Molecular architecture of the TRAPPII complex and implications for vesicle tethering

Yip, Calvin K.; Berscheminski, Julia; Walz, Thomas

doi:10.1038/nsmb.1914

Cited by 72 publications

(126 citation statements)

References 44 publications

(75 reference statements)

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“…During macroautophagy, Pho8Δ60 is delivered from the cytosol to the vacuole where it is activated (19). Interestingly, Trs20 was also implicated in the interaction of TRAPPI with the TRAPPII-specific subunit Trs130 (20,21), so the D46Y mutation appears to compromise the formation of both the TRAPPII and TRAPPIII complexes.…”

Section: Significancementioning

confidence: 99%

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

Tan

Cai

Wang

et al. 2013

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

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144

180

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The transport protein particle (TRAPP) III complex, comprising the TRAPPI complex and additional subunit Trs85, is an autophagyspecific guanine nucleotide exchange factor for the Rab GTPase Ypt1 that is recruited to the phagophore assembly site when macroautophagy is induced. We present the single-particle electron microscopy structure of TRAPPIII, which reveals that the domeshaped Trs85 subunit associates primarily with the Trs20 subunit of TRAPPI. We further demonstrate that TRAPPIII binds the coat protein complex (COP) II coat subunit Sec23. The COPII coat facilitates the budding and targeting of ER-derived vesicles with their acceptor compartment. We provide evidence that COPII-coated vesicles and the ER-Golgi fusion machinery are needed for macroautophagy. Our results imply that TRAPPIII binds to COPII vesicles at the phagophore assembly site and that COPII vesicles may provide one of the membrane sources used in autophagosome formation. These events are conserved in yeast to mammals.M acroautophagy is a highly conserved catabolic process that uses a specialized membrane trafficking pathway to target proteins and organelles for degradation (1). Defects in this process have been linked to a variety of human diseases, including neurodegenerative diseases such as Parkinson's disease (2). Macroautophagy is induced by a variety of physiological stresses and begins with the expansion of a cup-shaped nucleating membrane called the phagophore, or isolation membrane. As the phagophore expands, it engulfs intracellular proteins and membranes that are marked for degradation. This expanding membrane eventually closes to become an autophagosome, a double-membrane structure that seals its contents from the cytosol and delivers it to the lysosome or vacuole for degradation. A central unanswered question in the autophagy field is the mechanism by which the phagophore forms and matures into an autophagosome. Although it was once thought that the phagophore assembles de novo, recent evidence suggests it forms from a preexisting compartment. Compartments on the secretory pathway, including the endoplasmatic reticulum (ER) and Golgi complex, have been invoked in phagophore assembly (3, 4).A collection of ATG (autophagy-related) genes, the products of which regulate autophagy, were identified in the yeast Saccharomyces cerevisiae (1). Many of the Atg proteins needed for macroautophagy in yeast are shared with the biosynthetic cytoplasm to vacuole targeting (Cvt) pathway that transports certain hydrolases into the vacuole. Both pathways require the sequestration of cargo within a double-membrane structure; however, only the macroautophagy pathway is conserved in higher eukaryotes (5). When autophagy is induced, ATG gene products assemble at the phagophore assembly site (PAS) in a hierarchical manner. The scaffold protein complex that organizes this site is the Atg17 complex (6, 7).Previous studies have shown that the transport protein particle (TRAPP) III complex, an autophagy-specic guanine nucleotide exchange factor (GEF) for ...

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Section: Significancementioning

confidence: 99%

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

Tan

Cai

Wang

et al. 2013

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

Self Cite

144

180

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“…19,[37][38][39] In the case of TRAPPI-mediated COPII tethering, it is believed that the initial tethering requires an interaction between TRAPPI and Sec23, 37 perhaps also an interaction between TRAPPI and Ypt1. 38 It is likely that TRAPPII in plant cells can also serve as RAB-A1c(Q72L).…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

“…17,19,20 Arabidopsis RAB-D2a, a homolog of yeast Ypt1 and animal Rab1, has been localized to a population of TGN. 31 So we tested if expression of either wild type or constitutively active RAB-D2a(Q67L) could rescue the growth of attrs130.…”

Section: ©2 0 1 1 L a N D E S B I O S C I E N C E D O N O T D I S Tmentioning

confidence: 99%

“…15 Here, we extend our functional analysis of TRAPPII and report that, TRAPPII in Arabidopsis is required for polar distribution of AUX1, an auxin influx carrier in protophloem cells and epidermal cells in Arabidopsis root tips. In yeast cells, TRAPPII has been implicated to serve as a GEF for the activation of both Ypt1 and Ypt31/32, [16][17][18][19] while in mammalian cells, TRAPPII acts as a GEF for Rab1 (homolog of yeast Ypt1). 20 We show here that TRAPPII in Arabidopsis is not functionally linked the Rab-D2a protein, a homolog of yeast Ypt1 and animal Rab1 proteins.…”

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Arabidopsis TRAPPII is functionally linked to Rab-A, but not Rab-D in polar protein trafficking intrans-Golgi network

Zheng

2011

Plant Signaling & Behavior

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“…To validate these subunit locations in light of our ability to visualize SAGA with a fully extended tail and to further expand this analysis, we applied a proven labeling approach that involves introducing C-terminal GFP tags to different SAGA subunits (33). We purified the corresponding GFP-tagged SAGA complexes and located the additional electron density introduced by GFP by negative stain two-dimensional EM method.…”

Section: Improved Procedures For Isolating Native S Cerevisiae Saga-mentioning

confidence: 99%

Conformational Flexibility and Subunit Arrangement of the Modular Yeast Spt-Ada-Gcn5 Acetyltransferase Complex

Setiaputra

Ross

et al. 2015

Journal of Biological Chemistry

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Background:The Saccharomyces cerevisiae Spt-Ada-Gcn5 acetyltransferase (SAGA) complex regulates transcription through chromatin modification and other mechanisms. Results: The overall structure of SAGA and the arrangement of all subunits within this complex were determined. Conclusion: SAGA is flexible and is composed of core modules that support peripheral catalytic modules. Significance: Understanding the structural mechanisms of SAGA multifunctionality improves the understanding of other chromatin-modifying complexes.

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Molecular architecture of the TRAPPII complex and implications for vesicle tethering

Cited by 72 publications

References 44 publications

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway

Arabidopsis TRAPPII is functionally linked to Rab-A, but not Rab-D in polar protein trafficking intrans-Golgi network

Conformational Flexibility and Subunit Arrangement of the Modular Yeast Spt-Ada-Gcn5 Acetyltransferase Complex

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