Reactome | TRAPPC complexes exchange GTP for GDP on RAB1

TRAPPC complexes exchange GTP for GDP on RAB1

Stable Identifier

R-HSA-8877475

Type

Reaction [transition]

Species

Homo sapiens

Compartment

transport vesicle membrane, cytosol

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

TRAPPC complexes exchange GTP for GDP on RAB1

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

RAB1 is involved in COPII-mediated anterograde traffic from the endoplasmic reticulum to the ERGIC (ER-Golgi intermediate compartment) and in early steps of the macroautophagy pathway (reviewed in Szul and Sztul, 2011; Sandoval and Simmen, 2012; Lord et al, 2013; Yang et al, 2016; Lamb et al, 2016; Kim et al, 2016; Ao et al, 2014). RAB1 nucleotide exchange is stimulated in these pathways by the GEF activity of the multisubunit TRAPPC complexes II and III, respectively (reviewed in Brunet and Sacher, 2014; Kim et al, 2016). Note that the separate existence of a TRAPPCI complex is not clearly established in human cells (Barrowman et al, 2010; Bassik et al, 2013; reviewed in Brunet and Sacher, 2014; Kim et al, 2016). TRAPPCII is recruited to ER-derived vesicles by virtue of an interaction between the TRAPPCII component TRAPPC3 and the COPII coat protein SEC23 (Wang et al, 2000; Cai et al, 2007; Cai et al, 2008; Yamasaki et al, 2009; Lord et al, 2011; reviewed in Brunet and Sacher, 2014; Ishida et al, 2016). Interaction of TRAAPPCII with RAB1:GDP promotes release of GDP, allowing GTP to bind, and precludes the interaction of RAB1 with GDI and CHM proteins. Protein protein interactions involving activated RAB1:GTP help dock the ER-derived vesicle on the cis-Golgi membrane (reviewed in Lord et al, 2013). In the macroautophagy pathway, RAB1 and the TRAPPCIII complex play a role in the formation of the pre-autophagosomal structure (PAS) and contribute to the localization of ATG9, a key nucleator of autophagosome formation (Lynch-Day et al, 2010; Winslow et al, 2010; Zoppino et al, 2010; Mochizuki et al, 2013; Lamb et al, 2016; reviewed in Kim et al, 2016).

Literature References

PubMed ID	Title	Journal	Year
19656848	mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles Yamasaki, A, Menon, S, Yu, S, Barrowman, J, Meerloo, T, Oorschot, V, Klumperman, J, Satoh, A, Ferro-Novick, S	Mol. Biol. Cell	2009
17287728	TRAPPI tethers COPII vesicles by binding the coat subunit Sec23 Cai, H, Yu, S, Menon, S, Cai, Y, Lazarova, D, Fu, C, Reinisch, K, Hay, JC, Ferro-Novick, S	Nature	2007
22013193	COPII and COPI traffic at the ER-Golgi interface Szul, T, Sztul, E	Physiology (Bethesda)	2011
23176493	Rab proteins of the endoplasmic reticulum: functions and interactors Ortiz Sandoval, C, Simmen, T	Biochem. Soc. Trans.	2012
23378591	The highly conserved COPII coat complex sorts cargo from the endoplasmic reticulum and targets it to the golgi Lord, C, Ferro-Novick, S, Miller, EA	Cold Spring Harb Perspect Biol	2013
25341920	Rab proteins and the compartmentalization of the endosomal system Wandinger-Ness, A, Zerial, M	Cold Spring Harb Perspect Biol	2014
11038176	TRAPP stimulates guanine nucleotide exchange on Ypt1p Wang, W, Sacher, M, Ferro-Novick, S	J. Cell Biol.	2000
24917561	In sickness and in health: the role of TRAPP and associated proteins in disease Brunet, S, Sacher, M	Traffic	2014
18585354	The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes Cai, Y, Chin, HF, Lazarova, D, Menon, S, Fu, C, Cai, H, Sclafani, A, Rodgers, DW, De La Cruz, EM, Ferro-Novick, S, Reinisch, KM	Cell	2008
21532587	Sequential interactions with Sec23 control the direction of vesicle traffic Lord, C, Bhandari, D, Menon, S, Ghassemian, M, Nycz, D, Hay, J, Ghosh, P, Ferro-Novick, S	Nature	2011
27246931	Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases Ishida, M, Oguchi, ME, Fukuda, M	Cell Struct. Funct.	2016
27041585	Rab1 in cell signaling, cancer and other diseases Yang, XZ, Li, XX, Zhang, YJ, Rodriguez-Rodriguez, L, Xiang, MQ, Wang, HY, Zheng, XF	Oncogene	2016