Voici les éléments 1 - 10 sur 11
  • Publication
    Métadonnées seulement
    The Cytosolic Tail Dipeptide Ile-Met of the Pea Receptor BP80 Is Required for Recycling from the Prevacuole and for Endocytosis
    (2010)
    Saint-Jean, B.
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    Seveno-Carpentier, E.
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    Alcon, C.
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    Paris, Nadine
    Pea (Pisum sativum) BP80 is a vacuolar sorting receptor for soluble proteins and has a cytosolic domain essential for its intracellular trafficking between the trans-Golgi network and the prevacuole. Based on mammalian knowledge, we introduced point mutations in the cytosolic region of the receptor and produced chimeras of green fluorescent protein fused to the transmembrane domain of pea BP80 along with the modified cytosolic tails. By analyzing the subcellular location of these chimera, we found that mutating Glu-604, Asp-616, or Glu-620 had mild effects, whereas mutating the Tyr motif partially redistributed the chimera to the plasma membrane. Replacing both Ile-608 and Met-609 by Ala (IMAA) led to a massive redistribution of fluorescence to the vacuole, indicating that recycling is impaired. When the chimera uses the alternative route, the IMAA mutation led to a massive accumulation at the plasma membrane. Using Arabidopsis thaliana plants expressing a fluorescent reporter with the full-length sequence of At VSR4, we demonstrated that the receptor undergoes brefeldin A-sensitive endocytosis. We conclude that the receptors use two pathways, one leading directly to the lytic vacuole and the other going via the plasma membrane, and that the Ileu-608 Met-609 motif has a role in the retrieval step in both pathways.
  • Publication
    Métadonnées seulement
    Plant vacuoles. from biogenesis to function
    (2005) ;
    Paris, Nadine
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    Samaj, J. E.
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    Baluska, F. E.
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    Menzel, D.
  • Publication
    Métadonnées seulement
  • Publication
    Métadonnées seulement
    Targeting of ProConA to the Plant Vacuole Depends on Its Nine Amino-Acid C-Terminal Propeptide
    (2005)
    Saint-Jore-Dupas, Claude
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    Gilbert, Marie-Agnès
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    Ramis, Catalina
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    Paris, Nadine
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    Kiefer-Meyer, Marie-Christine
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    Faye, Loic
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    Gomord, Véronique
  • Publication
    Métadonnées seulement
    Arabidopsis mu A-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1
    (2004)
    Happel, Nicole
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    Honing, Stefan
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    Paris, Nadine
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    Robinson, David G
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    Holstein, Susanne E H
    In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) mu-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXO). We have analyzed the function of the muA-adaptin, one of the five mu-adaptins from Arabidopsis thaliana, by pull-down assays and plasmon resonance measurements using its receptor-binding domain (RBD) fused to a histidine tag. We show that this adaptin is able to bind the consensus tyrosine motif YXXO from the pea vacuolar sorting receptor (VSR)-PS1, as well as from the mammalian trans-Golgi network (TGN)38 protein. Moreover, the tyrosine residue was revealed to be crucial for binding of the complete cytoplasmic tail of VSR-PS1 to the plant muA-adaptin. The trans-Golgi localization of the muA-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.
  • Publication
    Métadonnées seulement
  • Publication
    Métadonnées seulement
  • Publication
    Métadonnées seulement
    Plant cell biology
    (Oxford: Oxford University Press, 2002)
    Ceriotti, A.
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    Paris, Nadine
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    Hillmer, S.
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    Frigerio, L.
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    Vitale, A.
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    Robinson, D. G.
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    Lord, M. E.
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    Davey, J.
  • Publication
    Métadonnées seulement
    Demonstration in yeast of the function of BP-80, a putative plant vacuolar sorting receptor
    (2001)
    Humair, David
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    Hernández Felipe, Doramys
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    ;
    Paris, Nadine
  • Publication
    Métadonnées seulement
    The internal propeptide of the ricin precursor carries a sequence-specific determinant for vacuolar sorting
    (2001)
    Frigerio, Lorenzo
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    Jolliffe, Nicholas A
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    Di Cola, Alessandra
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    Hernández Felipe, Doramys
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    Paris, Nadine
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    Lord, J Michael
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    Ceriotti, Aldo
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    Roberts, Lynne M
    Ricin is a heterodimeric toxin that accumulates in the storage vacuoles of castor bean (Ricinus communis) endosperm. Proricin is synthesized as a single polypeptide precursor comprising the catalytic A chain and the Gal-binding B chain joined by a 12-amino acid linker propeptide. Upon arrival in the vacuole, the linker is removed. Here, we replicate these events in transfected tobacco (Nicotiana tabacum) leaf protoplasts. We show that the internal linker propeptide is responsible for vacuolar sorting and is sufficient to redirect the ricin heterodimer to the vacuole when fused to the A or the B chain. This internal peptide can also target two different secretory protein reporters to the vacuole. Moreover, mutation of the isoleucine residue within an NPIR-like motif of the propeptide affects vacuolar sorting in proricin and in the reconstituted A-B heterodimer. This is the first reported example of a sequence-specific vacuolar sorting signal located within an internal propeptide.