IndraLab

Statements



sparser
"Moreover, VPA markedly increased the physical interaction between KCNQ4 and HSP90β ( xref A), which caused the upregulation of the protein expression of both KCNQ4 and HSP90β in HEK 293T cells."

sparser
"Furthermore, HDAC1 disrupted the KCNQ4HSP90β physical interaction ( xref B), which promoted the reduction in their protein expressions."

sparser
"VPA-Induced HSP90β Expression and HSP90βKCNQ4 Interaction."

sparser
"Indeed, HSP90α and HSP90β both bind to KCNQ4 and exert opposite effects on the KCNQ4 channel."

sparser
"However, HDAC1 (myc) interrupted the HSP90β (HA)–KCNQ4 (His) binding by recruiting KCNQ4 ( xref B)."

sparser
"Western blot showed that both HSP90α and HSP90β co-precipitated with KCNQ4 proteins; conversely, KCNQ4 proteins were detected in HSP90α and HSP90β immunoprecipitates ( xref , A. and B.), which confirmed that HSP90α and HSP90β physically interact with KCNQ4 proteins."

sparser
"This result showed that KCNQ4 binding competed with HDAC1 and HSP90β and that the KCNQ4–HDAC1 binding affinity was stronger than that of KCNQ4HSP90β."

sparser
"In summary, VPA suppressed HDAC1, leading to upregulation of KCNQ4, HSP90β expression, and interaction between KCNQ4 and HSP90β."

sparser
"VPA suppressed HDAC1, leading to upregulation of KCNQ4, HSP90β expression, and interaction between KCNQ4 and HSP90β."

sparser
"Overall, VPA treatment upregulated HSP90β and increased HSP90βKCNQ4 binding by inhibiting HDAC1 activation."

sparser
"The overexpression of HDAC1 downregulated KCNQ4 and HSP90β expression and disrupted the binding of KCNQ4 to HSP90β."

sparser
"In addition, treatment with VPA increased the KCNQ4 binding with HSP90β by inhibiting HDAC1 activation in HEI-OC1 in an in vitro study."