Key result
A 69-amino acid region of the yeast kinesin-related protein Smy1p tail physically interacts with the globular portion of the class V myosin Myo2p tail, which is necessary for Smy1p localization.
Population
Budding yeast
Design
Preclinical
Authors
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Does not inform clinical practice; leaves open whether Smy1p-Myo2p analogs coordinate vesicle transport in mammalian cardiomyocytes.
The study demonstrates a physical interaction between Smy1p and Myo2p in budding yeast, suggesting Smy1p enhances Myo2p function such as vesicle delivery or docking.
Beningo et al. (2000) studied this question. Smy1p and Myo2p interaction was evaluated on Physical interaction between Smy1p and Myo2p. A 69-amino acid region of the yeast kinesin-related protein Smy1p tail physically interacts with the globular portion of the class V myosin Myo2p tail, which is necessary for Smy1p localization.
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