidase Ape4, that bind competitively to the first ZZ domain of Nbr1 (Nbr1-ZZ1). High-resolution cryo-EM analyses reveal how a single ZZ domain recognizes two distinct protein cargos. Nbr1-ZZ1 not only recognizes the N-termini of cargos via a conserved acidic pocket, similar to other characterized ZZ domains, but also engages additional parts of cargos in a cargo-specific manner. Our findings unveil a single-domain bispecific mechanism of autophagy cargo recognition, elucidate its underlying structural basis, and expand the understanding of ZZ domain-mediated protein-protein interactions.

Indexed as

Binding SitesCryoelectron MicroscopyIntracellular Signaling Peptides and ProteinsMutationProtein DomainsSchizosaccharomycesSchizosaccharomyces pombe ProteinsIntracellular Signaling Peptides and Proteinsnbr1 protein, S pombeSchizosaccharomyces pombe Proteinsautophagy receptorSchizosaccharomyces pombeselective autophagyZZ domain

Identifiers

PMID34169534
PMCPMC8327946
OpenAlexW3175581376

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.