2013
DOI: 10.1074/jbc.m112.396408
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Filamin Interacts with Epithelial Sodium Channel and Inhibits Its Channel Function

Abstract: Background: ENaC is critical in Na ϩ homeostasis and blood pressure, but how it is regulated by the cytoskeleton remains

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Cited by 22 publications
(12 citation statements)
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“…Biotinylation-Biotinylation and Western blot analyses were carried out to measure the protein expression level of each isoform based upon a previously published protocol (19) with modification. Oocytes were washed three times with phosphate buffer saline (PBS), pH 8.0; then they were incubated in 2 mM Sulfo-NHS-LC-Biotin (Pierce) at room temperature for 30 min.…”
Section: Methodsmentioning
confidence: 99%
“…Biotinylation-Biotinylation and Western blot analyses were carried out to measure the protein expression level of each isoform based upon a previously published protocol (19) with modification. Oocytes were washed three times with phosphate buffer saline (PBS), pH 8.0; then they were incubated in 2 mM Sulfo-NHS-LC-Biotin (Pierce) at room temperature for 30 min.…”
Section: Methodsmentioning
confidence: 99%
“…Future studies should be performed to investigate whether Per1 indirectly regulates ENaC protein expression and activity at the apical plasma membrane by regulating chaperone proteins involved in its insertion into the membrane and effector proteins involved in its degradation and recycling back to the membrane. Moreover, studies should be performed to determine whether Per1 regulates actin cytoskeleton proteins such as myristoylated alaninerich protein kinase C substrate and filamin, which have been shown to play an essential role in stabilizing ENaC at the membrane (1,2,19,31).…”
Section: Direct Inhibition Of Per1 Reduces Enac Activitymentioning
confidence: 99%
“…However, it has been speculated that some cytoplasmic factors might inhibit ENaCs when the channels are resident in the intact basolateral cell membrane; these factors would be lost when switching to outside-out patches, thereby producing channel activation. Recent findings suggest that filamin, a cytoplasmic protein that binds actin in the cytoskeleton, inhibits ENaC activity [89]. It is tempting to speculate that during patch excision, the cytoskeleton layer under the cell membrane gets disrupted and this may remove a stationary inhibitory effect exerted by intracellular protein filaments on ENaCs.…”
Section: Excised Membrane Patchesmentioning
confidence: 99%