AtTRAPPC11/ROG2: A Role for TRAPPs in Maintenance of the Plant <i>Trans</i>-Golgi Network/Early Endosome Organization and Function

Rosquete, Michel Ruiz; Worden, Natasha; Ren, Guosheng; Sinclair, Rosalie; Pfleger, Sina; Salemi, Michelle; Phinney, Brett S.; Domozych, David S.; Wilkop, Thomas; Drakakaki, Georgia

doi:10.1105/tpc.19.00110

Cited by 29 publications

(46 citation statements)

References 120 publications

(217 reference statements)

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“…The presence of the homologs of the four animal TRAPPIII-specific subunits (TRAPPC8, TRAPPC11, TRAPPC12, and TRAPPC13) in the AtTRS33 interactome but not the TRIPP interactome suggests the existence of both TRIPP-containing TRAPPII complex and an equivalent of TRAPPIII complex that excludes TRIPP. Indeed, in accordance with our results, a recent IP-MS using AtTRAPPC11 has confirmed the presence of a TRAPPIII complex in Arabidopsis (Rosquette et al, 2019). Our Y2H data indicates that TRIPP interacts with the two TRAPPII-specific subunits TRS120 and TRS130, further corroborating TRIPP association with the TRAPPII complex.…”

Section: Discussionsupporting

confidence: 93%

Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development

Garcia

Ravikumar

et al. 2019

Preprint

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2How the membrane trafficking system spatially organizes intracellular activities and 3 3 intercellular signaling networks is not well understood in plants. The Transport Protein 3 4Particle (TRAPP) complexes are known to play key roles in selective delivery of 3 5 membrane vesicles to various subcellular compartments in yeast and animals, but 3 6 remain to be fully characterized in plants. Here we interrogate the TRAPP complexes in 3 7 Arabidopsis using quantitative proteomic approaches. TRS33 is a component shared by 3 8 all TRAPP complexes in yeast and animals, and the Arabidopsis AtTRS33 is essential 3 9for the subcellular dynamics of other TRAPP components. Affinity purification of 4 0AtTRS33 followed by quantitative mass spectrometry identified fourteen interacting 4 1 proteins; these include not only thirteen homologs of all known TRAPP components in 4 2 yeast and mammals but also a novel protein we named TRAPP-interacting plant protein 4 3 (TRIPP), which is conserved in multi-cellular photosynthetic organisms. Proteomic and 4 4 molecular analyses showed that TRIPP specifically associates with the TRAPPII 4 5 complex in vivo and directly interacts with the TRAPPII-specific subunits but not the 4 6 subunits shared with TRAPPIII. TRIPP co-localizes with a subset of TRS33 4 7

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Section: Discussionsupporting

confidence: 93%

Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development

Garcia

Ravikumar

et al. 2019

Preprint

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“…SNARF-1 staining (Thermo Fisher, C1270) was performed using a protocol adapted from Rosquete et al, 2019. Briefly, 1 μL of 10 mM SNARF-1 was diluted in 1 mL of CoroNa Green incubation buffer, and sections are incubated in this solution in the dark for 3 h at room temperature before imaging (Rosquete et al, 2019). Suberin staining was performed using a protocol adapted from Naseer et al (Naseer et al, 2012).…”

Section: Fluorescent Staining and Microscopymentioning

confidence: 99%

Root vacuolar sequestration and suberization contribute to salinity tolerance in Pistacia spp. rootstocks

Zhang¹,

Quartararo²,

Betz³

et al. 2020

Preprint

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Pistachio (Pistacia spp.) is a tree nut crop with relatively high salinity tolerance. Currently, limited information exists on its rootstock's cellular responses to salinity stress, especially in its roots. In this study, we investigated salinity tolerance at cellular level, in two pistachio rootstocks, Pistacia integerrima (PGI) and a hybrid, P. atlantica x P. integerrima (UCB1). Root tip sections were categorized across a developmental gradient according to their xylem development, and their sodium content and suberin deposition were analyzed with fluorescence microscopy. Our data demonstrated a correlation between vacuolar sequestration of sodium ions (Na+) and salinity tolerance in the UCB1 genotype. In addition, UCB1 displayed higher basal levels of suberization in both the exodermis and endodermis that increased further after salinity stress. Notably, the root region immediately distal to the region of secondary xylem initiation showed the highest amount of vacuolar Na+ sequestration, indicating a developmental regulation of this process. Our cumulative data demonstrate that salinity tolerance in pistachio rootstock species is associated with both vacuolar Na+ sequestration and suberin deposition at apoplastic barriers, and both are correlated with a root developmental gradient. These cellular characteristics are phenotypes that can be screened during the selection for salinity tolerant woody plant species.

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“…Sanderfoot et al, 2001;Uemura et al, 2004). SYP61 predominantly localized to the TGN/EE, but recent studies reported that SYP61 also localized to the plasma membrane and the vacuolar membranes under specific conditions (Gendre et al, 2013;Hachez et al, 2014;Rosquete et al, 2019). In addition, SYP61 colocalized with the LE markers, an R-SNARE VAMP727 and a RAB GTPase ARA7/RABF2b, to form the hybrid compartment of the TGN/EE and the LE involved in the endocytosis of FLS2 receptor protein after flg22 treatment (Choi et al, 2013).…”

Section: Discussionmentioning

confidence: 97%

TGN/EE SNARE protein SYP61 is ubiquitinated and required for carbon/nitrogen-nutrient responses in Arabidopsis

Hasegawa

Reyes

Uemura

et al. 2020

Preprint

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Ubiquitination is a post-translational modification with reversible attachment of the small protein ubiquitin, which is involved in numerous cellular processes including membrane trafficking. For example, ubiquitination of cargo proteins is known to regulate their subcellular dynamics, and plays important roles in plant growth and stress adaptation. However, the regulatory mechanism of the trafficking machinery components remains elusive. Here, we report Arabidopsis trans-Golgi network/early endosome (TGN/EE) localized soluble N-ethylmaleimide sensitive factor attachment protein receptor (SNARE) protein SYP61 as a novel ubiquitination target of a membrane localized ubiquitin ligase ATL31. SYP61 is a key component of membrane trafficking in Arabidopsis. SYP61 was ubiquitinated with K63-linked chain by ATL31 in vitro and in plants. The knockdown mutants of SYP61 were hypersensitive to the disrupted carbon (C)/nitrogen (N)-nutrient stress, suggesting its critical role in plant homeostasis in response to nutrients. We also found the ubiquitination status of SYP61 is affected by C/N-nutrient availability. These results provided possibility that ubiquitination of SNARE protein has important role in plant physiology.

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AtTRAPPC11/ROG2: A Role for TRAPPs in Maintenance of the Plant Trans-Golgi Network/Early Endosome Organization and Function

Cited by 29 publications

References 120 publications

Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development

Proteomic studies of the Arabidopsis TRAPP complexes reveal conserved organization and a novel plant-specific component with a role in plant development

Root vacuolar sequestration and suberization contribute to salinity tolerance in Pistacia spp. rootstocks

TGN/EE SNARE protein SYP61 is ubiquitinated and required for carbon/nitrogen-nutrient responses in Arabidopsis

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