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Kinetic properties and small‐molecule inhibition of human myosin‐6
Author(s) -
Heissler Sarah M.,
Selvadurai Jayashankar,
Bond Lisa M.,
Fedorov Roman,
Kendrick-Jones John,
Buss Folma,
Manstein Dietmar J.
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.07.014
Subject(s) - myosin , actin , myosin head , molecular motor , myosin light chain kinase , chemistry , microbiology and biotechnology , biophysics , biology , biochemistry
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.