KRIP6: A novel BTB/kelch protein regulating function of kainate receptors

Fernanda Laezza, Timothy J. Wilding, Sunitha Sequeira, Françoise Coussen, Xue Zhao Zhang, Rona Hill-Robinson, Christophe Mulle, James E. Huettner, Ann Marie Craig

Research output: Contribution to journalArticlepeer-review

41 Scopus citations


Whereas many interacting proteins have been identified for AMPA and NMDA glutamate receptors, fewer are known to directly bind and regulate function of kainate receptors. Using a yeast two-hybrid screen for interacting partners of the C-terminal domain of GluR6a, we identified a novel neuronal protein of the BTB/kelch family, KRIP6. KRIP6 binds to the GluR6a C-terminal domain at a site distinct from the PDZ-binding motif and it co-immunoprecipitates with recombinant and endogenous GluR6. Co-expression of KRIP6 alters GluR6 mediated currents in a heterologous expression system reducing peak current amplitude and steady-state desensitization, without affecting surface levels of GluR6. Endogenous KRIP6 is widely expressed in brain and overexpression of KRIP6 reduces endogenous kainate receptor-mediated responses evoked in hippocampal neurons. Taken together, these results suggest that KRIP6 can directly regulate native kainate receptors and provide the first evidence for a BTB/kelch protein in direct functional regulation of a mammalian glutamate receptor.

Original languageEnglish (US)
Pages (from-to)539-550
Number of pages12
JournalMolecular and Cellular Neuroscience
Issue number4
StatePublished - Apr 2007
Externally publishedYes


  • BTB/kelch proteins
  • Desensitization
  • GluR6
  • Hippocampus
  • Kainate receptors

ASJC Scopus subject areas

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology


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