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Neuhaus, Jean-Marc
Nom
Neuhaus, Jean-Marc
Affiliation principale
Fonction
Professeur ordinaire
Email
jean-marc.neuhaus@unine.ch
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2 Résultats
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- PublicationMétadonnées seulementArabidopsis mu A-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1(2004)
;Happel, Nicole ;Honing, Stefan; ;Paris, Nadine ;Robinson, David GHolstein, Susanne E HIn 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. - PublicationAccès libreArabidopsisµA-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1(2004)
;Happel, Nicole ;Höning, Stefan; ;Paris, Nadine ;Robinson, David G.Holstein, Suzanne E. H.In receptor-mediated transport pathways in mammalian cells, clathrin-coated vesicle (CCV) µ-adaptins are the main binding partners for the tyrosine sorting/internalization motif (YXXØ). We have analyzed the function of the µA-adaptin, one of the five µ-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 YXXØ 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 µA-adaptin. The trans-Golgi localization of the µA-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.