scholarly journals Visualization of Procollagen IV Reveals ER-to-Golgi Transport by ERGIC-independent Carriers

2020 ◽  
Vol 45 (2) ◽  
pp. 107-119
Author(s):  
Yuto Matsui ◽  
Yukihiro Hirata ◽  
Ikuo Wada ◽  
Nobuko Hosokawa
Keyword(s):  
Golgi Transport

scholarly journals Rab11-mediated post-Golgi transport of the sialyltransferase ST3GAL4 suggests a new mechanism for regulating glycosylation.

2021 ◽  
pp. 100354
Author(s):  
Masato Kitano ◽  
Yasuhiko Kizuka ◽  
Tomoaki Sobajima ◽  
Miyako Nakano ◽  
Kazuki Nakajima ◽  
...  
Keyword(s):  
Golgi Transport

scholarly journals The Hsp90 Chaperone Complex Regulates GDI-dependent Rab Recycling

2006 ◽  
Vol 17 (8) ◽  
pp. 3494-3507 ◽  
Author(s):  
Christine Y. Chen ◽  
William E. Balch
Keyword(s):  
Rab Gtpase ◽  
Rab Gtpases ◽  
Coding System ◽  
Golgi Transport ◽  
Guanine Nucleotide Dissociation Inhibitor ◽  
Hsp90 Activity ◽  
Hsp90 Chaperone ◽  
Chaperone Complex ◽  
Hsp 90 ◽  
Synaptic Vesicle Fusion

Rab GTPase regulated hubs provide a framework for an integrated coding system, the membrome network, that controls the dynamics of the specialized exocytic and endocytic membrane architectures found in eukaryotic cells. Herein, we report that Rab recycling in the early exocytic pathways involves the heat-shock protein (Hsp)90 chaperone system. We find that Hsp90 forms a complex with guanine nucleotide dissociation inhibitor (GDI) to direct recycling of the client substrate Rab1 required for endoplasmic reticulum (ER)-to-Golgi transport. ER-to-Golgi traffic is inhibited by the Hsp90-specific inhibitors geldanamycin (GA), 17-(dimethylaminoethylamino)-17-demethoxygeldanamycin (17-DMAG), and radicicol. Hsp90 activity is required to form a functional GDI complex to retrieve Rab1 from the membrane. Moreover, we find that Hsp90 is essential for Rab1-dependent Golgi assembly. The observation that the highly divergent Rab GTPases Rab1 involved in ER-to-Golgi transport and Rab3A involved in synaptic vesicle fusion require Hsp90 for retrieval from membranes lead us to now propose that the Hsp90 chaperone system may function as a general regulator for Rab GTPase recycling in exocytic and endocytic trafficking pathways involved in cell signaling and proliferation.

scholarly journals Intra-Golgi transport: A way to a new paradigm?

2005 ◽  
Vol 1744 (3) ◽  
pp. 340-350 ◽  
Author(s):  
Alexander A. Mironov ◽  
Galina V. Beznoussenko ◽  
Roman S. Polishchuk ◽  
Alvar Trucco
Keyword(s):  
New Paradigm ◽  
Golgi Transport
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