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Structural basis for spinophilin-neurabin receptor interaction.

Matthew S Kelker1, Barbara Dancheck, Tingting Ju

  • 1Department of Molecular Pharmacology, Physiology and Biotechnology, Brown University, 70 Ship Street, Box G-E3, Providence, Rhode Island 02912, USA.

Biochemistry
|February 7, 2007
PubMed
Summary

Neurabin and spinophilin PDZ domains bind glutamate receptors, revealing their role in targeting protein phosphatase 1 (PP1) to synapses. These neuronal proteins have distinct structural differences influencing peptide binding.

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Area of Science:

  • Neuroscience
  • Structural Biology
  • Molecular Biology

Background:

  • Neurabin and spinophilin are key neuronal scaffolding proteins regulating synaptic transmission.
  • They target protein phosphatase 1 (PP1) to dendritic spines, affecting glutamate receptor activity.
  • The mechanism of neurabin and spinophilin targeting to receptors remained unclear.

Purpose of the Study:

  • To elucidate the structural basis of neurabin and spinophilin interaction with synaptic targets.
  • To investigate the binding characteristics of neurabin and spinophilin PDZ domains with receptor peptides.
  • To classify the PDZ domains based on their binding properties.

Main Methods:

  • Biomolecular NMR spectroscopy was used to determine the structures of neurabin and spinophilin PDZ domains.
  • Two-dimensional 1H-15N HSQC NMR analysis was employed to study peptide binding.
  • C-terminal peptides from AMPA and NMDA receptors were synthesized for binding assays.

Main Results:

  • The structures of neurabin and spinophilin PDZ domains were determined, revealing canonical folds with distinct differences in peptide binding pockets.
  • Neurabin and spinophilin PDZ domains exhibit differential binding to C-terminal peptides from glutamatergic receptors and cytosolic proteins.
  • These PDZ domains were classified as neuronal hybrid class V, capable of binding both class I and II peptides.

Conclusions:

  • The PDZ domains of neurabin and spinophilin are crucial for targeting PP1 to glutamate receptors.
  • Structural differences in PDZ domains dictate differential binding to receptor subunits.
  • This interaction is vital for regulating PP1 activity at synaptic sites.