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Methods for the Discovery of Novel Compounds Modulating a Gamma-Aminobutyric Acid Receptor Type A Neurotransmission
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GGA autoinhibition revisited.

Jacob F Cramer1, Camilla Gustafsen, Manja A Behrens

  • 1MIND Centre, Department of Molecular Biology, Aarhus University, Gustav Wieds Vej 10 C, DK-8000 Aarhus C, Denmark.

Traffic (Copenhagen, Denmark)
|December 18, 2009
PubMed
Summary

The study challenges the concept of GGA1 autoinhibition, finding that intrinsic motifs are inactive. Only C-terminal DXXLL motifs are active GGA binding sites, refuting the functional significance of GGA autoinhibition.

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Area of Science:

  • Cell biology
  • Molecular and structural biology
  • Protein trafficking

Background:

  • Cytosolic adaptors GGA1-3 are crucial for sorting transmembrane proteins.
  • These proteins possess a C-terminal acidic dileucine motif (DXXLL).
  • GGA1 and GGA3 have intrinsic motifs proposed as autoinhibitory sites activated by phosphorylation.

Purpose of the Study:

  • To structurally and functionally examine the autoinhibition concept of GGA1.
  • To determine the role of intrinsic motifs versus C-terminal DXXLL motifs in GGA binding.
  • To investigate the impact of phosphorylation on GGA1 conformation and binding.

Main Methods:

  • Structural analysis of GGA1.
  • Functional assays to assess GGA1 binding.
  • Phosphorylation site analysis.

Main Results:

  • GGA1's intrinsic motif is inactive; only C-terminal DXXLL motifs are active binding sites.
  • Aspartates and upstream phosphoserines (1-2 positions) enhance GGA1 binding.
  • Phosphorylation of GGA1 does not alter its conformation or binding to Sortilin and SorLA.

Conclusions:

  • The functional significance of GGA autoinhibition is refuted.
  • Intrinsic GGA binding motifs appear to lack general functional importance.
  • C-terminal DXXLL motifs are the primary active GGA binding sites.