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

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 filaments. 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 cycle. 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.

journal_name

Nature

journal_title

Nature

authors

Tang F,Kauffman EJ,Novak JL,Nau JJ,Catlett NL,Weisman LS

doi

10.1038/nature01453

keywords:

subject

Has Abstract

pub_date

2003-03-06 00:00:00

pages

87-92

issue

6927

eissn

0028-0836

issn

1476-4687

pii

nature01453

journal_volume

422

pub_type

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