Ke Liang

ORCID: 0000-0003-4081-6859
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Research Areas
  • RNA Research and Splicing
  • Nuclear Structure and Function
  • Advanced Electron Microscopy Techniques and Applications
  • Photosynthetic Processes and Mechanisms
  • ATP Synthase and ATPases Research
  • Mitochondrial Function and Pathology
  • RNA modifications and cancer
  • RNA and protein synthesis mechanisms
  • Plant Molecular Biology Research
  • Antibiotic Resistance in Bacteria
  • Genetic Mapping and Diversity in Plants and Animals
  • Drug Transport and Resistance Mechanisms
  • Plant nutrient uptake and metabolism
  • Bacterial Genetics and Biotechnology

Sichuan Agricultural University
2025

Rice Research Institute
2025

Westlake University
2020-2024

Zhejiang University
2024

Institute for Advanced Study
2021-2022

INTRODUCTION The nuclear pore complex (NPC) resides on the envelope (NE) and mediates nucleocytoplasmic cargo transport. As one of largest cellular machineries, a vertebrate NPC consists cytoplasmic filaments, ring (CR), an inner ring, basket, luminal ring. Each has eight repeating subunits. Structure determination is prerequisite for understanding its functional mechanism. In past two decades, integrative modeling, which combines x-ray structures individual nucleoporins subcomplexes with...

10.1126/science.abl8280 article EN Science 2022-06-09

Abstract In Gram-negative bacteria, phospholipids are major components of the inner membrane and leaflet outer membrane, playing an essential role in forming unique dual-membrane barrier to exclude entry most antibiotics. Understanding mechanisms phospholipid translocation between represents one challenges surrounding bacterial homeostasis. The conserved MlaFEDB complex functions as ABC transporter drive periplasmic protein MlaC. However, mechanism remains elusive. Here we determined three...

10.1038/s41422-020-00404-6 article EN cc-by Cell Research 2020-09-03

Nuclear pore complex (NPC) shuttles cargo across the nuclear envelope. Here we present single-particle cryo-EM structure of ring (NR) subunit from Xenopus laevis NPC at an average resolution 5.6 Å. The NR comprises two 10-membered Y complexes, each with nucleoporin ELYS closely associating Nup160 and Nup37 long arm. Unlike cytoplasmic (CR) or inner (IR), contains only one molecule Nup205 Nup93. binds both arms complexes interacts stem neighboring subunit. Nup93 connects stems outer within...

10.1038/s41422-021-00610-w article EN cc-by Cell Research 2022-02-17

Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from Xenopus laevis NPC at an average resolution 4.2 Å. A homo-dimer Nup205 resides center IR subunit, flanked by two molecules Nup188. Four Nup93 each places extended helix into axial groove or Nup188, together constituting central scaffold. The channel nucleoporin hetero-trimer Nup62/58/54 is anchored on Six Nup155 interact with...

10.1038/s41422-022-00633-x article EN cc-by Cell Research 2022-03-18

SUMMARY Tillering contributes greatly to grain yield in rice ( Oryza sativa ). At present, many genes involved tillering regulation have been cloned and characterized. However, the identification of more novel is still necessary fully understand molecular mechanisms regulating tillering. In this study, we isolated a low ‐ dwarf 1 ltd1 ) mutant indica rice. Map‐based cloning MutMap analysis showed that candidate gene LTD1 LOC_Os01g19760 encodes putative FAM91A1 protein with an unknown...

10.1111/tpj.70119 article EN The Plant Journal 2025-03-31

Abstract The nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-EM structure of the cytoplasmic ring (CR) from Xenopus laevis NPC at 4.1-4.7 Å resolutions. an N-terminal domain Nup358 was resolved 3.0 Å, facilitating identification five molecules in each CR subunit. Aside unveiling assembly details two Y-shaped multicomponent complexes (Y complexes) subunit, improved resolutions reveal C-terminal fragment Nup160 to be organizing center...

10.1101/2022.02.14.480321 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2022-02-14

Abstract Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy (cryo-EM) structure of the inner ring (IR) subunit from Xenopus laevis NPC at an average resolution 4.4 Å. The symmetric IR comprises a cytoplasmic half and nuclear half. A homo-dimer Nup205 resides center subunit, flanked by two molecules Nup188. Four Nup93 each places extended helix into axial groove or Nup188, together constituting central scaffold. channel...

10.1101/2021.11.13.468242 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2021-11-13
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