Professional Education


  • Doctor of Philosophy, Institute of Biophysics, Chinese Academy of Sciences, Biochemistry and Molecular Biology (2021)
  • Bachelor of Engineering, Jilin University, Bioengineering (2015)
  • Exchange student, Peking University, Biology (2013)

Stanford Advisors


All Publications


  • Molecular and structural mechanisms of ZZ domain-mediated cargo selection by Nbr1 EMBO JOURNAL Wang, Y., Zhang, J., Liu, X., Li, Y., Sui, J., Dong, M., Ye, K., Du, L. 2021; 40 (15): e107497

    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.

    View details for DOI 10.15252/embj.2020107497

    View details for Web of Science ID 000665684600001

    View details for PubMedID 34169534

    View details for PubMedCentralID PMC8327946

  • Cryo-EM structure of fission yeast tetrameric alpha-mannosidase Ams1 FEBS OPEN BIO Zhang, J., Wang, Y., Du, L., Ye, K. 2020; 10 (11): 2437-2451

    Abstract

    Fungal α-mannosidase Ams1 and its mammalian homolog MAN2C1 hydrolyze terminal α-linked mannoses in free oligosaccharides released from misfolded glycoproteins or lipid-linked oligosaccharide donors. Ams1 is transported by selective autophagy into vacuoles. Here, we determine the tetrameric structure of Ams1 from the fission yeast Schizosaccharomyces pombe at 3.2 Å resolution by cryo-electron microscopy. Distinct from a low resolution structure of S. cerevisiae Ams1, S. pombe Ams1 has a prominent N-terminal tail that mediates tetramerization and an extra β-sheet domain. Ams1 shares a conserved active site with other enzymes in glycoside hydrolase family 38, to which Ams1 belongs, but contains extra N-terminal domains involved in tetramerization. The atomic structure of Ams1 reported here will aid understanding of its enzymatic activity and transport mechanism.

    View details for DOI 10.1002/2211-5463.12988

    View details for Web of Science ID 000579502400001

    View details for PubMedID 32981237

    View details for PubMedCentralID PMC7609781