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TitleMolecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1.
Journal, issue, pagesEMBO J, Vol. 40, Issue 15, Page e107497, Year 2021
Publish dateAug 2, 2021
AuthorsYing-Ying Wang / Jianxiu Zhang / Xiao-Man Liu / Yulu Li / Jianhua Sui / Meng-Qiu Dong / Keqiong Ye / Li-Lin Du /
PubMed AbstractIn 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 ...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.
External linksEMBO J / PubMed:34169534 / PubMed Central
MethodsEM (single particle)
Resolution2.26 - 2.4 Å
Structure data

30650

7dd9

EMDB-30650, PDB-7dd9:
Cryo-EM structure of the Ams1 and Nbr1 complex
Method: EM (single particle) / Resolution: 2.4 Å

30652

7dde

EMDB-30652, PDB-7dde:
Cryo-EM structure of the Ape4 and Nbr1 complex
Method: EM (single particle) / Resolution: 2.26 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • Schizosaccharomyces pombe 972h- (yeast)
  • escherichia coli (strain k12) (bacteria)
  • schizosaccharomyces pombe (strain 972 / atcc 24843) (yeast)
KeywordsHYDROLASE / glycoside hydrolase / signaling protein / autophagy / aspartyl aminopeptidase

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