Trafficking of phosphatidylinositol 3-phosphate from the trans-Golgi network to the lumen of the central vacuole in plant cells

被引:212
作者
Kim, DH
Eu, YJ
Yoo, CM
Kim, YW
Pih, KT
Jin, JB
Kim, SJ
Stenmark, H
Hwang, I [1 ]
机构
[1] Gyeongsang Natl Univ, Dept Mol Biol, Chinju 660701, South Korea
[2] Pohang Univ Sci & Technol, Div Mol & Life Sci, Pohang 790784, South Korea
[3] Pohang Univ Sci & Technol, Ctr Plant Intracellular Trafficking, Pohang 790784, South Korea
[4] Norwegian Radium Hosp, Dept Biochem, N-0310 Oslo, Norway
关键词
D O I
10.1105/tpc.13.2.287
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Very limited information is available on the role of phosphatidytinositol 3-phosphate (P1[3]P) in vesicle trafficking in plant cells. To investigate the role of PI(3)P during the vesicle trafficking in plant cells, we exploited the Pt(3)P-specific binding property of the endosome binding domain (EBD) (amino acids 1257 to 1411) of human early endosome antigen 1, which is involved in endosome fusion. When expressed transiently in Arabidopsis protoplasts, a green fluorescent protein (GFP):EBD fusion protein exhibited PI(3)P-dependent localization to various compartments-such as the trans-Golgi network, the prevacuolar compartment, the tonoplasts, and the vesicles in the vacuolar lumen-that varied with time. The internalized GFP:EBD eventually disappeared from the lumen. Deletion experiments revealed that the P1(3)P-dependent localization required the Rab5 binding motif in addition to the zinc finger motif. Overexpression of GFP:EBD inhibited vacuolar trafficking of sporamin but not trafficking of Hf-ATPase to the plasma membrane. On the basis of these results, we propose that the trafficking of GFP:EBD reflects that of P1(3)P and that P1(3)P synthesized at the trans-Golgi network is transported to the vacuole through the prevacuolar compartment for degradation in plant cells.
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页码:287 / 301
页数:15
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