SNARE proteins in membrane trafficking

Wang, Tuanlao; Li, Liangcheng; Hong, Wanjin

doi:10.1111/tra.12524

Cited by 144 publications

(130 citation statements)

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“…First, co-localization studies using organelle-associated molecular markers, and the FM4-64 marker demonstrated that NISP is associated with TGN/early endosomal vesicles. Second, we confirmed that NISP interacted with NSP in planta and showed that the complex formation occurred in vesicle-like structures, which resemble the NISP-associated TGN/endosomal vesicles, the typical subcellular localization of syntaxin-6-like proteins from Arabidopsis and humans [49]. Third, we showed that NISP exhibits a pro-viral function, and begomovirus infection required NISP-NSP interaction.…”

Section: Discussionsupporting

confidence: 64%

“…SYP61 has been shown to form functional SNARE complexes involved in the vacuolar-TGN recycling pathway and in exocytotic trafficking to the plasma membrane [43, 50]. The process of membrane fusion is the final step of vesicle transport, which is generally driven by a specific pairing of 1 v-SNAREs with the 3 or 3 cognate t-SNARE molecules into a trans-SNARE complex [49, 51]. The proteins from the SYP61 subclade contain the typical structural configuration of t-SNARES, including the N-terminal syntaxin-6 domain, followed by a C-terminal t-SNARE coiled-coil homology domain and a transmembrane segment at the C-terminus.…”

Section: Discussionmentioning

confidence: 99%

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A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

Gouveia-Mageste

Martins

Dal-Bianco

et al. 2020

Preprint

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2526 Due to limited free diffusion in the cytoplasm, viruses must use active transport mechanisms to 27 move intracellularly. Nevertheless, how the plant ssDNA begomovirus hijacks the host 28 intracytoplasmic transport machinery to move from the nucleus to the plasmodesma remains 29 enigmatic. Here, we identified nuclear shuttle protein (NSP)-interacting proteins by probing a 30 protein microarray and demonstrated that viral NSP, a facilitator of the nucleocytoplasmic 31 trafficking of viral (v)DNA, interacts with a new endosomal vesicle-localized plant-specific 32 syntaxin-6 protein, designated NISP in planta. We also showed that begomovirus infection 33 requires the NISP-NSP interaction; NISP displays a pro-viral function, but not the syntaxin-6 34 paralog AT2G18860 that failed to interact with NSP. Consistent with these findings, nisp-1 mutant 35 plants were less susceptible to begomovirus infection, a phenotype reversed by NISP 36 complementation, whereas overexpressing lines accumulated higher levels of viral DNA than 37 wild-type. Furthermore, NISP interacts with NIG, another pro-viral factor that accessorizes the 38 NSP-vDNA nucleocytoplasmic translocation. Additionally, the NISP-NIG interaction is enhanced 39 by NSP. We also showed that NISP associates with vDNA and might assemble a NISP-NIG-NSP-40 vDNA-complex. NISP may function as a docking site for recruiting NIG and NSP into trafficking 41 vesicles, providing a mechanism for the intracytoplasmic translocation of the NSP-vDNA complex 42 towards the cell periphery. 43 44 Author Summary 45 As viruses must use an active and directed intracellular movement, they hijack the intracellular 46 host transport system for their benefit. Therefore, the identification of interactions between host 3 47 proteins and begomovirus movement proteins should target the intracellular transport machinery.48 This work focused on the identification of these protein-protein interactions; it addressed the 49 molecular bases for the intracellular transport of begomoviruses. We used a protein microarray to 50 identify cellular partners for the movement protein (MP) and the viral nuclear shuttle protein 51 (NSP), which is a facilitator of the nucleocytoplasmic trafficking of viral (v)DNA. We identified 52 relevant protein-protein interaction (PPI) hubs connecting host and viral proteins. We revealed a 53 novel NSP-interacting protein, which functions in the intracytoplasmic transport of proteins and 54 DNA from begomoviruses and was designated NSP-interacting syntaxin domain-containing 55 protein (NISP). Our data suggest an intracellular route connecting the release of newly-synthesized 56 begomoviral DNA in the cytosol with the cell surface. Resolving viral DNA-host protein 57 complexes led to the identification of a novel class of components of the cell machinery and a 58 representative member, NISP, that functions as a susceptibility gene against begomoviruses. As 59 geminiviruses pose a severe threat to agriculture and food security, this recessive gene can now be 60 exploited ...

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Section: Discussionsupporting

confidence: 64%

Section: Discussionmentioning

confidence: 99%

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

Gouveia-Mageste

Martins

Dal-Bianco

et al. 2020

Preprint

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“…ORF3a detects 7 components of the SNARE complex (NAPA, STX4/6/7/12/16 and SNAP23) and uniquely interacts with 12 components of the 33A/39/41). The SNARE complex is involved in membrane trafficking and fusion79 ; the TRAPP complex in tethering vesicle transported from ER to Golgi80 ; and the HOPS and CORVET complexes in vacuolar, late endosomal and lysosomal membranes tethering and fusion81 . These data strongly suggest that ORF3a acts as a major regulator of endosomal and membrane trafficking by interfering with vesicular membrane attachment machineries.…”

mentioning

confidence: 99%

Global BioID-based SARS-CoV-2 proteins proximal interactome unveils novel ties between viral polypeptides and host factors involved in multiple COVID19-associated mechanisms

Laurent

Sofianatos

Komarova

et al. 2020

Preprint

128

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The worldwide SARS-CoV-2 outbreak poses a serious challenge to human societies and economies. SARS-CoV-2 proteins orchestrate complex pathogenic mechanisms that underlie COVID-19 disease. Thus, understanding how viral polypeptides rewire host protein networks enables better-founded therapeutic research. In complement to existing proteomic studies, in this study we define the first proximal interaction network of SARS-CoV-2 proteins, at the whole proteome level in human cells. Applying a proximity-dependent biotinylation (BioID)-based approach greatly expanded the current knowledge by detecting interactions within poorly soluble compartments, transient, and/or of weak affinity in living cells. Our BioID study was complemented by a stringent filtering and uncovered 2,128 unique cellular targets (1,717 not previously associated with SARS-CoV-1 or 2 proteins) connected to the N- and C-ter BioID-tagged 28 SARS-CoV-2 proteins by a total of 5,415 (5,236 new) proximal interactions. In order to facilitate data exploitation, an innovative interactive 3D web interface was developed to allow customized analysis and exploration of the landscape of interactions (accessible at http://www.sars-cov-2-interactome.org/). Interestingly, 342 membrane proteins including interferon and interleukin pathways factors, were associated with specific viral proteins. We uncovered ORF7a and ORF7b protein proximal partners that could be related to anosmia and ageusia symptoms. Moreover, comparing proximal interactomes in basal and infection-mimicking conditions (poly(I:C) treatment) allowed us to detect novel links with major antiviral response pathway components, such as ORF9b with MAVS and ISG20; N with PKR and TARB2; NSP2 with RIG-I and STAT1; NSP16 with PARP9-DTX3L. Altogether, our study provides an unprecedented comprehensive resource for understanding how SARS-CoV-2 proteins orchestrate host proteome remodeling and innate immune response evasion, which can inform development of targeted therapeutic strategies.

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“…In accordance with the known involvement of PLDs in vesicle fusions, we observed an increased abundance of alpha-soluble NSF attachment protein 2 (Alpha-SNAP2) in the pldα1-1 mutant. Alpha-SNAP proteins bind the SNARE complex [44] and are required for the vesicle pre-docking, an initial step of the membrane fusion reaction [45,46]. The precise function of alpha-SNAP2 is unknown so far, but it might require PLDα1.…”

Section: Vesicular Transportmentioning

confidence: 99%

Shot-Gun Proteomic Analysis on Roots of Arabidopsis <em>pldα1</em> Mutants Suggesting New Roles of PLDα1 in Mitochondrial Protein Import, Vesicular Trafficking and Glucosinolate Biosynthesis

Takáč¹,

Šamajová²,

Vadovič³

et al. 2018

Preprint

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Phospholipase Dα1 (PLDα1) belongs to phospholipases, a large phospholipid hydrolyzing protein family. PLDα1 has a substrate preference for phosphatidylcholine leading to enzymatic production of phosphatidic acid, a lipid second messenger with multiple cellular functions. PLDα1 itself is implicated in biotic and abiotic stress responses. We present here a shot-gun differential proteomic analysis on roots of two pldα1 mutants compared to the Col-0 wild type. Our data suggest new roles of PLDα1 in endomembrane transport, mitochondrial protein import and protein quality control and glucosinolate biosynthesis. Thus, we identified proteins involved in endocytosis, endoplasmic reticulum-Golgi transport and attachment sites of endoplasmic reticulum and plasma membrane (V-type proton ATPases, protein transport protein SEC13 homolog A, vesicle-associated protein 1-2, vacuolar protein sorting-associated protein 29, syntaxin-32, all upregulated in the mutants), mitochondrial import and electron transport chain (mitochondrial import inner membrane translocase subunits TIM23-2 and TIM13, mitochondrial NADH dehydrogenases, ATP synthases, cytochrome c oxidase subunit 6b-1, ADP,ATP carrier protein 2, downregulated in the mutants) and glucosinolate biosynthesis (3-isopropylmalate dehydrogenases 1, 2 and 3, methylthioalkylmalate synthase 1, cytochrome P450 83B1, Glutathione S-transferase F9, indole glucosinolate O-methyltransferase 1, adenylyl-sulfate kinase 1, all upregulated in mutants). Our results suggest broader biological roles of PLDα1 as anticipated so far.

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SNARE proteins in membrane trafficking

Cited by 144 publications

References 132 publications

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

Global BioID-based SARS-CoV-2 proteins proximal interactome unveils novel ties between viral polypeptides and host factors involved in multiple COVID19-associated mechanisms

Shot-Gun Proteomic Analysis on Roots of Arabidopsis <em>pldα1</em> Mutants Suggesting New Roles of PLDα1 in Mitochondrial Protein Import, Vesicular Trafficking and Glucosinolate Biosynthesis

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SNARE proteins in membrane trafficking

Cited by 144 publications

References 132 publications

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

A plant-specific syntaxin-6 protein contributes to the intracytoplasmic route for begomoviruses

Global BioID-based SARS-CoV-2 proteins proximal interactome unveils novel ties between viral polypeptides and host factors involved in multiple COVID19-associated mechanisms

Shot-Gun Proteomic Analysis on Roots of Arabidopsis <em>pld&alpha;1</em> Mutants Suggesting New Roles of PLD&alpha;1 in Mitochondrial Protein Import, Vesicular Trafficking and Glucosinolate Biosynthesis

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Shot-Gun Proteomic Analysis on Roots of Arabidopsis <em>pldα1</em> Mutants Suggesting New Roles of PLDα1 in Mitochondrial Protein Import, Vesicular Trafficking and Glucosinolate Biosynthesis