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Kinetic properties and small-molecule inhibition of human myosin-6.

Published version
Peer-reviewed

Type

Article

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

Volume Title

586

Publisher

Wiley