The synaptic scaffolding protein Delphilin interacts with monocarboxylate transporter 2

Neuroreport. 2007 Mar 26;18(5):489-93. doi: 10.1097/WNR.0b013e3280586821.

Abstract

Delphilin, which interacts with a glutamate receptor (GluR) delta2-subunit, is a postsynaptic density scaffolding protein at the cerebellar parallel fiber-Purkinje cell synapses. Delphilin specifically interacts with the GluRdelta2 C-terminus via its postsynaptic density-95/discs-large/ZO-1 (PDZ) domain. As a number of PDZ-containing scaffolding proteins bind to several membrane proteins, we expected that Delphilin might also have other binding partners besides GluRdelta2. To search for the link between Delphilin and other binding proteins, we carried out screening among candidate membrane proteins localized in Purkinje cells by surface plasmon resonance analyses. As a result, we found that the C-terminus of the monocarboxylate transporter 2 binds specifically and significantly with Delphilin PDZ and there is a probable existence of GluRdelta2-Delphilin-monocarboxylate transporter 2 complex in synaptic membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cerebellum / cytology
  • Immunoprecipitation / methods
  • Mice
  • Monocarboxylic Acid Transporters / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • Purkinje Cells / ultrastructure
  • Receptors, Glutamate / metabolism
  • Subcellular Fractions / metabolism
  • Surface Plasmon Resonance / methods
  • Synapses / ultrastructure
  • Synaptic Membranes / metabolism*
  • Time Factors

Substances

  • Monocarboxylic Acid Transporters
  • Nerve Tissue Proteins
  • Receptors, Glutamate
  • Slc16a7 protein, mouse
  • delphilin
  • glutamate receptor delta 2
  • postsynaptic density proteins