14-3-3 proteins regulate cullin 7-mediated Eag1 degradation
Journal
Cell & bioscience
Journal Volume
13
Journal Issue
1
Date Issued
2023-01-30
Author(s)
Hsieh, Chang-Heng
Chou, Chia-Cheng
Fang, Ya-Ching
Hsu, Po-Hao
Chiu, Yi-Hung
Yang, Chi-Sheng
Jow, Guey-Mei
Jeng, Chung-Jiuan
Abstract
Mutations in the human gene encoding the neuron-specific Eag1 (KV10.1; KCNH1) potassium channel are linked to congenital neurodevelopmental diseases. Disease-causing mutant Eag1 channels manifest aberrant gating function and defective protein homeostasis. Both the E3 ubiquitin ligase cullin 7 (Cul7) and the small acid protein 14-3-3 serve as binding partners of Eag1. Cul7 mediates proteasomal and lysosomal degradation of Eag1 protein, whereas over-expression of 14-3-3 notably reduces Eag1 channel activity. It remains unclear whether 14-3-3 may also contribute to Eag1 protein homeostasis.
Subjects
Lysosomal degradation; Potassium channel; Proteasomal degradation; Protein interaction; Protein stability; Ubiquitin ligase
Type
journal article