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Related Experiment Videos

PICK1 interacts with ABP/GRIP to regulate AMPA receptor trafficking.

Wei Lu1, Edward B Ziff

  • 1Program in Neuroscience and Physiology, New York University School of Medicine, New York, New York 10016, USA.

Neuron
|August 2, 2005
PubMed
Summary

Protein interactions involving PICK1 and ABP/GRIP control AMPA receptor (AMPAR) GluR2 trafficking. Disrupting PICK1-ABP/GRIP binding impairs GluR2 phosphorylation and surface expression, affecting receptor endocytosis and recycling.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • The AMPA receptor (AMPAR) GluR2 subunit C terminus interacts with PICK1 and ABP/GRIP.
  • Receptor trafficking is potentially initiated by the transfer of GluR2 from ABP/GRIP to PICK1, a process facilitated by GluR2 S880 phosphorylation.

Purpose of the Study:

  • To investigate the protein interactions that regulate AMPA receptor GluR2 trafficking.
  • To elucidate the role of PICK1 and ABP/GRIP interactions in GluR2 phosphorylation and surface expression.

Main Methods:

  • Protein interaction studies involving PICK1, ABP/GRIP, GluR2, and PKCalpha.
  • Analysis of GluR2 S880 phosphorylation.
  • Assessment of GluR2 surface expression, NMDA-induced endocytosis, and recycling.

Related Experiment Videos

Main Results:

  • The PICK1 BAR domain exhibits both intermolecular and intramolecular interactions.
  • Binding of PKCalpha or GluR2 to the PICK1 PDZ domain disrupts intramolecular interactions, promoting PICK1 BAR domain association with ABP/GRIP.
  • Interference with the PICK1-ABP/GRIP interaction impairs GluR2 phosphorylation and decreases surface expression, NMDA-induced endocytosis, and recycling.

Conclusions:

  • The interaction between PICK1 and ABP/GRIP is crucial for regulating GluR2 trafficking.
  • This interaction influences GluR2 phosphorylation by PKC and subsequent receptor trafficking events, including surface expression, endocytosis, and recycling.