Defective Quiescent Center/AtTRS85 Encoding a TRAPPIII-specific Subunit Required for the Trans-golgi Network/Early Endosome Integrity is Essential for the Proper Root Development in Arabidopsis

2020 ◽  
Vol 63 (1) ◽  
pp. 23-31
Author(s):  
Sang-Kee Song ◽  
Yo Han Kim ◽  
Jaehyo Song ◽  
Myeong Min Lee
Keyword(s):  
Root Development ◽  
Early Endosome ◽  
Quiescent Center ◽  
Trans Golgi Network ◽  
Golgi Network

BFA-induced compartments from the Golgi apparatus and trans-Golgi network/early endosome are distinct in plant cells

2009 ◽  
Vol 60 (5) ◽  
pp. 865-881 ◽  
Author(s):  
Sheung Kwan Lam ◽  
Yi Cai ◽  
Yu Chung Tse ◽  
Juan Wang ◽  
Angus Ho Yin Law ◽  
...  
Keyword(s):  
Golgi Apparatus ◽  
Plant Cells ◽  
Early Endosome ◽  
Trans Golgi Network ◽  
Golgi Network

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
Keyword(s):  
Early Endosome ◽  
Vesicle Transport ◽  
Trans Golgi Network ◽  
F Box Protein ◽  
Golgi Network ◽  
Phospholipid Flippase

scholarly journals Endocytic and Secretory Traffic in Arabidopsis Merge in the Trans-Golgi Network/Early Endosome, an Independent and Highly Dynamic Organelle

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

scholarly journals AtTRAPPC11/ROG2: A Role for TRAPPs in Maintenance of the Plant Trans-Golgi Network/Early Endosome Organization and Function

2019 ◽  
Vol 31 (8) ◽  
pp. 1879-1898 ◽  
Author(s):  
Michel Ruiz Rosquete ◽  
Natasha Worden ◽  
Guangxi Ren ◽  
Rosalie M. Sinclair ◽  
Sina Pfleger ◽  
...  
Keyword(s):  
Early Endosome ◽  
Trans Golgi Network ◽  
And Function ◽  
Golgi Network

scholarly journals Yeast Golgi-localized, γ-Ear–containing, ADP-Ribosylation Factor-binding Proteins Are but Adaptor Protein-1 Is Not Required for Cell-free Transport of Membrane Proteins from the Trans-Golgi Network to the Prevacuolar Compartment

2008 ◽  
Vol 19 (11) ◽  
pp. 4826-4836 ◽  
Author(s):  
Mohamed E. Abazeed ◽  
Robert S. Fuller
Keyword(s):  
Binding Proteins ◽  
Adaptor Protein ◽  
Early Endosome ◽  
Dominant Negative ◽  
Factor Binding ◽  
Trans Golgi Network ◽  
Direct Pathway ◽  
Prevacuolar Compartment ◽  
Golgi Network ◽  
Adp Ribosylation Factor

Golgi-localized, γ-Ear–containing, ADP-ribosylation factor-binding proteins (GGAs) and adaptor protein-1 (AP-1) mediate clathrin-dependent trafficking of transmembrane proteins between the trans-Golgi network (TGN) and endosomes. In yeast, the vacuolar sorting receptor Vps10p follows a direct pathway from the TGN to the late endosome/prevacuolar compartment (PVC), whereas, the processing protease Kex2p partitions between the direct pathway and an indirect pathway through the early endosome. To examine the roles of the Ggas and AP-1 in TGN–PVC transport, we used a cell-free assay that measures delivery to the PVC of either Kex2p or a chimeric protein (K-V), in which the Vps10p cytosolic tail replaces the Kex2p tail. Either antibody inhibition or dominant-negative Gga2p completely blocked K-V transport but only partially blocked Kex2p transport. Deletion of APL2, encoding the β subunit of AP-1, did not affect K-V transport but partially blocked Kex2p transport. Residual Kex2p transport seen with apl2Δ membranes was insensitive to dominant-negative Gga2p, suggesting that the apl2Δ mutation causes Kex2p to localize to a compartment that precludes Gga-dependent trafficking. These results suggest that yeast Ggas facilitate the specific and direct delivery of Vps10p and Kex2p from the TGN to the PVC and that AP-1 modulates Kex2p trafficking through a distinct pathway, presumably involving the early endosome.

Sign in / Sign up

Export Citation Format

Share Document