A5028750512- Advanced Electron Microscopy Techniques and Applications
- Electron and X-Ray Spectroscopy Techniques
- Photosynthetic Processes and Mechanisms
- Microtubule and mitosis dynamics
- Enzyme Structure and Function
- Advanced X-ray Imaging Techniques
- Anodic Oxide Films and Nanostructures
- Biopolymer Synthesis and Applications
- DNA Repair Mechanisms
- Ubiquitin and proteasome pathways
University of Hong Kong
2022-2024
ETH Zurich
2024
Hong Kong University of Science and Technology
2022-2024
Abstract γ-Tubulin ring complex (γ-TuRC) is the major microtubule-nucleating factor. After nucleation, microtubules can be released from γ-TuRC and stabilized by other proteins, such as CAMSAPs, but biochemical cross-talk between minus-end regulation pathways poorly understood. Here we reconstituted this process in vitro using purified components. We found that all CAMSAPs could bind to minus ends of γ-TuRC-attached microtubules. CAMSAP2 CAMSAP3, which decorate stabilize growing not tracking...
Microtubule nucleation is templated by the γ-tubulin ring complex (γ-TuRC), but its structure deviates from geometry of α-/β-tubulin in microtubule, explaining complex's poor nucleating activity. Several proteins may activate γ-TuRC, mechanisms underlying activation are not known. Here, we determined porcine γ-TuRC purified using CDK5RAP2's centrosomin motif 1 (CM1). We identified an unexpected conformation bound to multiple protein modules containing MZT2, GCP2, and CDK5RAP2, resulting a...
The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly that provides a template for microtubule nucleation. γ-TuRC recruited to microtubule-organizing centers (MTOCs) by the evolutionarily conserved attachment factor NEDD1. However, structural basis of NEDD1–γ-TuRC interaction not known. Here, we report cryo-EM structures NEDD1 bound human in absence or presence activating CDK5RAP2. We found C-terminus forms tetrameric α-helical contacts lumen cone and orients its...
Recent technological breakthroughs in single-particle cryo-electron microscopy (cryo-EM) enable rapid atomic structure determination of biological macromolecules. A major bottleneck the current single particle cryo-EM pipeline is preparation good quality frozen grids, which mostly a trial-and-error process. Among many issues, preferred orientation and sample damage by air-water interface (AWI) are common practical problems. Here we report method applying metallo-supramolecular branched...
Abstract Recent technological breakthroughs in single-particle cryo-electron microscopy (cryo-EM) enabled rapid atomic structure determination of biological macromolecules. A major bottleneck the current single particle cryo-EM pipeline is preparation good quality frozen grids, which mostly a trial-and-error process. Among many issues, preferred orientation and sample damage by air-water interface (AWI) are common practical problems. Here we reported method applying metallo-supramolecular...