The TPLATE Adaptor Complex Drives Clathrin-Mediated Endocytosis in Plants

Gadeyne, Astrid; Sánchez‐Rodríguez, Clara; Vanneste, Steffen; Rubbo, Simone Di; Zauber, Henrik; Vanneste, Kevin; Leene, Jelle Van; Winne, Nancy De; Eeckhout, Dominique; Persiau, Geert; Slijke, Eveline Van De; Cannoot, Bernard; Vercruysse, Leen; Mayers, Jonathan R.; Adamowski, Maciek; Kania, Urszula; Ehrlich, Matthias; Schweighofer, Alois; Ketelaar, Tijs; Maere, Steven; Bednarek, Sebastian Y.; Friml, Jiřı́; Gevaert, Kris; Witters, Erwin; Russinova, Eugenia; Persson, Staffan; Jaeger, Geert De; Damme, Daniël Van

doi:10.1016/j.cell.2014.01.039

Cited by 247 publications

(475 citation statements)

References 98 publications

(110 reference statements)

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“…Subunits of the canonical adaptor protein complex AP2 can interact with the CesAs in vitro and in yeast [45], and mutations in AP2µ may cause an over-accumulation of CesAs at the plasma membrane. In addition, components of the newly identified TPLATE complex [46] may work with the AP2 complex to facilitate CesA internalization [47]. While these data support an internalization of the CesAs via CME, direct evidences, e.g.…”

mentioning

confidence: 62%

Cellulose and callose synthesis and organization in focus, what's new?

Schneider

Hanak

Persson

et al. 2016

Current Opinion in Plant Biology

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104

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Article available under the terms of the CC-BY-NC-ND licence (https://creativecommons.org/licenses/by-nc-nd/4.0/) eprints@whiterose.ac.uk https://eprints.whiterose.ac.uk/ Reuse Unless indicated otherwise, fulltext items are protected by copyright with all rights reserved. The copyright exception in section 29 of the Copyright, Designs and Patents Act 1988 allows the making of a single copy solely for the purpose of non-commercial research or private study within the limits of fair dealing. The publisher or other rights-holder may allow further reproduction and re-use of this version -refer to the White Rose Research Online record for this item. Where records identify the publisher as the copyright holder, users can verify any specific terms of use on the publisher's website. TakedownIf you consider content in White Rose Research Online to be in breach of UK law, please notify us by emailing eprints@whiterose.ac.uk including the URL of the record and the reason for the withdrawal request. Abstract Plant growth and development are supported by plastic but strong cell walls. These walls consist largely of polysaccharides that vary in content and structure. Most of the polysaccharides are produced in the Golgi apparatus and are then secreted to the apoplast and built into the growing walls. However, the two glucan polymers cellulose and callose are synthesized at the plasma membrane by cellulose or callose synthase complexes, respectively. Cellulose is the most common cell wall polymer in land plants and provides strength to the walls to support directed cell expansion. In contrast, callose is integral to specialized cell walls, such as the cell plate that separates dividing cells and growing pollen tube walls, and maintains important functions during abiotic and biotic stress responses. The last years have seen a dramatic increase in our understanding of how cellulose and callose are manufactured, and new factors that regulate the synthases have been identified. Much of this knowledge has been amassed via various microscopy-based techniques, including various confocal techniques and super-resolution imaging. Here, we summarize and synthesize recent findings in the fields of cellulose and callose synthesis in plant biology. Title

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mentioning

confidence: 62%

Cellulose and callose synthesis and organization in focus, what's new?

Schneider

Hanak

Persson

et al. 2016

Current Opinion in Plant Biology

Self Cite

104

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“…However, AP-2 and TPLATE are not unvariably linked, and there are also isolated subpopulations of TPLATE as well as AP-2 at the PM, which indicate that each may serve a unique, nonoverlapping role. It seems that ECA4 and CAP1 interact directly with TML, one of the core components of the TPLATE complex (Gadeyne et al, 2014) (Table 1); however, an interaction study in the absence of any remaining bridging factors, such as clathrin, has not been performed to date. It will be interesting to see whether CAP1 and ECA4 indeed are specific accessory proteins for the TPLATE complex or if they can also associate with AP-2 and with what affinity.…”

Section: Anths: a Large Group Involved In Endocytosismentioning

confidence: 99%

“…Evidence for a role of ECA4 and another related ANTH protein, CAP1 (AT4G32285), in CME comes from the recent identification of the TPLATE complex (Gadeyne et al, 2014), a tightly interacting multiprotein complex that includes ECA4 and CAP1. The eponymous TPLATE protein was originally identified as a factor in cytokinesis and pollen development with some similarity to other adaptor proteins (Van Damme et al, 2006).…”

Section: Anths: a Large Group Involved In Endocytosismentioning

confidence: 99%

Helping Hands for Budding Prospects: ENTH/ANTH/VHS Accessory Proteins in Endocytosis, Vacuolar Transport, and Secretion

Zouhar

Sauer

2014

The Plant Cell

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Coated vesicles provide a major mechanism for the transport of proteins through the endomembrane system of plants. Transport between the endoplasmic reticulum and the Golgi involves vesicles with COPI and COPII coats, whereas clathrin is the predominant coat in endocytosis and post-Golgi trafficking. Sorting of cargo, coat assembly, budding, and fission are all complex and tightly regulated processes that involve many proteins. The mechanisms and responsible factors are largely conserved in eukaryotes, and increasing organismal complexity tends to be associated with a greater numbers of individual family members. Among the key factors is the class of ENTH/ANTH/VHS domain-containing proteins, which link membrane subdomains, clathrin, and other adapter proteins involved in early steps of clathrin coated vesicle formation. More than 30 Arabidopsis thaliana proteins contain this domain, but their generally low sequence conservation has made functional classification difficult. Reports from the last two years have greatly expanded our knowledge of these proteins and suggest that ENTH/ANTH/VHS domain proteins are involved in various instances of clathrin-related endomembrane trafficking in plants. This review aims to summarize these new findings and discuss the broader context of clathrin-dependent plant vesicular transport.

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“…More recently, the activity of another, apparently plant-specific complex -the TPLATE adaptor complex -has been linked to early events in CME. TPLATE consists of eight core subunits and has been demonstrated to accumulate at distinct sites at the plasma membrane, preceding the recruitment of further components required for CCV formation (Gadeyne et al, 2014), thereby establishing TPLATE as a major adaptor complex that acts during early stages of CCV formation in plant cells (Fig. 4A).…”

Section: Clathrin and Adaptor Proteins: Key Mediators Of Protein Endomentioning

confidence: 99%

The dynamics of plant plasma membrane proteins: PINs and beyond

2014

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Plants are permanently situated in a fixed location and thus are well adapted to sense and respond to environmental stimuli and developmental cues. At the cellular level, several of these responses require delicate adjustments that affect the activity and steady-state levels of plasma membrane proteins. These adjustments involve both vesicular transport to the plasma membrane and protein internalization via endocytic sorting. A substantial part of our current knowledge of plant plasma membrane protein sorting is based on studies of PIN-FORMED (PIN) auxin transport proteins, which are found at distinct plasma membrane domains and have been implicated in directional efflux of the plant hormone auxin. Here, we discuss the mechanisms involved in establishing such polar protein distributions, focusing on PINs and other key plant plasma membrane proteins, and we highlight the pathways that allow for dynamic adjustments in protein distribution and turnover, which together constitute a versatile framework that underlies the remarkable capabilities of plants to adjust growth and development in their ever-changing environment.

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The TPLATE Adaptor Complex Drives Clathrin-Mediated Endocytosis in Plants

Cited by 247 publications

References 98 publications

Cellulose and callose synthesis and organization in focus, what's new?

Cellulose and callose synthesis and organization in focus, what's new?

Helping Hands for Budding Prospects: ENTH/ANTH/VHS Accessory Proteins in Endocytosis, Vacuolar Transport, and Secretion

The dynamics of plant plasma membrane proteins: PINs and beyond

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