Rice small GTPase Rab11 is required for intracellular trafficking from the trans-Golgi-network to the plasma membrane and/or prevacuolar compartments

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• 作者：Hee Rang Yun ; Yeong Gil Rim ; Jae Bok Heo
• 刊名：Journal of the Korean Society for Applied Biological Chemistry
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：59
• 期：2
• 页码：163-171
• 全文大小：2,149 KB
• 刊物主题：Applied Microbiology; Bioorganic Chemistry; Biological Techniques;
• 出版者：Springer Netherlands
• ISSN：2234-344X
• 卷排序：59

文摘

Members of the Rab family of small GTPases play important roles in membrane trafficking along the exocytic and endocytic pathways, their function being dependent on their localization. Here, we show the vital roles of the Oryza sativaRab11 (OsRab11) in intracellular trafficking using a dominant-negative mutant approach based on a protoplast-trafficking assay. GTP-binding and GTP hydrolysis assays revealed that OsRab11 is a small GTP-binding protein complementing △ypt32/ypt31. Green fluorescent protein (GFP)-OsRab11 has been localized to both the trans-Golgi-network (TGN) and the endosomes/prevacuolar compartments (PVC) in Arabidopsis protoplasts. The protoplast transformation with the dominant-negative mutant OsRab11(S28N) revealed that the trafficking of plasma membrane marker proteins [H+-ATPase-GFP and Ca2+-ATPase8-GFP (ACA8-GFP)] and central vacuole marker proteins [Arabidopsis aleurain-like protein (AALP-GFP) and sporamin (Spo-GFP)] was inhibited. Moreover, overexpression of Arabidopsis AtRha1 did not recover the trafficking inhibition of marker proteins from the central vacuole. These results strongly indicate that OsRab11 localizes to either the TGN or the PVC, and plays a significant role in the intracellular trafficking from the TGN to the PM and/or to the PVC in planta.KeywordsGolgiMembrane traffickingRab proteinPlasma membraneVacuole