TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabE
            <sup>RAB11</sup>

Pinar, Mario; Arst, Herbert N.; Pantazopoulou, Areti; Tagua, Víctor G.; Rı́os, Vivian de los; Rodríguez‐Salarichs, Javier; Díaz, J. Fernando; Peñalva, Miguel

doi:10.1073/pnas.1419168112

Cited by 61 publications

(110 citation statements)

References 52 publications

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“…First, we have shown that Ypt1 mutants used to implicate Ypt1 in late-Golgi transport (Sclafani et al, 2010) are instead defective in autophagy (Lipatova et al, 2013). Second, in vitro and in vivo studies support a role for TRAPP II at the late Golgi as a GEF for the S. cerevisiae Ypt31 (Morozova et al, 2006) and its Aspergillus nidulans ortholog RabE RAB11 (Pinar et al, 2015). Thus, our and others cumulative data reinforce the idea that TRAPP I-stimulated Ypt1 regulates transport at the early Golgi, whereas TRAPP II-activated Ypt31/32 regulate transport at the late Golgi.…”

Section: Discussionmentioning

confidence: 97%

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

et al. 2016

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Current models entail that transport through the Golgi — the main sorting compartment of the cell — occurs via cisternal progression/maturation, and that Ypt/Rab GTPases regulate this process. However, there is very limited evidence that cisternal progression is regulated, and no evidence for involvement of Ypt/Rab GTPases in such a regulation. Moreover, controversy about the placement of two of the founding members of the Ypt/Rab family, Ypt1 and Ypt31, to specific Golgi cisternae interferes with addressing this question in yeast, where cisternal progression has been extensively studied. Here, we establish the localization of Ypt1 and Ypt31 to opposite faces of the Golgi, early and late, respectively. Moreover, we show that they partially overlap on a transitional compartment. Finally, we determine that changes in Ypt1 and Ypt31 activity affect Golgi cisternal progression, early-to- transitional and transitional-to-late, respectively. These results show that Ypt/Rab GTPases regulate two separate steps of Golgi cisternal progression.

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Section: Discussionmentioning

confidence: 97%

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

et al. 2016

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“…TRAPP tethering complexes are known to act as guanine exchange factors (GEFs) and, thus, activate RAB GTPases (Jones et al, 2000;Wang et al, 2000;Pinar et al, 2015). Colocalization at the TGN and functional studies suggest that TRAPPII acts as a GEF for RABA1c, facilitating RABA1c-mediated trafficking of material from the TGN to the cell plate (Qi et al, 2011).…”

Section: Tgn and The Cell Plate: A Timely Connectionmentioning

confidence: 99%

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

2017

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“…Interestingly, the TRAPPII-binding N-terminal domain of Rabin8 is absent from Sec2 (yeast homolog of Rabin8). As TRAPPII mediates nucleotide exchange on the Ypt31 ortholog RabERAB11 53 , it could also function as a GEF for vertebrate Rab11. TRAPPC10 has a longin domain (LD) that forms a platform for small GTPases in Rab GEFs 54 , and a conserved, centrosome-targeting ASH domain 55 .…”

Section: Cilia Targeted Trafficking Complexesmentioning

confidence: 99%

Novel topography of the Rab11-effector interaction network within a ciliary membrane targeting complex

et al. 2015

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Small GTPases function as universal molecular switches due to the nucleotide dependent conformational changes of their switch regions that allow interacting proteins to discriminate between the active GTP-bound and the inactive GDP-bound states. Guanine nucleotide exchange factors (GEFs) recognize the inactive GDP-bound conformation whereas GTPase activating proteins (GAPs), and the GTPase effectors recognize the active GTP-bound state. Small GTPases are linked to each other through regulatory and effector proteins into functional networks that regulate intracellular membrane traffic through diverse mechanisms that include GEF and GAP cascades, GEF-effector interactions, common effectors and positive feedback loops linking interacting proteins. As more structural and functional information is becoming available, new types of interactions between regulatory proteins, and new mechanisms by which GTPases are networked to control membrane traffic are being revealed. This review will focus on the structure and function of the novel Rab11-FIP3-Rabin8 dual effector complex and its implications for the targeting of sensory receptors to primary cilia, dysfunction of which causes cilia defects underlying human diseases and disorders know as ciliopathies.

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TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabE ^RAB11

Cited by 61 publications

References 52 publications

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

Novel topography of the Rab11-effector interaction network within a ciliary membrane targeting complex

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TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabE RAB11

Cited by 61 publications

References 52 publications

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

Regulation of Golgi Cisternal Progression by Ypt/Rab GTPases

The Plant Trans-Golgi Network: Not Just a Matter of Distinction

Novel topography of the Rab11-effector interaction network within a ciliary membrane targeting complex

Contact Info

Product

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TRAPPII regulates exocytic Golgi exit by mediating nucleotide exchange on the Ypt31 ortholog RabE ^RAB11