scholarly journals Interaction of the phospholipid flippase Drs2p with the F-box protein Rcy1p plays an important role in early endosome to trans-Golgi network vesicle transport in yeast

2013 ◽  
Vol 155 (1) ◽  
pp. 51-62 ◽  
Author(s):  
Hisatoshi Hanamatsu ◽  
Konomi Fujimura-Kamada ◽  
Takaharu Yamamoto ◽  
Nobumichi Furuta ◽  
Kazuma Tanaka
2009 ◽  
Vol 60 (5) ◽  
pp. 865-881 ◽  
Author(s):  
Sheung Kwan Lam ◽  
Yi Cai ◽  
Yu Chung Tse ◽  
Juan Wang ◽  
Angus Ho Yin Law ◽  
...  

2010 ◽  
Vol 22 (4) ◽  
pp. 1344-1357 ◽  
Author(s):  
Corrado Viotti ◽  
Julia Bubeck ◽  
York-Dieter Stierhof ◽  
Melanie Krebs ◽  
Markus Langhans ◽  
...  

2019 ◽  
Vol 31 (8) ◽  
pp. 1879-1898 ◽  
Author(s):  
Michel Ruiz Rosquete ◽  
Natasha Worden ◽  
Guangxi Ren ◽  
Rosalie M. Sinclair ◽  
Sina Pfleger ◽  
...  

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Makoto Nagano ◽  
Junko Y. Toshima ◽  
Daria Elisabeth Siekhaus ◽  
Jiro Toshima

AbstractEarly endosomes, also called sorting endosomes, are known to mature into late endosomes via the Rab5-mediated endolysosomal trafficking pathway. Thus, early endosome existence is thought to be maintained by the continual fusion of transport vesicles from the plasma membrane and the trans-Golgi network (TGN). Here we show instead that endocytosis is dispensable and post-Golgi vesicle transport is crucial for the formation of endosomes and the subsequent endolysosomal traffic regulated by yeast Rab5 Vps21p. Fittingly, all three proteins required for endosomal nucleotide exchange on Vps21p are first recruited to the TGN before transport to the endosome, namely the GEF Vps9p and the epsin-related adaptors Ent3/5p. The TGN recruitment of these components is distinctly controlled, with Vps9p appearing to require the Arf1p GTPase, and the Rab11s, Ypt31p/32p. These results provide a different view of endosome formation and identify the TGN as a critical location for regulating progress through the endolysosomal trafficking pathway.


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