C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking

Scrivens, P. James; Noueihed, Baraa; Shahrzad, Nassim; Hul, Sokunthear; Brunet, Stephanie; Sacher, Michael

doi:10.1091/mbc.e10-11-0873

Cited by 111 publications

(194 citation statements)

References 43 publications

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“…It was recently reported that depletion of the mammalian homolog of Trs85 (mTrs85) leads to a reduction in autophagosome formation (16), however, to date, only one TRAPP complex has been described in mammals (17,18). Since the roles of Ypt1 and its homolog Rab1 appear to be highly conserved from yeast to man (12), we asked if mTrs85 is a component of a TRAPP complex that is analogous to yeast TRAPPIII.…”

Section: Trs85 Is a Component Of A Transport Protein Particle III Commentioning

confidence: 99%

Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Wang

Menon

Yamasaki

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

113

141

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When macroautophagy, a catabolic process that rids the cells of unwanted proteins, is initiated, 30-60 nm Atg9 vesicles move from the Golgi to the preautophagosomal structure (PAS) to initiate autophagosome formation. The Rab GTPase Ypt1 and its mammalian homolog Rab1 regulate macroautophagy and two other trafficking events: endoplasmic reticulum-Golgi and intra-Golgi traffic. How a Rab, which localizes to three distinct cellular locations, achieves specificity is unknown. Here we show that transport protein particle III (TRAPPIII), a conserved autophagy-specific guanine nucleotide exchange factor for Ypt1/Rab1, is recruited to the PAS by Atg17. We also show that activated Ypt1 recruits the putative membrane curvature sensor Atg1 to the PAS, bringing it into proximity to its binding partner Atg17. Since Atg17 resides at the PAS, these events ensure that Atg1 will specifically localize to the PAS and not to the other compartments where Ypt1 resides. We propose that Ypt1 regulates Atg9 vesicle tethering by modulating the delivery of Atg1 to the PAS. These events appear to be conserved in higher cells.GEF | membrane tethering

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Section: Trs85 Is a Component Of A Transport Protein Particle III Commentioning

confidence: 99%

Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Wang

Menon

Yamasaki

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

113

141

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“…Unlike yeasts, no small-core TRAPP complex equivalent to the yeast TRAPP I complex appears to be present in mammals, suggesting that TRAPP complexes play differently roles in early secretory trafficking in yeasts and mammals (Scrivens et al, 2011). On the other hand, mammals contain two functionally different TRAPP complexes, named mTRAPP II and mTRAPP III, that are broadly similar to but clearly different in terms of their subunit composition from the yeast TRAPP II complex and TRAPP III complex, respectively.…”

Section: Trapp Complexesmentioning

confidence: 99%

Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases

Ishida

Oguchi

Fukuda

2016

Cell Struct. Funct.

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ABSTRACT. Rab small GTPases are highly conserved master regulators of membrane traffic in all eukaryotes. The same as the activation and inactivation of other small GTPases, the activation and inactivation of Rabs are tightly controlled by specific GEFs (guanine nucleotide exchange factors) and GAPs (GTPase-activating proteins), respectively. Although almost all Rab-GAPs reported thus far have a TBC (Tre-2/Bub2/Cdc16)/Rab-GAP domain in common, recent accumulating evidence has indicated the existence of a number of structurally unrelated types of Rab-GEFs, including DENN proteins, VPS9 proteins, Sec2 proteins, TRAPP complexes, heterodimer GEFs (Mon1-Ccz1, HPS1-HPS4 (BLOC-3 complex), Ric1-Rgp1 and Rab3GAP1/2), and other GEFs (e.g., REI-1 and RPGR). In this review article we provide an up-to-date overview of the structures and functions of all putative Rab-GEFs in mammals, with a special focus on their substrate Rabs, interacting proteins, associations with genetic diseases, and intracellular localizations.

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“…2 and Sacher et al, 2008). Fibroblasts from patients with TRAPPC11 or TRAPPC2 mutations (Bögershausen et al, 2013;Scrivens et al, 2009), and cultured cells depleted of TRAPPC11 (Scrivens et al, 2011;Wendler et al, 2010) display Golgi fragmentation and secretory protein retention. However, when these proteins are depleted in whole organisms their cell-specific roles are uncovered: patients with TRAPPC2 mutation develop spondyloepiphyseal dysplasia tarda (SEDT) distinguished by skeletal defects, short stature and microcephaly (Gedeon et al, 1999;Huson et al, 1993).…”

Section: Diseases Caused By Secretory Pathway Disruption In Zebrafishmentioning

confidence: 99%

In vivo cell biology in zebrafish – providing insights into vertebrate development and disease

Vacaru

Ünlü

Spitzner

et al. 2014

Journal of Cell Science

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Over the past decades, studies using zebrafish have significantly advanced our understanding of the cellular basis for development and human diseases. Zebrafish have rapidly developing transparent embryos that allow comprehensive imaging of embryogenesis combined with powerful genetic approaches. However, forward genetic screens in zebrafish have generated unanticipated findings that are mirrored by human genetic studies: disruption of genes implicated in basic cellular processes, such as protein secretion or cytoskeletal dynamics, causes discrete developmental or disease phenotypes. This is surprising because many processes that were assumed to be fundamental to the function and survival of all cell types appear instead to be regulated by cell-specific mechanisms. Such discoveries are facilitated by experiments in whole animals, where zebrafish provides an ideal model for visualization and manipulation of organelles and cellular processes in a live vertebrate. Here, we review well-characterized mutants and newly developed tools that underscore this notion. We focus on the secretory pathway and microtubule-based trafficking as illustrative examples of how studying cell biology in vivo using zebrafish has broadened our understanding of the role fundamental cellular processes play in embryogenesis and disease.

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C4orf41 and TTC-15 are mammalian TRAPP components with a role at an early stage in ER-to-Golgi trafficking

Abstract: Using two different TRAPP subunits as bait, we have identified four additional components of this human vesicle–tethering complex. Functional studies suggest that TRAPP functions early in ER-to-Golgi traffic, at or before the level of the ERGIC compartment.

Cited by 111 publications

References 43 publications

Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Ypt1 recruits the Atg1 kinase to the preautophagosomal structure

Multiple Types of Guanine Nucleotide Exchange Factors (GEFs) for Rab Small GTPases

In vivo cell biology in zebrafish – providing insights into vertebrate development and disease

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