Protein Degradation Mechanism of Eag1 K+ Channel
نویسندگان
چکیده
منابع مشابه
Eag1 K+ Channel: Endogenous Regulation and Functions in Nervous System
Ether-à-go-go1 (Eag1, Kv10.1, KCNH1) K+ channel is a member of the voltage-gated K+ channel family mainly distributed in the central nervous system and cancer cells. Like other types of voltage-gated K+ channels, the EAG1 channels are regulated by a variety of endogenous signals including reactive oxygen species, rendering the EAG1 to be in the redox-regulated ion channel family. The role of EA...
متن کاملCa2+‐binding protein centrin 4 is a novel binding partner of rat Eag1 K+ channels
Eag1 is neuron-specific K(+) channel abundantly expressed in the brain and retina. Subcellular localization and physiological analyses in neurons reveal that Eag1 may participate in Ca(2+)-signaling processes in the synapse. Here, we searched for rat Eag1 (rEag1)-binding proteins that may contribute to Ca(2+) regulation of the K(+) channel. Yeast two-hybrid screening identified centrin 4, a mem...
متن کاملCullin 7 mediates proteasomal and lysosomal degradations of rat Eag1 potassium channels
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 ...
متن کاملExpression of Eag1 K+ channel and ErbBs in human pituitary adenomas: cytoskeleton arrangement patterns in cultured cells.
Pituitary adenomas can invade surrounded tissue, but the mechanism remains elusive. Ether à go-go-1 (Eag1) potassium channel and epidermal growth factor receptors (ErbB1 and ErbB2) have been associated to invasive phenotypes or poor prognosis in cancer patients. However, cells arrange their cytoskeleton in order to acquire a successful migration pattern. We have studied ErbBs and Eag1 expressio...
متن کاملNa+ activation of the muscarinic K+ channel by a G-protein-independent mechanism
Muscarinic potassium channels (KACh) are composed of two subunits, GIRK1 and GIRK4 (or CIR), and are directly gated by G proteins. We have identified a novel gating mechanism of KACh, independent of G-protein activation. This mechanism involved functional modification of KACh which required hydrolysis of physiological levels of intracellular ATP and was manifested by an increase in the channel ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2018
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2017.11.1681