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Arabidopsis µA‐adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR‐PS1
Author(s) -
Happel Nicole,
Höning Stefan,
Neuhaus JeanMarc,
Paris Nadine,
Robinson David G.,
Holstein Susanne E. H.
Publication year - 2004
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2003.01995.x
Subject(s) - clathrin , golgi apparatus , tyrosine , vacuole , internalization , arabidopsis , endosome , microbiology and biotechnology , cytoplasm , biology , vesicle , receptor , clathrin adaptor proteins , biochemistry , gene , endocytosis , membrane , endoplasmic reticulum , mutant
Summary 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.