Literature DB >> 18595704

Ypt11 functions in bud-directed transport of the Golgi by linking Myo2 to the coatomer subunit Ret2.

Seisuke Arai1, Yoichi Noda, Satoko Kainuma, Ikuo Wada, Koji Yoda.   

Abstract

A yeast class V myosin Myo2 transports the Golgi into the bud during its inheritance. However, the mechanism that links the Golgi to Myo2 is unknown. Here, we report that Ypt11, a Rab GTPase that reportedly interacts with Myo2, binds to Ret2, a subunit of the coatomer complex. When Ypt11 is overproduced, Ret2 and the Golgi markers, Och1 and Sft2, are accumulated in the growing bud and are lost in the mother cell. In a ret2 mutant that produces the Ret2 protein with reduced affinity to Ypt11, no such accumulation is observed upon overproduction of Ypt11. At a certain stage of budding, it is known that the late Golgi cisternae labeled with Sec7-GFP show polarized distribution in the bud. We find that this polarization of late Golgi cisternae is not observed in the ypt11Delta mutant. Indeed, analyses of Sec7-GFP dynamics with spatio-temporal image correlation spectroscopy (STICS) and fluorescence loss in photobleaching (FLIP) reveals that Ypt11 is required for the vectorial actin-dependent movement of the late Golgi from the mother cell toward the emerging bud. These results indicate that the Ypt11 and Ret2 are components of a Myo2 receptor complex that functions during the Golgi inheritance into the growing bud.

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Year:  2008        PMID: 18595704     DOI: 10.1016/j.cub.2008.06.028

Source DB:  PubMed          Journal:  Curr Biol        ISSN: 0960-9822            Impact factor:   10.834


  32 in total

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8.  Active segregation of yeast mitochondria by Myo2 is essential and mediated by Mmr1 and Ypt11.

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9.  Analysis of ER resident proteins in Saccharomyces cerevisiae: implementation of H/KDEL retrieval sequences.

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10.  Myosin-driven peroxisome partitioning in S. cerevisiae.

Authors:  Andrei Fagarasanu; Fred D Mast; Barbara Knoblach; Yui Jin; Matthew J Brunner; Michael R Logan; J N Mark Glover; Gary A Eitzen; John D Aitchison; Lois S Weisman; Richard A Rachubinski
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