Arabidopsis mu A-adaptin interacts with the tyrosine motif of the vacuolar sorting receptor VSR-PS1

Plant J. 2004 Mar;37(5):678-93. doi: 10.1111/j.1365-313x.2003.01995.x.


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 (YXXØ). We have analyzed the function of the mu A-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 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 mu A-adaptin. The trans-Golgi localization of the mu A-adaptin strongly suggests its involvement in Golgi- to vacuole-trafficking events.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adaptor Protein Complex mu Subunits / genetics
  • Adaptor Protein Complex mu Subunits / metabolism*
  • Amino Acid Sequence
  • Arabidopsis / genetics
  • Arabidopsis / metabolism*
  • Arabidopsis Proteins / genetics
  • Arabidopsis Proteins / metabolism
  • DNA, Complementary / chemistry
  • DNA, Complementary / genetics
  • Gene Expression Regulation, Plant
  • Golgi Apparatus / metabolism
  • Molecular Sequence Data
  • Protein Transport
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Tyrosine / genetics
  • Tyrosine / metabolism*
  • Vacuoles / metabolism*
  • Vesicular Transport Proteins / genetics
  • Vesicular Transport Proteins / metabolism*


  • Adaptor Protein Complex mu Subunits
  • Arabidopsis Proteins
  • DNA, Complementary
  • Vesicular Transport Proteins
  • Tyrosine