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

FEBS letters (2012-08-14)
Sarah M Heissler, Jayashankar Selvadurai, Lisa M Bond, Roman Fedorov, John Kendrick-Jones, Folma Buss, Dietmar J Manstein
RÉSUMÉ

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.

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Sigma-Aldrich
2,4,6-Triiodophenol, 97%