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Rab6 Is Required for Multiple Apical Transport Pathways but Not the Basolateral Transport Pathway in Drosophila Photoreceptors

文献类型： 外文期刊

作者： Iwanami, Nozomi 1 ; Nakamura, Yuri 1 ; Satoh, Takunori 1 ; Liu, Ziguang 2 ; Satoh, Akiko K. 1 ;

作者机构： 1.Hiroshima Univ, Grad Sch Integral Arts & Sci, Div Life Sci, Higashihiroshima, Japan

2.Heilongjiang Acad Agr Sci, Inst Anim Husb, Harbin, Heilongjiang, Peoples R China

期刊名称：PLOS GENETICS （ 影响因子：5.917； 五年影响因子：6.284 ）

ISSN： 1553-7404

年卷期： 2016 年 12 卷 2 期

页码：

收录情况： SCI

摘要： Polarizedmembrane trafficking is essential for the construction and maintenance of multiple plasma membrane domains of cells. Highly polarized Drosophila photoreceptors are an excellent model for studying polarized transport. A single cross-section of Drosophila retina contains many photoreceptors with 3 clearly differentiated plasma membrane domains: a rhabdomere, stalk, and basolateralmembrane. Genome-wide high-throughput ethylmethanesulfonate screening followed by precise immunohistochemical analysis identified a mutant with a rare phenotype characterized by a loss of 2 apical transport pathways with normal basolateral transport. Rapid gene identification using whole-genome resequencing and single nucleotide polymorphism mapping identified a nonsense mutation of Rab6 responsible for the apical-specific transport deficiency. Detailed analysis of the trafficking of a major rhabdomere protein Rh1 using blue light-induced chromophore supply identified Rab6 as essential for Rh1 to exit the Golgi units. Rab6 is mostly distributed from the trans-Golgi network to a Golgi-associated Rab11-positive compartment that likely recycles endosomes or transport vesicles going to recycling endosomes. Furthermore, the Rab6 effector, Rich, is required for Rab6 recruitment in the trans-Golgi network. Moreover, a Rich null mutation phenocopies the Rab6 null mutant, indicating that Rich functions as a guanine nucleotide exchange factor for Rab6. The results collectively indicate that Rab6 and Rich are essential for the trans-Golgi network-recycling endosome transport of cargoes destined for 2 apical domains. However, basolateral cargos are sorted and exported from the trans-Golgi network in a Rab6-independent manner.

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