Trafficking of Phosphatidylinositol 3-Phosphate from the trans-Golgi Network to the Lumen of the Central Vacuole in Plant Cells

2001 ◽  
Vol 13 (2) ◽  
pp. 287 ◽  
Author(s):  
Dae Heon Kim ◽  
Young-Jae Eu ◽  
Cheol Min Yoo ◽  
Yong-Woo Kim ◽  
Kyeong Tae Pih ◽  
...  
2001 ◽  
Vol 13 (2) ◽  
pp. 287-301 ◽  
Author(s):  
Dae Heon Kim ◽  
Young-Jae Eu ◽  
Cheol Min Yoo ◽  
Yong-Woo Kim ◽  
Kyeong Tae Pih ◽  
...  

2009 ◽  
Vol 60 (5) ◽  
pp. 865-881 ◽  
Author(s):  
Sheung Kwan Lam ◽  
Yi Cai ◽  
Yu Chung Tse ◽  
Juan Wang ◽  
Angus Ho Yin Law ◽  
...  

EMBO Reports ◽  
2001 ◽  
Vol 2 (4) ◽  
pp. 330-335 ◽  
Author(s):  
Akio Kihara ◽  
Yukiko Kabeya ◽  
Yoshinori Ohsumi ◽  
Tamotsu Yoshimori

2001 ◽  
Vol 13 (7) ◽  
pp. 1511-1526 ◽  
Author(s):  
Jing Bo Jin ◽  
Young A Kim ◽  
Soo Jin Kim ◽  
Sung Hoon Lee ◽  
Dae Heon Kim ◽  
...  

1997 ◽  
Vol 8 (4) ◽  
pp. 577-582 ◽  
Author(s):  
Y Nakajima ◽  
S R Pfeffer

Mannose 6-phosphate receptors carry newly synthesized lysosomal hydrolases from the trans-Golgi network to endosomes, then return to the trans-Golgi network for another round of enzyme delivery. Wortmannin, an inhibitor of phosphatidylinositol 3-kinase, interferes with the delivery of newly synthesized lysosomal enzymes to lysosomes. We used two independent assays of mannose 6-phosphate receptor trafficking to determine the precise step that is blocked by wortmannin. Using an assay that monitors resialylation of desialylated cell surface 300-kDa mannose 6-phosphate receptors, we found that receptor endocytosis and transport to the trans-Golgi network were not inhibited by 2 microM wortmannin. In addition, this concentration of drug had no effect on the transport of the mannose 6-phosphate receptor from late endosomes to the trans-Golgi network using a system that reconstitutes this transport process in cell extracts. Under the same conditions, wortmannin significantly inhibited the generation of mature cathepsin D. In addition, the structurally unrelated phosphatidylinositol 3-kinase inhibitor, LY294002, was also without effect when added to in vitro endosome-trans-Golgi network transport reactions. These experiments demonstrate that the interruption in lysosomal enzyme targeting is most likely due to a wortmannin-sensitive process required for the export of these receptors from the trans-Golgi network, consistent with the established role of phosphatidylinositol 3-kinase in the equivalent transport process in Saccharomyces cerevisiae.


2001 ◽  
Vol 13 (7) ◽  
pp. 1511 ◽  
Author(s):  
Jing Bo Jin ◽  
Young A. Kim ◽  
Soo Jin Kim ◽  
Sung Hoon Lee ◽  
Dae Heon Kim ◽  
...  

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