The Coiled-Coil Protein VIG1 Is Essential for Tethering Vacuoles to Mitochondria during Vacuole Inheritance of Cyanidioschyzon merolae
The Coiled-Coil Protein VIG1 Is Essential for Tethering Vacuoles to Mitochondria during Vacuole Inheritance of Cyanidioschyzon merolae
复制标题
DOI:
10.1105/tpc.109.070227
复制
发表时间:
2010-03-01
期刊:
影响因子:
11.6
通讯作者:
Kuroiwa, Tsuneyoshi
中科院分区:
文献类型:
--
作者:
Fujiwara, Takayuki;Kuroiwa, Haruko;Kuroiwa, Tsuneyoshi
Vacuoles/lysosomes function in endocytosis and in storage and digestion of metabolites. These organelles are inherited by the daughter cells in eukaryotes. However, the mechanisms of this inheritance are poorly understood because the cells contain multiple vacuoles that behave randomly. The primitive red alga Cyanidioschyzon merolae has a minimum set of organelles. Here, we show that C. merolae contains about four vacuoles that are distributed equally between the daughter cells by binding to dividing mitochondria. Binding is mediated by VIG1, a 30-kD coiled-coil protein identified by microarray analyses and immunological assays. VIG1 appears on the surface of free vacuoles in the cytosol and then tethers the vacuoles to the mitochondria. The vacuoles are released from the mitochondrion in the daughter cells following VIG1 digestion. Suppression of VIG1 by antisense RNA disrupted the migration of vacuoles. Thus, VIG1 is essential for tethering vacuoles to mitochondria during vacuole inheritance in C. merolae.