Cullin 7 mediates proteasomal and lysosomal degradations of rat Eag1 potassium channels.

ABSTRACT: Mammalian Eag1 (Kv10.1) potassium (K⁺) channels are widely expressed in the brain. Several mutations in the gene encoding human Eag1 K⁺ channel have been associated with congenital neurodevelopmental anomalies. Currently very little is known about the molecules mediating protein synthesis and degradation of Eag1 channels. Herein we aim to ascertain the protein degradation mechanism of rat Eag1 (rEag1). We identified cullin 7 (Cul7), a member of the cullin-based E3 ubiquitin ligase family, as a novel rEag1 binding partner. Immunoprecipitation analyses confirmed the interaction between Cul7 and rEag1 in heterologous cells and neuronal tissues. Cul7 and rEag1 also exhibited significant co-localization at synaptic regions in neurons. Over-expression of Cul7 led to reduced

SUBMITTER: Hsu PH 

PROVIDER: S-EPMC5241692 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature