Regulated degradation of a class V myosin receptor directs movement of the yeast vacuole

Fusheng Tang, Emily J. Kauffman, Jennifer L. Novak, Johnathan J. Nau, Natalie L. Catlett and Lois S. Weisman ()
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Fusheng Tang: University of Iowa
Emily J. Kauffman: University of Iowa
Jennifer L. Novak: University of Iowa
Johnathan J. Nau: University of Iowa
Natalie L. Catlett: University of Iowa
Lois S. Weisman: University of Iowa

Nature, 2003, vol. 422, issue 6927, 87-92

Abstract: Abstract Normal cellular function requires that organelles be positioned in specific locations. The direction in which molecular motors move organelles is based in part on the polarity of microtubules and actin filaments1,2,3. However, this alone does not determine the intracellular destination of organelles. For example, the yeast class V myosin, Myo2p, moves several organelles to distinct locations during the cell cycle4,5,6,7,8. Thus the movement of each type of Myo2p cargo must be regulated uniquely. Here we report a regulatory mechanism that specifically provides directionality to vacuole movement. The vacuole-specific Myo2p receptor, Vac17p, has a key function in this process. Vac17p binds simultaneously to Myo2p and to Vac8p, a vacuolar membrane protein. The transport complex, Myo2p–Vac17p–Vac8p, moves the vacuole to the bud, and is then disrupted through the degradation of Vac17p. The vacuole is ultimately deposited near the centre of the bud. Removal of a PEST sequence (a potential signal for rapid protein degradation) within Vac17p causes its stabilization and the subsequent ‘backward’ movement of vacuoles, which mis-targets them to the neck between the mother cell and the bud. Thus the regulated disruption of this transport complex places the vacuole in its proper location. This may be a general mechanism whereby organelles are deposited at their terminal destination.

Date: 2003
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DOI: 10.1038/nature01453

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