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

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.

SUBMITTER: Heissler SM

PROVIDER: S-EPMC3527664 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature

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

Heissler Sarah M SM Selvadurai Jayashankar J Bond Lisa M LM Fedorov Roman R Kendrick-Jones John J Buss Folma F Manstein Dietmar J DJ

FEBS letters 20120731 19

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 s ...[more]

PMID: 22884421

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