The sorLA cytoplasmic domain interacts with GGA1 and -2 and defines minimum requirements for GGA binding

FEBS Lett. 2002 Jan 30;511(1-3):155-8. doi: 10.1016/s0014-5793(01)03299-9.


We report that the Vps10p domain receptor sorLA binds the adaptor proteins GGA1 and -2, which take part in Golgi-endosome sorting. The GGAs bind with differential requirements via three critical residues in the C-terminal segment of the sorLA cytoplasmic tail. Unlike in sortilin and the mannose 6-phosphate receptors, the GGA-binding segment in sorLA contains neither an acidic cluster nor a dileucine. Our results support the concept of sorLA as a potential sorting receptor and suggest that key residues in sorLA and sortilin conform to a new type of motif (psi-psi-X-X-phi) defining minimum requirements for GGA binding to cytoplasmic receptor domains.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ADP-Ribosylation Factors / chemistry
  • ADP-Ribosylation Factors / genetics
  • ADP-Ribosylation Factors / metabolism*
  • Adaptor Proteins, Vesicular Transport*
  • Amino Acid Sequence
  • Binding Sites
  • Carrier Proteins / chemistry
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cytoplasm / metabolism*
  • Golgi Apparatus / metabolism
  • Hydrophobic and Hydrophilic Interactions
  • Methionine / genetics
  • Methionine / metabolism
  • Molecular Sequence Data
  • Protein Binding
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Proteins / genetics
  • Proteins / metabolism*
  • Receptors, LDL / chemistry*
  • Receptors, LDL / genetics
  • Receptors, LDL / metabolism*
  • Two-Hybrid System Techniques


  • Adaptor Proteins, Vesicular Transport
  • Carrier Proteins
  • GGA adaptor proteins
  • GGA2 protein, human
  • Proteins
  • Receptors, LDL
  • Methionine
  • ADP-Ribosylation Factors