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Nature. 1992 Mar 26;356(6367):358-61.

Suppression of a myosin defect by a kinesin-related gene.

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Department of Anatomy and Cell Biology, University of Michigan Medical School, Ann Arbor 48109.


Motor proteins in cells include myosin, which is actin-based, and kinesin, dynein and dynamin, which are microtubule-based. Several proteins have recently been identified that have amino-acid sequences with similarity to the motor domains of either myosin or kinesin, but are otherwise dissimilar. This has led to the suggestion that these may all be motor proteins, but that they are specialized for moving different cargos. Genetic analysis can address the question of the different functions of these new proteins. Studies of a temperature-sensitive mutation (myo2-66) in a gene of the myosin superfamily (MYO2) have implicated the Myo2 protein (Myo2p) in the process of polarized secretion in yeast (Saccharomyces cerevisiae). To understand more about the role of Myo2p, we have looked for 'multicopy suppressors' (heterologous genes that, when overexpressed, can correct the temperature sensitivity of the myo2-66 mutant). Here we report the identification of such a suppressor (SMY1) that (surprisingly) encodes a predicted polypeptide sharing sequence similarity with the motor portion of proteins in the kinesin superfamily.

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