A5092907456- Microtubule and mitosis dynamics
- DNA Repair Mechanisms
- Photosynthetic Processes and Mechanisms
- Origins and Evolution of Life
- Photoreceptor and optogenetics research
- Protist diversity and phylogeny
- Ubiquitin and proteasome pathways
- Advanced Electron Microscopy Techniques and Applications
- Enzyme Structure and Function
- Neuroscience and Neuropharmacology Research
Institute of Molecular Biology and Biophysics
2025
ETH Zurich
2023-2025
Freie Universität Berlin
2023
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...
Summary Microtubule nucleation in cells is templated by the γ-tubulin ring complex (γ-TuRC), a 2.3 MDa multiprotein assembly concentrated at microtubule organizing centers (MTOCs). Current γ-TuRC structures exhibit an open conformation that deviates from geometry of α/β-tubulin microtubule, potentially explaining their low vitro microtubule-nucleating activity. Several proteins have been proposed to activate γ-TuRC, but mechanisms underlying activation are not known. Here, we isolated...
Directional ion transport across biological membranes plays a central role in many cellular processes. Elucidating the molecular determinants for vectorial is key to understanding functional mechanism of membrane-bound pumps. The extensive investigation light-driven proton pump bacteriorhodopsin from Halobacterium salinarum(HsBR) enabled detailed description outward transport. Although structure inward-directed pumping rhodopsins very similar HsBR, little known about their protonation...
The γ-tubulin ring complex (γ-TuRC) is an essential multiprotein assembly, in which γ-tubulin, GCP2-6, actin, MZT1 and MZT2 form asymmetric cone-shaped structure that provides a template for microtubule nucleation. γ-TuRC recruited to organizing centers (MTOCs), such as centrosomes pre-existing mitotic spindle microtubules, via the evolutionarily-conserved attachment factor NEDD1. NEDD1 contains N-terminal WD40 domain binds C-terminal associates with γ-TuRC. However, structural basis of...