PI4P and Rab Inputs Collaborate in Myosin-V-Dependent Transport of Secretory Compartments in Yeast

被引:84
作者
Santiago-Tirado, Felipe H. [1 ,2 ]
Legesse-Miller, Aster [1 ]
Schott, Daniel [1 ]
Bretscher, Anthony [1 ,2 ]
机构
[1] Cornell Univ, Dept Mol Biol & Genet, Ithaca, NY 14853 USA
[2] Cornell Univ, Weill Inst Cell & Mol Biol, Ithaca, NY 14853 USA
关键词
SAC1 LIPID PHOSPHATASE; SACCHAROMYCES-CEREVISIAE; PHOSPHATIDYLINOSITOL; 4-PHOSPHATE; PLASMA-MEMBRANE; PHOSPHOINOSITIDE PHOSPHATASE; ARABIDOPSIS-THALIANA; ACTIN CYTOSKELETON; GENE ENCODES; MYO2P; GOLGI;
D O I
10.1016/j.devcel.2010.11.006
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cell polarity involves transport of specific membranes and macromolecules at the right time to the right place. In budding yeast, secretory vesicles are transported by the myosin-V Myo2p to sites of cell growth. We show that phosphatidylinositol 4-phosphate (PI4P) is present in late secretory compartments and is critical for their association with, and transport by, Myo2p. Further, the trans-Golgi network Rab Ypt31/32p and secretory vesicle Rab Sec4p each bind directly, but distinctly, to Myo2p, and these interactions are also required for secretory compartment transport. Enhancing the interaction of Myo2p with PI4P bypasses the requirement for interaction with Ypt31/32p and Sec4p. Together with additional genetic data, the results indicate that Rab proteins and PI4P collaborate in the association of secretory compartments with Myo2p. Thus, we show that a coincidence detection mechanism coordinates inputs from PI4P and the appropriate Rab for secretory compartment transport.
引用
收藏
页码:47 / 59
页数:13
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