Arabidopsis mu A-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1
Author(s)
Happel, Nicole
Honing, Stefan
Paris, Nadine
Robinson, David G
Holstein, Susanne E H
Date issued
2004
In
Plant Journal
Vol
5
No
37
From page
678
To page
693
Subjects
mu-adaptin vacuolar transport tyrosine-based sorting motif TRANS-GOLGI NETWORK CLATHRIN ASSEMBLY PROTEIN COATED VESICLE ADAPTERS PLASMA-MEMBRANE MEDIUM CHAINS CYTOPLASMIC DOMAIN PREVACUOLAR COMPARTMENT STRUCTURAL EXPLANATION TARGETING RECEPTOR APPENDAGE DOMAIN
Abstract
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 type
journal article