Plant endosomal trafficking pathways

Reyes, Francisca; Buono, Rafael Andrade; Otegui, Marisa S.

doi:10.1016/j.pbi.2011.07.009

Cited by 139 publications

(126 citation statements)

References 63 publications

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“…We found that (Leitner et al, 2012;Martins et al, 2015). Collectively, in some cases, the recognition of PYL4 by the endosomal trafficking pathway might depend on a direct interaction with the sorting complexes; in other cases, this recognition might rely on post-translational modifications, such as ubiquitination or phosphorylation (Reyes et al, 2011).…”

Section: Discussionmentioning

confidence: 71%

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Lou

Tian

et al. 2016

Molecular Plant

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This is a PDF file of an unedited manuscript that has been accepted for publication. As a service to our customers we are providing this early version of the manuscript. The manuscript will undergo copyediting, typesetting, and review of the resulting proof before it is published in its final form. Please note that during the production process errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.All studies published in MOLECULAR PLANT are embargoed until 3PM ET of the day they are published as corrected proofs on-line. Studies cannot be publicized as accepted manuscripts or uncorrected proofs. proteasome system, which strengthens our understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling. proteasome system, further strengthen our understanding of both the turnover of ABA receptors and ESCRTs in plant hormone signaling. M A N U S C R I P T A C C E P T E D

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Section: Discussionmentioning

confidence: 71%

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Lou

Tian

et al. 2016

Molecular Plant

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“…Receptors and transporters returning from the PM are either recycled or targeted to the vacuole for degradation. Delivery and recycling sorting pathways overlap in the trans-Golgi network (TGN)/early endosome (EE), an intermediate compartment for both exocytosis and endocytosis (Reyes et al, 2011). In plant systems, the endoplasmic reticulum and PM provide membrane continuity between cells through the connections made by plasmodesmata (PD), cytoplasmic channels that regulate traffic in the symplasm (Maule et al, 2011).…”

mentioning

confidence: 99%

Hitching a Ride on Vesicles: Cauliflower Mosaic Virus Movement Protein Trafficking in the Endomembrane System

2014

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The transport of a viral genome from cell to cell is enabled by movement proteins (MPs) targeting the cell periphery to mediate the gating of plasmodesmata. Given their essential role in the development of viral infection, understanding the regulation of MPs is of great importance. Here, we show that cauliflower mosaic virus (CaMV) MP contains three tyrosine-based sorting signals that interact with an Arabidopsis (Arabidopsis thaliana) mA-adaptin subunit. Fluorophore-tagged MP is incorporated into vesicles labeled with the endocytic tracer N-(3-triethylammoniumpropyl)-4-(6-(4-(diethylamino)phenyl)hexatrienyl)pyridinium dibromide. The presence of at least one of the three endocytosis motifs is essential for internalization of the protein from the plasma membrane to early endosomes, for tubule formation, and for CaMV infection. In addition, we show that MP colocalizes in vesicles with the Rab GTPase AtRAB-F2b, which is resident in prevacuolar late endosomal compartments that deliver proteins to the vacuole for degradation. Altogether, these results demonstrate that CaMV MP traffics in the endocytic pathway and that virus viability depends on functional host endomembranes.

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“…Recent findings underline a role for the spatiotemporal control of PM protein degradation in plant development (Reyes et al 2011). Specifically, decisions concerning polarized, directional growth have been intimately linked to the controlled decay of receptor and/or hormone transport proteins.…”

Section: Christian Luschnigmentioning

confidence: 99%

“…Recent studies revealed that endocytosis is important for a variety of plant functions, including establishment of cell polarity, auxin transport, pathogen defense and cytokinesis, which all require tight regulation of localization and/or activity of PM proteins (Murphy et al 2005;Geldner and Jurgens 2006;Ebine and Ueda 2009;Chen et al 2011;Reyes et al 2011). In plants, this first acceptor compartment is the TGN, which is the compartment where the endocytic and the secretory pathway meet and sorting and recycling takes place (Dettmer et al 2006;Lam et al 2007;Viotti et al 2010).…”

Section: Endocytic Sorting Pathways In Plantsmentioning

confidence: 99%

“…Specifically control of localization and steady-state protein levels play an essential role in the regulation of PM protein function (Titapiwatanakun and Murphy 2009;Lofke et al 2013a). However, while research in (Corresponding author) animals and fungi has revealed a complex machinery of cis-and trans-acting determinants, regulation of plant PM protein localization and turnover is still less understood (Murphy et al 2005;Schellmann and Pimpl 2009;Zarsky and Potocky 2010;Reyes et al 2011). Convincing evidence for clathrin-dependent endocytosis of PM proteins being operative in higher plants has been provided for only very recently (Dhonukshe et al 2007;Paul and Frigerio 2007).…”

Section: Introductionmentioning

confidence: 99%

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Plasma membrane protein ubiquitylation and degradation as determinants of positional growth in plants

Korbei

Luschnig

2013

J. Integr. Plant Biol.

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Being sessile organisms, plants evolved an unparalleled plasticity in their post-embryonic development, allowing them to adapt and finetune their vital parameters to an ever-changing environment. Crosstalk between plants and their environment requires tight regulation of information exchange at the plasma membrane (PM). Plasma membrane proteins mediate such communication, by sensing variations in nutrient availability, external cues as well as by controlled solute transport across the membrane border. Localization and steady-state levels are essential for PM protein function and ongoing research identified cis-and trans-acting determinants, involved in control of plant PM protein localization and turnover. In this overview, we summarize recent progress in our understanding of plant PM protein sorting and degradation via ubiquitylation, a post-translational and reversible modification of proteins. We highlight characterized components of the machinery involved in sorting of ubiquitylated PM proteins and discuss consequences of protein ubiquitylation on fate of selected PM proteins. Specifically, we focus on the role of ubiquitylation and PM protein degradation in the regulation of polar auxin transport (PAT). We combine this regulatory circuit with further aspects of PM protein sorting control, to address the interplay of events that might control PAT and polarized growth in higher plants.

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Plant endosomal trafficking pathways

Cited by 139 publications

References 63 publications

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

ESCRT-I Component VPS23A Affects ABA Signaling by Recognizing ABA Receptors for Endosomal Degradation

Hitching a Ride on Vesicles: Cauliflower Mosaic Virus Movement Protein Trafficking in the Endomembrane System

Plasma membrane protein ubiquitylation and degradation as determinants of positional growth in plants

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