A Family of Plasmodesmal Proteins with Receptor-Like Properties for Plant Viral Movement Proteins

Amari, Khalid; Boutant, Emmanuel; Hofmann, Christina; Schmitt-Keichinger, Corinne; Fernández‐Calvino, Lourdes; Didier, Pascal; Lerich, Alexander; Mutterer, Jérôme; Thomas, Colwyn M.; Heinlein, Manfred; Mély, Yves; Maule, Andrew J.; Ritzenthaler, Christophe

doi:10.1371/journal.ppat.1001119

Cited by 166 publications

(176 citation statements)

References 59 publications

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“…The evidence we provide that the MPtyr1-2-3 mutant can efficiently interact with PDLP1 (Fig. 5), a PD protein involved in the assembly of CaMV MP into tubules (Amari et al, 2010), suggests that this mutant is potentially competent to form tubules and that its failure to accumulate in PD (Supplemental Fig. S3) and to form tubules (Fig.…”

Section: Discussionmentioning

confidence: 74%

“…CaMV movement certainly requires large amounts of MP at the cell periphery; thus, MP would cycle between the PM and endosomes to specifically target PD and to be readily available in the amounts required for tubule formation. As CaMV MP and virions have never been found in close vicinity anywhere other than in the PD channel (Stavolone et al, 2005), we hypothesize that, at or near the PD, MP encounters virus particles and with the help of PDLP proteins (Amari et al, 2010) assembles in tubules to move virions through the plasmodesmal pore. To maintain homeostasis at the cell periphery and/or to prevent permanent gating of PD and the consequent deleterious cytopathic effects for host (and, in turn, virus) survival, excess MP molecules at the PM are targeted for degradation via MVBs.…”

Section: Discussionmentioning

confidence: 97%

“…When fused to GFP, MP cannot facilitate virus movement, probably because the fusion protein is sterically hindered in tubule assembly within the PD pore (Thomas and Maule, 2000;Amari et al, 2010). Therefore, a role for MP endocytosis in virus activity was examined by testing the effect of Tyr domain mutations on CaMV viability and infectivity.…”

Section: Yxxf Signals Play Redundant But Essential Roles In Camv Inmentioning

confidence: 99%

“…Within PD, CaMV MP interacts with PD-located protein1 (PDLP1), a protein with receptor-like properties involved in the assembly of MP tubules required for virus movement (Amari et al, 2010). To exclude that mutation of Tyr signals changed the structural properties of MP, causing the failure of such interaction and thus explaining the loss of MP tubule assembly function, we tested the ability of the MPts1-2-3 mutant to bind PDLP1.…”

Section: Tyr-based Sorting Motifs Are Essential For Tubule Formation mentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 74%

Section: Discussionmentioning

confidence: 97%

Section: Yxxf Signals Play Redundant But Essential Roles In Camv Inmentioning

confidence: 99%

Section: Tyr-based Sorting Motifs Are Essential For Tubule Formation mentioning

confidence: 99%

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

2014

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“…To quantitatively record MT patterns, we adapted an approach used previously to measure actin structures in mammalian cells (Möller et al, 2014). We imaged epidermal cell outlines in the red channel by PI staining or by the expression of an RFP-fused PM-localized protein, PLASMODESMATA-LOCATED PROTEIN1 (PDLP1)-RFP (Amari et al, 2010), and traced GFP-IQD-decorated MT arrays in the green channel. Two-channel maximum projections of Z-stacks covering the upper half of the epidermal cell layer were analyzed, texture feature vectors were extracted from square windows based on local binary patterns (Ojala et al, 2002), and groups of MT patterns were defined by cluster analysis (Fig.…”

Section: Quantitative Analysis Of Gfp-iqd-labeled Mt Patternsmentioning

confidence: 99%

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

et al. 2017

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ORCID IDs: 0000-0002-3493-4800 (K.B.); 0000-0002-7146-043X (B.M.).Calcium (Ca 2+ ) signaling and dynamic reorganization of the cytoskeleton are essential processes for the coordination and control of plant cell shape and cell growth. Calmodulin (CaM) and closely related calmodulin-like (CML) polypeptides are principal sensors of Ca 2+ signals. CaM/CMLs decode and relay information encrypted by the second messenger via differential interactions with a wide spectrum of targets to modulate their diverse biochemical activities. The plant-specific IQ67 DOMAIN (IQD) family emerged as possibly the largest class of CaM-interacting proteins with undefined molecular functions and biological roles. Here, we show that the 33 members of the IQD family in Arabidopsis (Arabidopsis thaliana) differentially localize, using green fluorescent protein (GFP)-tagged proteins, to multiple and distinct subcellular sites, including microtubule (MT) arrays, plasma membrane subdomains, and nuclear compartments. Intriguingly, the various IQD-specific localization patterns coincide with the subcellular patterns of IQD-dependent recruitment of CaM, suggesting that the diverse IQD members sequester Ca 2+ -CaM signaling modules to specific subcellular sites for precise regulation of Ca 2+ -dependent processes. Because MT localization is a hallmark of most IQD family members, we quantitatively analyzed GFP-labeled MT arrays in Nicotiana benthamiana cells transiently expressing GFP-IQD fusions and observed IQD-specific MT patterns, which point to a role of IQDs in MT organization and dynamics. Indeed, stable overexpression of select IQD proteins in Arabidopsis altered cellular MT orientation, cell shape, and organ morphology. Because IQDs share biochemical properties with scaffold proteins, we propose that IQD families provide an assortment of platform proteins for integrating CaM-dependent Ca 2+ signaling at multiple cellular sites to regulate cell function, shape, and growth.

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Secoviridae: A Family of Plant Picorna‐Like Viruses with Monopartite or Bipartite Genomes

Sanfaçon

2015

Encyclopedia of Life Sciences

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Members of the family Secoviridae , referred to as secovirids, are plant viruses that share features with animal and human viruses of the family Picornaviridae and other insect or marine viruses of the order Picornavirales . These common features include a conserved structure of the icosahedral virus particles, the expression of viral proteins by proteolytic cleavage of large polyproteins and viral replication proteins with conserved sequence motifs, including the viral RNA‐dependent RNA polymerase and protease. Secovirids also share the distinguishing feature of encoding specialised proteins that enable their movement in plant and counteract plant defence mechanisms, such as RNA silencing. The family Secoviridae includes eight genera. Members of the genera Comovirus , Fabavirus , Nepovirus , Cheravirus , Sadwavirus and Torradovirus have a bipartite positive‐strand RNA genome, whereas members of the genera Sequivirus and Waikavirus have a monopartite genome. Key Concepts Many plant viruses are related to animal and human viruses of the family Picornaviridae and to other picorna‐like viruses infecting algae and arthropods. A recent update in the taxonomy of plant picorna‐like viruses has led to the creation of the family Secoviridae which amalgamates the previous families Comoviridae and Sequiviridae as well as the genera Cheravirus , Sequivirus and Torradovirus . Secovirids share common characteristics including having both similar virus particle structures and genomic organizations and requiring specialised proteins to facilitate their movement within the host plant or counteract plant defence mechanism. Secovirids produce their proteins in the form of large polyproteins that are cleaved at specific sites by a viral protease. Replication of the viral RNA occurs in large protein complexes in association with intracellular membranes from the host. Plant cells infected with secovirids generally display tubular structures that are composed of the viral movement protein, contain virus‐like particles and traverse the cell wall. These tubular structures are involved in the movement of the virus from cell to cell. Secovirids can be transmitted through seeds and pollen or with the help of nematode or arthropod vectors and their spread in the field is largely dependent on their mode of transmission. Some secovirids have been successfully exploited as plant vectors, allowing epitope presentation for vaccine production, expression of proteins in plants and silencing of endogenous plant genes.

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A Family of Plasmodesmal Proteins with Receptor-Like Properties for Plant Viral Movement Proteins

Cited by 166 publications

References 59 publications

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

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

The IQD Family of Calmodulin-Binding Proteins Links Calcium Signaling to Microtubules, Membrane Subdomains, and the Nucleus

Secoviridae: A Family of Plant Picorna‐Like Viruses with Monopartite or Bipartite Genomes

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