KRIP6: a novel BTB/kelch protein regulating function of kainate receptors.
Molecular and Cellular Neuroscience. 2007-04-01; 34(4): 539-550
DOI: 10.1016/j.mcn.2006.12.003
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1. Mol Cell Neurosci. 2007 Apr;34(4):539-50. Epub 2007 Jan 24.
KRIP6: a novel BTB/kelch protein regulating function of kainate receptors.
Laezza F(1), Wilding TJ, Sequeira S, Coussen F, Zhang XZ, Hill-Robinson R, Mulle
C, Huettner JE, Craig AM.
Author information:
(1)Department of Anatomy and Neurobiology, Washington University School of
Medicine, St. Louis, MO 63110, USA.
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.
DOI: 10.1016/j.mcn.2006.12.003
PMCID: PMC1939939
PMID: 17254796 [Indexed for MEDLINE]