Faculty Opinions recommendation of SMAP2, a novel ARF GTPase-activating protein, interacts with clathrin and clathrin assembly protein and functions on the AP-1-positive early endosome/trans-Golgi network.

2006 ◽  
Author(s):  
Matthew Seaman
Keyword(s):  
Early Endosome ◽  
Gtpase Activating Protein ◽  
Trans Golgi Network ◽  
Golgi Network

scholarly journals SMAP2, a Novel ARF GTPase-activating Protein, Interacts with Clathrin and Clathrin Assembly Protein and Functions on the AP-1–positive Early Endosome/Trans-Golgi Network

2006 ◽  
Vol 17 (6) ◽  
pp. 2592-2603 ◽  
Author(s):  
Waka Natsume ◽  
Kenji Tanabe ◽  
Shunsuke Kon ◽  
Naomi Yoshida ◽  
Toshio Watanabe ◽  
...  
Keyword(s):  
Brefeldin A ◽  
Adaptor Proteins ◽  
Early Endosome ◽  
Dependent Manner ◽  
Transferrin Receptors ◽  
Gtpase Activating Protein ◽  
Trans Golgi Network ◽  
Early Endosomes ◽  
Golgi Network

We recently reported that SMAP1, a GTPase-activating protein (GAP) for Arf6, directly interacts with clathrin and regulates the clathrin-dependent endocytosis of transferrin receptors from the plasma membrane. Here, we identified a SMAP1 homologue that we named SMAP2. Like SMAP1, SMAP2 exhibits GAP activity and interacts with clathrin heavy chain (CHC). Furthermore, we show that SMAP2 interacts with the clathrin assembly protein CALM. Unlike SMAP1, however, SMAP2 appears to be a regulator of Arf1 in vivo, because cells transfected with a GAP-negative SMAP2 mutant were resistant to brefeldin A. SMAP2 colocalized with the adaptor proteins for clathrin AP-1 and EpsinR on the early endosomes/trans-Golgi-network (TGN). Moreover, overexpression of SMAP2 delayed the accumulation of TGN38/46 molecule on the TGN. This suggests that SMAP2 functions in the retrograde, early endosome-to-TGN pathway in a clathrin- and AP-1–dependent manner. Thus, the SMAP gene family constitutes an important ArfGAP subfamily, with each SMAP member exerting both common and distinct functions in vesicle trafficking.

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
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