Kinetic properties and small-molecule inhibition of human myosin-6.
Published version
Peer-reviewed
Repository URI
Repository DOI
Change log
Authors
Heissler, Sarah M
Selvadurai, Jayashankar
Bond, Lisa M
Fedorov, Roman
Kendrick-Jones, John
Abstract
Myosin-6 is an actin-based motor protein that moves its cargo towards the minus-end of actin filaments. Mutations in the gene encoding the myosin-6 heavy chain and changes in the cellular abundance of the protein have been linked to hypertrophic cardiomyopathy, neurodegenerative diseases, and cancer. Here, we present a detailed kinetic characterization of the human myosin-6 motor domain, describe the effect of 2,4,6-triiodophenol on the interaction of myosin-6 with F-actin and nucleotides, and show how addition of the drug reduces the number of myosin-6-dependent vesicle fusion events at the plasma membrane during constitutive secretion.
Description
Keywords
Actins, Amino-Acid N-Acetyltransferase, Animals, Gene Knockdown Techniques, HeLa Cells, Humans, In Vitro Techniques, Kinetics, Models, Biological, Models, Molecular, Molecular Motor Proteins, Mutagenesis, Site-Directed, Myosin Heavy Chains, Phenols, Protein Interaction Domains and Motifs, RNA, Small Interfering, Rabbits, Recombinant Fusion Proteins
Journal Title
FEBS Lett
Conference Name
Journal ISSN
0014-5793
1873-3468
1873-3468
Volume Title
586
Publisher
Wiley