Role of Rab GTPases in Membrane Traffic

Author(s):  
Vesa M. Olkkonen ◽  
Harald Slenmark
Keyword(s):  
2003 ◽  
Vol 3 ◽  
pp. 870-880 ◽  
Author(s):  
Rytis Prekeris

Rab GTPases, proteins belonging to the Ras-like small GTP-binding protein superfamily, have emerged as master regulators of cellular membrane transport. Rab11 GTPase, a member of the Rab protein family, plays a role in regulating various cellular functions, including plasma membrane recycling, phagocytosis, and cytokinesis. Rab11 acts by forming mutually exclusive complexes with Rab11-family binding proteins, known as FIPs. Rab11-FIP complexes serve a role of �targeting complexes� by recruiting various membrane traffic factors to cellular membranes. Recent studies have identified several Rab11-FIP complex-binding proteins that regulate distinct membrane traffic pathways.


2021 ◽  
Author(s):  
Jing Wu ◽  
Jiaqi Gu ◽  
Li Shen ◽  
Xiaonan Jia ◽  
Yiqian Yin ◽  
...  

Influenza A virus (IAV) is a crucial cause of respiratory infections in humans worldwide. Therefore, studies should clarify adaptation mechanisms of IAV and critical factors of the viral pathogenesis in human hosts. GTPases of the Rab family are the largest branch of the Ras-like small GTPase superfamily, and they regulate almost every step during vesicle-mediated trafficking. Evidence has shown that Rab proteins participate in the lifecycle of IAV. In this mini-review, we outline the regulatory mechanisms of different Rab proteins in the lifecycle of IAV. Understanding the role of Rab proteins in IAV infections is important to develop broad-spectrum host-targeted antiviral strategies.


2018 ◽  
Vol 10 (2) ◽  
pp. 828-838 ◽  
Author(s):  
Xian Zhang ◽  
Timothy Y. Huang ◽  
Joel Yancey ◽  
Hong Luo ◽  
Yun-wu Zhang

1999 ◽  
Vol 112 (1) ◽  
pp. 21-33 ◽  
Author(s):  
D. Toomre ◽  
P. Keller ◽  
J. White ◽  
J.C. Olivo ◽  
K. Simons

The mechanisms and carriers responsible for exocytic protein trafficking between the trans-Golgi network (TGN) and the plasma membrane remain unclear. To investigate the dynamics of TGN-to-plasma membrane traffic and role of the cytoskeleton in these processes we transfected cells with a GFP-fusion protein, vesicular stomatitis virus G protein tagged with GFP (VSVG3-GFP). After using temperature shifts to block VSVG3-GFP in the endoplasmic reticulum and subsequently accumulate it in the TGN, dynamics of TGN-to-plasma membrane transport were visualized in real time by confocal and video microscopy. Both small vesicles (<250 nm) and larger vesicular-tubular structures (>1.5 microm long) are used as transport containers (TCs). These TCs rapidly moved out of the Golgi along curvilinear paths with average speeds of approximately 0.7 micrometer/second. Automatic computer tracking objectively determined the dynamics of different carriers. Fission and fusion of TCs were observed, suggesting that these late exocytic processes are highly interactive. To directly determine the role of microtubules in post-Golgi traffic, rhodamine-tubulin was microinjected and both labeled cargo and microtubules were simultaneously visualized in living cells. These studies demonstrated that exocytic cargo moves along microtubule tracks and reveals that carriers are capable of switching between tracks.


2003 ◽  
pp. 727-731
Author(s):  
Melissa M. McKay ◽  
Richard A. Kahn

2019 ◽  
Vol 59 ◽  
pp. 73-80 ◽  
Author(s):  
Luis Bonet-Ponce ◽  
Mark R Cookson

1997 ◽  
Vol 9 (4) ◽  
pp. 519-526 ◽  
Author(s):  
Michael G Roth ◽  
Paul C Sternweis

2015 ◽  
Vol 43 (3) ◽  
pp. 434-441 ◽  
Author(s):  
Jonathan S. Marchant ◽  
Sandip Patel

Two-pore channels (TPCs) are ancient members of the voltage-gated ion channel superfamily that localize to acidic organelles such as lysosomes. The TPC complex is the proposed target of the Ca2+-mobilizing messenger NAADP, which releases Ca2+ from these acidic Ca2+ stores. Whereas details of TPC activation and native ion permeation remain unclear, a consensus has emerged around their function in regulating endolysosomal trafficking. This role is supported by recent proteomic data showing that TPCs interact with proteins controlling membrane organization and dynamics, including Rab GTPases and components of the fusion apparatus. Regulation of TPCs by PtdIns(3,5)P2 and/or NAADP (nicotinic acid adenine dinucleotide phosphate) together with their functional and physical association with Rab proteins provides a mechanism for coupling phosphoinositide and trafficking protein cues to local ion fluxes. Therefore, TPCs work at the regulatory cross-roads of (patho)physiological cues to co-ordinate and potentially deregulate traffic flow through the endolysosomal network. This review focuses on the native role of TPCs in trafficking and their emerging contributions to endolysosomal trafficking dysfunction.


2008 ◽  
Vol 4 (11) ◽  
pp. e1000216 ◽  
Author(s):  
George A. Belov ◽  
Qian Feng ◽  
Krisztina Nikovics ◽  
Catherine L. Jackson ◽  
Ellie Ehrenfeld

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