IndraLab

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WNK4 inhibits KCNMA1. 11 / 11
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"Coexpression of WNK4 significantly inhibited BK channel activity and decreased the outward K currents as demonstrated in a current (I)/voltage (V) curve (XREF_FIG)."
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"Our results suggest that WNK4 inhibits BK channel activity, in part, by increasing channel degradation through an ubiquitin dependent pathway."
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"WNK4 kinase inhibits Maxi K channel activity by a kinase dependent mechanism."
21613417
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"suggested that WNK4 or a WNK4 mutant with a region containing a coiled coil domain and a autoinhibitory domain may decrease BK alpha-subunit plasma membrane expression as well as the whole cell expression, which suggests that WNK4 inhibits BK channel function by enhancing the degradation of BK channels via an ubiquitin dependent pathway in the distal nephron."
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"Here, we report that WNK4 wild-type (WT) significantly inhibits Maxi K channel activity in HEK alphaBK stable cell lines compared with the control group."
21613417
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"Previous studies have demonstrated that WNK4 inhibits BK channel activity by activating the ERK 1/2 signaling pathway and leading to enhancing BK degradation through a lysosomal pathway ( Kahle et al ., 2003 ; Zhuang et al ., 2011 ; Wang et al ., 2013 ; Yue et al ., 2013 ) , whereas WNK1 stimulates BK activity by suppressing the ERK 1/2 signaling pathway ( Liu et al ., 2015 ) ."
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"Previous studies have demonstrated that WNK4 inhibits BK channel activity by activating the ERK 1/2 signaling pathway and leading to enhancing BK degradation through a lysosomal pathway, whereas WNK1 stimulates BK activity by suppressing the ERK 1/2 signaling pathway."
32714200
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"WNK4 has been shown to significantly inhibit Maxi-K channel (BK) activity and expression in a kinase-dependent manner."
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"This study indicated that WNK4 inhibits BK channel activity partly by degradation of the channel protein through an ubiquitin dependent pathway."
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"WNK4 reduces plasma membrane renal outer medullary potassium channel (ROMK) and maxi-K channel (BK) abundance and these inhibitory effects are markedly increased by mutant WNK4 [34,53]."
31795491
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"These findings suggest that WNK4 WT inhibits Maxi K activity by reducing Maxi K protein at the membrane, but that the inhibition is not due to an increase in clathrin mediated endocytosis of Maxi K, but likely due to enhancing its lysosomal degradation."
21613417