TRAPP complexes in membrane traffic: convergence through a common Rab. (Q50336119)

5 March 2018

title

TRAPP complexes in membrane traffic: convergence through a common Rab. (English)

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5 March 2018

author name string

Jemima Barrowman

1

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5 March 2018

Deepali Bhandari

2

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5 March 2018

Karin Reinisch

3

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5 March 2018

Susan Ferro-Novick

4

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5 March 2018

publication date

1 November 2010

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5 March 2018

Nature Reviews Molecular Cell Biology

published in

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5 March 2018

volume

11

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5 March 2018

issue

11

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page(s)

759-763

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5 March 2018

https://scigraph.springernature.com/pub.10.1038/nrm2999

exact match

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cites work

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Bi-directional protein transport between the ER and Golgi

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Coats, tethers, Rabs, and SNAREs work together to mediate the intracellular destination of a transport vesicle

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Rabs and their effectors: achieving specificity in membrane traffic

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The GTP-binding protein Ypt1 is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants

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GTP-binding Ypt1 protein and Ca2+ function independently in a cell-free protein transport reaction

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Coupled ER to Golgi transport reconstituted with purified cytosolic proteins

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TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion

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SNAREs--engines for membrane fusion

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TRAPP I implicated in the specificity of tethering in ER-to-Golgi transport

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Identification of the novel TRAPP associated protein Tca17.

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TRAPPC2L is a novel, highly conserved TRAPP-interacting protein

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Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles

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TRAPPI tethers COPII vesicles by binding the coat subunit Sec23.

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Mutants in trs120 disrupt traffic from the early endosome to the late Golgi

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mTrs130 is a component of a mammalian TRAPPII complex, a Rab1 GEF that binds to COPI-coated vesicles

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Identification of the gene (SEDL) causing X-linked spondyloepiphyseal dysplasia tarda

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Identification of mutations in TRAPPC9, which encodes the NIK- and IKK-beta-binding protein, in nonsyndromic autosomal-recessive mental retardation

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A truncating mutation of TRAPPC9 is associated with autosomal-recessive intellectual disability and postnatal microcephaly

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Combination of linkage mapping and microarray-expression analysis identifies NF-kappaB signaling defect as a cause of autosomal-recessive mental retardation

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A mouse TRAPP-related protein is involved in pigmentation

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mBet3p is required for homotypic COPII vesicle tethering in mammalian cells

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Mammalian Bet3 functions as a cytosolic factor participating in transport from the ER to the Golgi apparatus

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Identification and characterization of five new subunits of TRAPP.

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SNARE status regulates tether recruitment and function in homotypic COPII vesicle fusion.

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Distinct isocomplexes of the TRAPP trafficking factor coexist inside human cells

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Control systems for membrane fusion in the ancestral eukaryote; evolution of tethering complexes and SM proteins

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Trs85 directs a Ypt1 GEF, TRAPPIII, to the phagophore to promote autophagy

31 March 2020

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The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes

31 March 2020

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The architecture of the multisubunit TRAPP I complex suggests a model for vesicle tethering

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TRAPPII subunits are required for the specificity switch of a Ypt-Rab GEF.

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TRAPPII is required for cleavage furrow ingression and localization of Rab11 in dividing male meiotic cells of Drosophila

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A Ypt32p exchange factor is a putative effector of Ypt1p

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The yeast GTP-binding YPT1 protein and a mammalian counterpart are associated with the secretion machinery

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Trs85 (Gsg1), a component of the TRAPP complexes, is required for the organization of the preautophagosomal structure during selective autophagy via the Cvt pathway

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Trs85 is required for macroautophagy, pexophagy and cytoplasm to vacuole targeting in Yarrowia lipolytica and Saccharomyces cerevisiae

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Network organization of the human autophagy system

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The conserved oligomeric Golgi complex is involved in double-membrane vesicle formation during autophagy

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Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins

31 March 2020

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Uso1 protein is a dimer with two globular heads and a long coiled-coil tail

31 March 2020

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Structure and mechanism in membrane trafficking

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Vesicle tethering complexes in membrane traffic

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1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20966969

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Molecular architecture of the TRAPPII complex and implications for vesicle tethering

1 reference

PubMed

https://pubmed.ncbi.nlm.nih.gov/20966969

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1038/NRM2999

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5 March 2018

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5 March 2018