A5031298041- Microtubule and mitosis dynamics
- Photosynthetic Processes and Mechanisms
- Protist diversity and phylogeny
- Cellular transport and secretion
- Ubiquitin and proteasome pathways
- Micro and Nano Robotics
- Glycosylation and Glycoproteins Research
- Autophagy in Disease and Therapy
- Advanced Electron Microscopy Techniques and Applications
- Cardiomyopathy and Myosin Studies
- Cellular Mechanics and Interactions
- Biotin and Related Studies
- Supramolecular Chemistry and Complexes
- Protein Degradation and Inhibitors
- Glaucoma and retinal disorders
- Retinal Development and Disorders
- Histone Deacetylase Inhibitors Research
- Advanced Fluorescence Microscopy Techniques
- Photoreceptor and optogenetics research
- Global Peace and Security Dynamics
- Phytochemicals and Antioxidant Activities
- Advanced NMR Techniques and Applications
- Energy Load and Power Forecasting
- Advanced Glycation End Products research
- International Development and Aid
University of California, Berkeley
2014-2024
Berkeley College
2014-2024
University Hospital of Wales
2023
University of California, San Diego
2017-2022
QB3
2020-2022
Howard Hughes Medical Institute
2021-2022
Harvard University
2017-2020
Harvard Bioscience (United States)
2017-2020
Technological University Kyaukse
2018
Boston University
2017
In human cells, cytoplasmic dynein-1 is essential for long-distance transport of many cargos, including organelles, RNAs, proteins, and viruses, towards microtubule minus ends. To understand how a single motor achieves cargo specificity, we identified the dynein interactome by attaching promiscuous biotin ligase (‘BioID’) to seven components machinery, subunit cofactor dynactin. This method reported spatial information about large cytosolic dynein/dynactin complex in living cells. achieve...
The lissencephaly 1 gene, LIS1 , is mutated in patients with the neurodevelopmental disease lissencephaly. Lis1 protein conserved from fungi to mammals and a key regulator of cytoplasmic dynein-1, major minus-end-directed microtubule motor many eukaryotes. only dynein known bind directly dynein’s domain, by doing so alters mechanochemistry. required for formation fully active complexes, which also contain essential cofactors: dynactin an activating adaptor. Here, we report first...
The 26S proteasome recognizes thousands of appropriate protein substrates in eukaryotic cells through attached ubiquitin chains and uses its adenosine triphosphatase (ATPase) motor for mechanical unfolding translocation into a proteolytic chamber. Here, we used single-molecule Förster resonance energy transfer measurements to monitor the conformational dynamics proteasome, observe individual during their progression toward degradation, elucidate how these processes are regulated by chains....
Microtubules are dynamic polymers that used for intracellular transport and chromosome segregation during cell division. Their instability stems from the low energy of tubulin dimer interactions, which sets growing polymer close to its disassembly conditions. function in coordination with kinesin dynein molecular motors, use ATP hydrolysis produce mechanical work move on microtubules. This raises possibility forces produced by walking motors can break interactions trigger microtubule...
Summary The 26S proteasome is the major compartmental protease in eukaryotic cells, responsible for ATP-dependent turnover of obsolete, damaged, or misfolded proteins that are delivered degradation through attached ubiquitin modifications. In addition to targeting substrates proteasome, was recently shown promote initiation by directly modulating conformational switching yet underlying mechanisms unknown. Here, we used biochemical, mutational, and single-molecule FRET-based approaches show...
Abstract Cytoplasmic dynein-1 is a molecular motor that drives nearly all minus-end-directed microtubule-based transport in human cells, performing functions ranging from retrograde axonal to mitotic spindle assembly 1,2 . Activated dynein complexes consist of one or two dimers, the dynactin complex, and an “activating adaptor”, with maximal velocity seen dimers present (Fig. 1a) 3-6 Little known about how this massive ∼4MDa complex assembled. Using purified recombinant proteins, we...
Abstract The lissencephaly 1 gene, LIS1 , is mutated in patients with the neurodevelopmental disease lissencephaly. Lis1 protein conserved from fungi to mammals and a key regulator of cytoplasmic dynein-1, major minus-end-directed microtubule motor many eukaryotes. only dynein that binds directly dynein’s domain, by doing so alters mechanochemistry. required for formation fully active complexes, which also contain essential cofactors: dynactin an activating adaptor. Here, we report first...
ABSTRACT In human cells, cytoplasmic dynein-1 is essential for long-distance transport of many cargos, including organelles, RNAs, proteins, and viruses, towards microtubule minus ends. To understand how a single motor achieves cargo specificity, we identified the dynein interactome or “transportome” by attaching promiscuous biotin ligase (“BioID”) to seven components machinery, subunit cofactor dynactin. This method reported spatial information about large cytosolic dynein/dynactin complex...
Summary Regulation is central to the functional versatility of cytoplasmic dynein, a motor involved in intracellular transport, cell division, and neurodevelopment. Previous work established that Lis1, conserved ubiquitous regulator binds its domain induces tight microtubule-binding state dynein. The we present here—a combination biochemistry, single-molecule assays, cryo-electron microscopy vivo experiments—led surprising discovery Lis1 has two opposing modes regulating being capable...
Abstract Cytoplasmic dynein-1 (dynein) is an AAA+ motor that transports intracellular cargos towards the microtubule minus end. Lissencephaly-1 (Lis1) binds to ring and stalk of dynein’s domain promotes assembly active dynein complexes. Recent studies showed Lis1 slows motility when it remains bound dynein, but underlying mechanism remained unclear. Using single-molecule optical trapping assays, we investigated how binding affects force generation yeast in vitro. We does not slow by serving...
SUMMARY The 26S proteasome is the major ATP-dependent protease in eukaryotic cells, where it catalyzes degradation of thousands proteins for general homeostasis and control vital processes. It specifically recognizes appropriate substrates through attached ubiquitin chains uses its ATPase motor mechanical unfolding translocation into a proteolytic chamber. Here, we used single-molecule Förster Resonance Energy Transfer (FRET) measurements to provide unprecedented insights mechanisms...
In this paper, we developed method and software system to ensure reliability technical diagnostics for improving efficiency of high performance computing (HPC). This paper is devoted the development study analyze problems remote control increasing information management. Therefore can realize implement design management reliability.