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