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Neuhaus, Jean-Marc

Nom
Neuhaus, Jean-Marc
Affiliation principale
Fonction
Professeur ordinaire
Email
jean-marc.neuhaus@unine.ch
Identifiants
https://libra.unine.ch/handle/123456789/300

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  • Publication
    Métadonnées seulement
    Arabidopsis mu A-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1
    (2004)
    Happel, Nicole
    ;
    Honing, Stefan
    ;
    Neuhaus, Jean-Marc 
    ;
    Paris, Nadine
    ;
    Robinson, David G
    ;
    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
    The internal propeptide of the ricin precursor carries a sequence-specific determinant for vacuolar sorting
    (2001)
    Frigerio, Lorenzo
    ;
    Jolliffe, Nicholas A
    ;
    Di Cola, Alessandra
    ;
    Hernández Felipe, Doramys
    ;
    Paris, Nadine
    ;
    Neuhaus, Jean-Marc 
    ;
    Lord, J Michael
    ;
    Ceriotti, Aldo
    ;
    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.