Selective Trafficking of Non-Cell-Autonomous Proteins Mediated by NtNCAPP1

Lee, Jinkee; Yoo, Byung-Chun; Rojas, María R.; Gomez‐Ospina, Natalia; Staehelin, L. Andrew; Lucas, William J.

doi:10.1126/science.1077813

Cited by 162 publications

(126 citation statements)

References 21 publications

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“…1 The identification of the plant functional analogs of viral MPs suggests the presence of endogenous RNA transport machinery in transportation of non-cell autonomous RNAs. 37,38 Previously, the movement of KN1 RNA was found to be mediated through its own protein. 39,40 However, when FT protein was retained in companion cells, FT RNA still moved long distance to the scion (Fig.…”

Section: P35s-ft-ir/p35s-rfp-ft P35s-ft-ir/p35s-gfp-ftmentioning

confidence: 99%

Long-distance movement of ArabidopsisFLOWERING LOCUS TRNA participates in systemic floral regulation

Huang

Liu

et al. 2012

RNA Biology

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Section: P35s-ft-ir/p35s-rfp-ft P35s-ft-ir/p35s-gfp-ftmentioning

confidence: 99%

Long-distance movement of ArabidopsisFLOWERING LOCUS TRNA participates in systemic floral regulation

Huang

Liu

et al. 2012

RNA Biology

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“…Also, binding studies of MP30 with cell fractions enriched in plasmodesmal components indicate the presence of potential receptor molecules mediating protein movement via plasmodesmata (Kragler et al, 1998). Recently, Nt-NCAPP1, an ER-localized protein, was found to be involved in the plasmodesmal transport pathway of MP30 (Lee et al, 2003). Furthermore, a cell wallassociated kinase is known to phosphorylate the MP30 (Citovsky et al, 1993) thereby modulating its cell-to-cell movement activity (Waigmann et al, 2000).…”

mentioning

confidence: 99%

MPB2C, a Microtubule-Associated Plant Protein Binds to and Interferes with Cell-to-Cell Transport of Tobacco Mosaic Virus Movement Protein

et al. 2003

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The movement protein of tobacco mosaic virus, MP30, mediates viral cell-to-cell transport via plasmodesmata. The complex MP30 intra-and intercellular distribution pattern includes localization to the endoplasmic reticulum, cytoplasmic bodies, microtubules, and plasmodesmata and likely requires interaction with plant endogenous factors. We have identified and analyzed an MP30-interacting protein, MPB2C, from the host plant Nicotiana tabacum. MPB2C constitutes a previously uncharacterized microtubule-associated protein that binds to and colocalizes with MP30 at microtubules. In vivo studies indicate that MPB2C mediates accumulation of MP30 at microtubules and interferes with MP30 cell-to-cell movement. In contrast, intercellular transport of a functionally enhanced MP30 mutant, which does not accumulate and colocalize with MP30 at microtubules, is not impaired by MPB2C. Together, these data support the concept that MPB2C is not required for MP30 cell-to-cell movement but may act as a negative effector of MP30 cell-to-cell transport activity.Plant viruses produce movement proteins required to mediate cell-to-cell spread of the viral genomic information via plasmodesmata (Lucas, 1995;Lazarowitz and Beachy, 1999;McLean and Zambryski, 2000;Tzfira et al., 2000;Haywood et al., 2002;Heinlein, 2002). Tobacco mosaic virus (TMV), a virus with a (ϩ) single-stranded RNA genome encodes one of the most extensively studied movement proteins, MP30. Several biochemical and cell biological features of MP30 were revealed: MP30 binds cooperatively single-stranded nucleic acids (Citovsky et al., 1990), interacts with the tubulin-and actin-based cytoskeleton (Heinlein et al., 1995;McLean et al., 1995), associates to the endoplasmic reticulum (ER; Heinlein et al., 1998;Reichel and Beachy, 1998;Mas and Beachy, 1999;Gillespie et al., 2002), and increases the size exclusion limit of plasmodesmata (Wolf et al., 1989;Waigmann et al., 1994). In the current model, MP30 is proposed to form complexes with genomic TMV-RNA (vRNA) and to move these vRNA-protein complexes from ER-associated sites of synthesis throughout the cell via the cytoskeletal network toward plasmodesmata. There, MP30 induces an increase in plasmodesmal size exclusion limit and facilitates the transport of the vRNA-MP30 complex through the enlarged plasmodesmal channels into adjacent cells (Lazarowitz and Beachy, 1999;Tzfira et al., 2000;Haywood et al., 2002;Heinlein, 2002). In line with this model, microtubules have been functionally implicated in guiding vRNA-MP30 complexes toward plasmodesmata (Mas and Beachy, 2000; Boyko et al., 2000a Boyko et al., , 2000b. However, an alternate, non-movement-promoting role of microtubules in providing a route toward an MP30 degradation site was suggested (Padgett et al., 1996;Mas and Beachy, 1999;Reichel and Beachy, 2000). This model is supported by the observation that TMV was able to spread in tissues with functionally impaired microtubules and by studies performed with a mutant variant of MP30, MP R3 with strongly decreased affinity...

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“…A destination-selective mechanism was also proposed for the trafficking of proteins in sieve elements (Aoki et al, 2005). A few non-cell-autonomous proteins (NCAPs) binding to phloem sap proteins and acting as chaperones have been implicated in this longdistance trafficking pathway (Aoki et al, 2002(Aoki et al, , 2005Lee et al, 2003;Taoka et al, 2007;Ham et al, 2009).…”

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confidence: 99%

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

et al. 2010

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Phloem Protein2 (PP2) is a component of the phloem protein bodies found in sieve elements. We describe here the lectin properties of the Arabidopsis (Arabidopsis thaliana) PP2-A1. Using a recombinant protein produced in Escherichia coli, we demonstrated binding to N-acetylglucosamine oligomers. Glycan array screening showed that PP2-A1 also bound to highmannose N-glycans and 9-acyl-N-acetylneuraminic sialic acid. Fluorescence spectroscopy-based titration experiments revealed that PP2-A1 had two classes of binding site for N,N#,N$-triacetylchitotriose, a low-affinity site and a high-affinity site, promoting the formation of protein dimers. A search for structural similarities revealed that PP2-A1 aligned with the Cbm4 and Cbm22-2 carbohydrate-binding modules, leading to the prediction of a b-strand structure for its conserved domain. We investigated whether PP2-A1 interacted with phloem sap glycoproteins by first characterizing abundant Arabidopsis phloem sap proteins by liquid chromatography-tandem mass spectrometry. Then we demonstrated that PP2-A1 bound to several phloem sap proteins and that this binding was not completely abolished by glycosidase treatment. As many plant lectins have insecticidal activity, we also assessed the effect of PP2-A1 on weight gain and survival in aphids. Unlike other mannosebinding lectins, when added to an artificial diet, recombinant PP2-A1 had no insecticidal properties against Acyrthosiphon pisum and Myzus persicae. However, at mid-range concentrations, the protein affected weight gain in insect nymphs. These results indicate the presence in PP2-A1 of several carbohydrate-binding sites, with potentially different functions in the trafficking of endogenous proteins or in interactions with phloem-feeding insects.

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Selective Trafficking of Non-Cell-Autonomous Proteins Mediated by NtNCAPP1

Cited by 162 publications

References 21 publications

Long-distance movement of ArabidopsisFLOWERING LOCUS TRNA participates in systemic floral regulation

Long-distance movement of ArabidopsisFLOWERING LOCUS TRNA participates in systemic floral regulation

MPB2C, a Microtubule-Associated Plant Protein Binds to and Interferes with Cell-to-Cell Transport of Tobacco Mosaic Virus Movement Protein

Binding Properties of the N-Acetylglucosamine and High-Mannose N-Glycan PP2-A1 Phloem Lectin in Arabidopsis

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