The crowding dynamics of the motor protein kinesin-II
Autor: | Seyda Acar, Peter Schall, Dmitry Denisov, Erwin J.G. Peterman, Daniël M. Miedema, Vandana S. Kushwaha |
---|---|
Přispěvatelé: | Faculty of Science, IoP (FNWI), Soft Matter (WZI, IoP, FNWI), Center of Experimental and Molecular Medicine, Amsterdam Gastroenterology Endocrinology Metabolism, Physics of Living Systems, LaserLaB - Molecular Biophysics |
Rok vydání: | 2020 |
Předmět: |
Nematoda
Kinesins Microtubules Biochemistry Fluorescence Microscopy 0302 clinical medicine Cytoskeleton Caenorhabditis elegans Physics Microscopy 0303 health sciences Multidisciplinary biology Molecular Motor Proteins Cilium Microtubule Motors Eukaryota Light Microscopy Animal Models Protein Transport Experimental Organism Systems Flagella Medicine Kinesin Cellular Structures and Organelles Research Article Imaging Techniques Science Motor Proteins Motility Image Analysis Myosins Research and Analysis Methods Motor protein 03 medical and health sciences SDG 17 - Partnerships for the Goals Model Organisms Molecular Motors Microtubule Intraflagellar transport Fluorescence Imaging Animals Cilia Caenorhabditis elegans Proteins 030304 developmental biology Total internal reflection fluorescence microscope Organisms Biology and Life Sciences Proteins Dyneins Biological Transport Cell Biology biology.organism_classification Invertebrates Cytoskeletal Proteins Kinetics Animal Studies Caenorhabditis Biophysics 030217 neurology & neurosurgery |
Zdroj: | PLoS ONE, Vol 15, Iss 2, p e0228930 (2020) PLoS ONE, 15(2):e0228930. Public Library of Science PLoS ONE Kushwaha, V S, Acar, S, Miedema, D M, Denisov, D V, Schall, P & Peterman, E J G 2020, ' The crowding dynamics of the motor protein kinesin-II ', PLoS ONE, vol. 15, no. 2, e0228930, pp. 1-16 . https://doi.org/10.1371/journal.pone.0228930 PLoS ONE, 15(2):e0228930, 1-16. Public Library of Science |
ISSN: | 1932-6203 |
DOI: | 10.1371/journal.pone.0228930 |
Popis: | Intraflagellar transport (IFT) in C. elegans chemosensory cilia is an example of functional coordination and cooperation of two motor proteins with distinct motility properties operating together in large groups to transport cargoes: a fast and processive homodimeric kinesin-2, OSM-3, and a slow and less processive heterotrimeric kinesin-2, kinesin-II. To study the mechanism of the collective dynamics of kinesin-II of C. elegans cilia in an in vitro system, we used Total Internal Reflection Fluorescence microscopy to image the motility of truncated, heterodimeric kinesin-II constructs at high motor densities. Using an analysis technique based on correlation of the fluorescence intensities, we extracted quantitative motor parameters, such as motor density, velocity and average run length, from the image. Our experiments and analyses show that kinesin-II motility parameters are far less affected by (self) crowding than OSM-3. Our observations are supported by numerical calculations based on the TASEP-LK model (Totally Asymmetric Simple Exclusion Process-Langmuir Kinetics). From a comparison of data and modelling of OSM-3 and kinesin-II, a general picture emerges of the collective dynamics of the kinesin motors driving IFT in C. elegans chemosensory cilia and the way the motors deal with crowding. |
Databáze: | OpenAIRE |
Externí odkaz: |