Inroads into Internalization: Five Years of Endocytic Exploration

Reynolds, Gregory D.; Wang, Chao; Pan, Jian-Wei; Bednarek, Sebastian Y.

doi:10.1104/pp.17.01117

Cited by 65 publications

(65 citation statements)

References 128 publications

(202 reference statements)

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“…By contrast, TA23, which is also generally considered a specific inhibitor of CME in plant cells because it disrupts the association of the plasma membrane with different subunits of AP2 and the TPLATE subunit of the TPC complex (Lam et al ., ; van Damme et al ., ; Fan et al ., ; Wang et al ., ), only partially blocked the uptake of FM dye. This puzzling, partial inhibition of FM 4‐64FX recruitment in wood by TA23 could be the result of redundancy with AP2 of other adaptor proteins such as DRP2B, which were recently identified in plants (Fujimoto et al ., ; for a review see Fan et al ., ; Reynolds et al ., ), and/or unspecific selectivity of this inhibitor for FM dyes (Ortiz‐Zapater et al ., ; Dhonukshe et al ., ). Interestingly, TA23 induced the formation of distinct aggregates inside the VACs.…”

Section: Discussionmentioning

confidence: 99%

Endocytosis acts as transport pathway in wood

et al. 2019

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Summary In trees, dead and living cells of secondary xylem (wood) function collectively, rendering cell‐to‐cell communication challenging. Water and solutes are transported over long distances from the roots to the above‐ground organs via vessels, the main component of wood, and then radially over short distances to the neighboring cells. This enables proper functioning of trees and integrates whole‐plant activity. In this study, tracer loading, immunolocalization experiments and inhibitor assays were used to decipher the mechanisms enabling transport in wood of Acer pseudoplatanus (maple), Fraxinus excelsior (ash) and Populus tremula × tremuloides (poplar) trees. We show that tracer uptake from dead water‐conducting vessels, elements of the apoplasm, to living vessel‐associated cells (VACs) of the xylem parenchyma of the symplasm system proceeds via the endocytic pathway, including clathrin‐mediated and clathrin‐independent processes. These findings enhance our understanding of the transport pathways in complex wood tissue, providing experimental evidence of the involvement of VACs and endocytosis in radial uptake from vessels.

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Section: Discussionmentioning

confidence: 99%

Endocytosis acts as transport pathway in wood

et al. 2019

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“…YFP-AtTRAPPC11/ROG2 localized in the cytosol ( Figure 1A), as usually observed for TRAPP subunits (Sacher et al, 1998;Loh et al, 2005;Rybak et al, 2014), and colocalized with SYP61 at the TGN/EE (percentage of colocalization 5 62%, Pearson's correlation coefficient [PCC] 5 0.61; Figures 1A to 1C). Brefeldin A (BFA) is an inhibitor of post-Golgi trafficking and endosomal recycling that causes aggregation of post-Golgi compartments (Nebenführ et al, 2002;Geldner et al, 2003;Naramoto et al, 2010Naramoto et al, , 2014bSingh and Jurgens, 2017;Reynolds et al, 2018). SYP61 and AtTRAPPC11/ROG2 colocalize in BFA-induced bodies (percentage of colocalization 5 100%, PCC 5 0.75), implicating AtTRAPPC11/ROG2 in TGN/EE-associated trafficking ( Figures 1D to 1F).…”

Section: Attrappc11/rog2 Localizes To Syp61 Vesiclesmentioning

confidence: 99%

“…vesicle-associated YFP-RABD2A (Geldner et al, 2009;Drakakaki et al, 2012) under BFA treatment in attrappc11/rog2-2. BFA inhibits post-Golgi trafficking and endosomal recycling, thereby causing aggregation of Golgi, TGN, and endosomal material in BFA bodies (Nebenführ et al, 2002;Geldner et al, 2003;Naramoto et al, 2014b;Singh and Jurgens, 2017;Reynolds et al, 2018). While in the wild-type background CFP-SYP61 aggregated in large BFA bodies (>20 mm 3 ) at a ratio of 30 per 1000 mm 3 ( Figures 5A and 5C), formation of typical BFA bodies was impaired in attrappc11/rog2-2, where only punctae smaller than 20 mm 3 were detectable (E) to (G) Mislocalization of CFP-SYP61 to tonoplast in attrappc11/rog2-2 is reverted by complementation of the mutant with fluorescently tagged versions of AtTRAPPC11/ROG2 expressed under either the UBIQUITIN10 (UBQ10) (E) or the native (NAT) AtTRAPPC11/ROG2 promoter (F), as shown by the quantification of the percentage of cells displaying tonoplast SYP61 in the wild-type (WT), attrappc11/rog2-2, and complemented mutant backgrounds (G).…”

Section: Loss Of Attrappc11/rog2 Causes Bfa Resistance and Affects Enmentioning

confidence: 99%

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

et al. 2019

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The dynamic trans-Golgi network/early endosome (TGN/EE) facilitates cargo sorting and trafficking and plays a vital role in plant development and environmental response. Transport protein particles (TRAPPs) are multi-protein complexes acting as guanine nucleotide exchange factors and possibly as tethers, regulating intracellular trafficking. TRAPPs are essential in all eukaryotic cells and are implicated in a number of human diseases. It has been proposed that they also play crucial roles in plants; however, our current knowledge about the structure and function of plant TRAPPs is very limited. Here, we identified and characterized AtTRAPPC11/RESPONSE TO OLIGOGALACTURONIDE2 (AtTRAPPC11/ROG2), a TGN/EE-associated, evolutionarily conserved TRAPP protein in Arabidopsis (Arabidopsis thaliana). AtTRAPPC11/ROG2 regulates TGN integrity, as evidenced by altered TGN/EE association of several residents, including SYNTAXIN OF PLANTS61, and altered vesicle morphology in attrappc11/rog2 mutants. Furthermore, endocytic traffic and brefeldin A body formation are perturbed in attrappc11/rog2, suggesting a role for AtTRAPPC11/ROG2 in regulation of endosomal function. Proteomic analysis showed that AtTRAPPC11/ROG2 defines a hitherto uncharacterized TRAPPIII complex in plants. In addition, attrappc11/rog2 mutants are hypersensitive to salinity, indicating an undescribed role of TRAPPs in stress responses. Overall, our study illustrates the plasticity of the endomembrane system through TRAPP protein functions and opens new avenues to explore this dynamic network.

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“…Endocytosis of plasma membrane proteins is mediated mainly by clathrin, which is conserved among eukaryotes (reviewed in Reynolds et al, 2018;Robinson, 2015). In concert with several adaptor proteins, clathrin cagescomposed of clathrin trimers that form symmetrical three-legged structures called triskeliaare assembled at the plasma membrane allowing the internalisation of the proteins in clathrin-coated vesicles (CCVs).…”

Section: Introductionmentioning

confidence: 99%

Ubiquitin recognition in endocytic trafficking – with or without ESCRT-0

Mosesso

Nagel

Isono

2019

Journal of Cell Science

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The ability to sense and adapt to the constantly changing environment is important for all organisms. Cell surface receptors and transporters are key for the fast response to extracellular stimuli and, thus, their abundance on the plasma membrane has to be strictly controlled. Heteromeric endosomal sorting complexes required for transport (ESCRTs) are responsible for mediating the post-translational degradation of endocytosed plasma membrane proteins in eukaryotes and are essential both in animals and plants. ESCRTs bind and sort ubiquitylated cargoes for vacuolar degradation. Although many components that comprise the multi-subunit ESCRT-0, ESCRT-I, ESCRT-II and ESCRT-III complexes are conserved in eukaryotes, plant and animal ESCRTs have diverged during the course of evolution. Homologues of ESCRT-0, which recognises ubiquitylated cargo, have emerged in metazoan and fungi but are not found in plants. Instead, the Arabidopsis genome encodes plant-specific ubiquitin adaptors and a greater number of target of Myb protein 1 (TOM1) homologues than in mammals. In this Review, we summarise and discuss recent findings on ubiquitin-binding proteins in Arabidopsis that could have equivalent functions to ESCRT-0. We further hypothesise that SH3 domain-containing proteins might serve as membrane curvature-sensing endophilin and amphiphysin homologues during plant endocytosis.

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Inroads into Internalization: Five Years of Endocytic Exploration

Cited by 65 publications

References 128 publications

Endocytosis acts as transport pathway in wood

Endocytosis acts as transport pathway in wood

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

Ubiquitin recognition in endocytic trafficking – with or without ESCRT-0

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