Reactome | RIC1:RGP1 recruits RAB6:GDP to the TGN

RIC1:RGP1 recruits RAB6:GDP to the TGN

Stable Identifier

R-HSA-6811428

Type

Reaction [binding]

Species

Homo sapiens

Compartment

trans-Golgi network membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

RAB proteins are required for the RINT-1/ZW10 and COG-dependent organization of the Golgi ribbon stack, and for the trafficking of proteins through the Golgi. Indeed, cargo traffic through the Golgi depends on the maintenance of the Golgi stacks (Hirose et al, 2004; Arasaki et al, 2006; Sun et al, 2007; reviewed in Liu and Storrie, 2015). RAB6 is the primary RAB protein involved in intra-Golgi trafficking; it also has roles in COPI-independent retrograde traffic from the Golgi to the ER. RAB6A is a widely expressed isoform, while RAB6B is restricted to neuronal tissue (Darchen and Goud, 2000). RAB6 is localized to the trans-Golgi network (TGN), and a GTP-locked constitutively active form induces concentration of Golgi enzymes into the ER (Ferrano et al, 2104; Jiang and Storrie, 2005; Martinex et al, 1997; Micaroni et al, 2013; Storrie et al, 2012; Sun et al, 2007; Young et al, 2005). Inactive RAB6:GDP is recruited to the TGN through interaction with the RIC1:RGP1 complex, which also acts as a guanine nucleotide exchange factor (GEF) for RAB6 (Pusapati et al, 2012; Siniossoglou et al, 2000; Siniossoglou et al, 2001).

Literature References

PubMed ID	Title	Journal	Year
24794632	A two-tier Golgi-based control of organelle size underpins the functional plasticity of endothelial cells Ketteler, R, Burden, JJ, Martin-Martin, B, Knight, AE, Dyer, CE, Westmoreland, D, Kriston-Vizi, J, Ferraro, F, Cutler, DF, Freeman, J, Metcalf, DJ	Dev. Cell	2014
15029241	Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi Tagaya, M, Hatsuzawa, K, Takio, K, Tohyama, M, Tani, K, Hirose, H, Arasaki, K, Dohmae, N, Yamamoto, A, Nagahama, M	EMBO J.	2004
11689439	An effector of Ypt6p binds the SNARE Tlg1p and mediates selective fusion of vesicles with late Golgi membranes Pelham, HR, Siniossoglou, S	EMBO J.	2001
10990452	Ric1p and Rgp1p form a complex that catalyses nucleotide exchange on Ypt6p Pelham, HR, Siniossoglou, S, Peak-Chew, SY	EMBO J.	2000
22335553	Electron tomography reveals Rab6 is essential to the trafficking of trans-Golgi clathrin and COPI-coated vesicles and the maintenance of Golgi cisternal number Morgan, GP, Jones, N, Micaroni, M, Pan, TH, Kamykowski, JA, Marsh, BJ, Wilkins, N, Storrie, B	Traffic	2012
9050864	GTP-bound forms of rab6 induce the redistribution of Golgi proteins into the endoplasmic reticulum Martinez, O, Berger, EG, Pehau-Arnaudet, G, Salamero, J, Goud, B, Antony, C	Proc. Natl. Acad. Sci. U.S.A.	1997
15483056	Regulation of microtubule-dependent recycling at the trans-Golgi network by Rab6A and Rab6A' Young, J, Pepperkok, R, Stauber, T, Vernos, I, Nilsson, T, del Nery, E	Mol. Biol. Cell	2005
23091056	Ric1-Rgp1 complex is a guanine nucleotide exchange factor for the late Golgi Rab6A GTPase and an effector of the medial Golgi Rab33B GTPase Pfeffer, SR, Luchetti, G, Pusapati, GV	J. Biol. Chem.	2012
10865125	Multiple aspects of Rab protein action in the secretory pathway: focus on Rab3 and Rab6 Goud, B, Darchen, F	Biochimie	2000
16571679	RINT-1 regulates the localization and entry of ZW10 to the syntaxin 18 complex Taniguchi, M, Tagaya, M, Tani, K, Arasaki, K	Mol. Biol. Cell	2006
17451557	Multiple and stepwise interactions between coatomer and ADP-ribosylation factor-1 (Arf1)-GTP Wieland, F, Brugger, B, Zhao, L, Fröhlich, K, Anderl, F, Béthune, J, Hanke, S, Sun, Z	Traffic	2007
15758030	Cisternal rab proteins regulate Golgi apparatus redistribution in response to hypotonic stress Storrie, B, Jiang, S	Mol. Biol. Cell	2005
23437303	Rab6a/a' are important Golgi regulators of pro-inflammatory TNF secretion in macrophages Stanley, AC, Micaroni, M, Khromykh, T, Storrie, B, Marsh, BJ, Wong, CX, Lim, JP, Venturato, J, Stow, JL, Gleeson, PA	PLoS ONE	2013