2013
DOI: 10.3389/fncel.2013.00137
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β1- and β3- voltage-gated sodium channel subunits modulate cell surface expression and glycosylation of Nav1.7 in HEK293 cells

Abstract: Voltage-gated sodium channels (Navs) are glycoproteins composed of a pore-forming α-subunit and associated β-subunits that regulate Nav α-subunit plasma membrane density and biophysical properties. Glycosylation of the Nav α-subunit also directly affects Navs gating. β-subunits and glycosylation thus comodulate Nav α-subunit gating. We hypothesized that β-subunits could directly influence α-subunit glycosylation. Whole-cell patch clamp of HEK293 cells revealed that both β1- and β3-subunits coexpression shifted… Show more

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Cited by 61 publications
(55 citation statements)
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“…It should be noted that coexpression versus association of α-and β-subunits per se are not synonymous; thus, for example, Na V β1 coexpression can affect the glycosylation of the α-subunit (27), and the glycosylation state of the α-subunit, rather than its physical association with a β-subunit, could be responsible for the altered pharmacology of the VGSC.…”
Section: Discussionmentioning
confidence: 99%
“…It should be noted that coexpression versus association of α-and β-subunits per se are not synonymous; thus, for example, Na V β1 coexpression can affect the glycosylation of the α-subunit (27), and the glycosylation state of the α-subunit, rather than its physical association with a β-subunit, could be responsible for the altered pharmacology of the VGSC.…”
Section: Discussionmentioning
confidence: 99%
“…19 The exact pathways leading to the dysregulation of NaV1.7 are poorly understood but likely involve mechanisms related to its surface trafficking and regulation via protein–protein interactions. 18,2022 Recent studies have identified neuronal CRMP2 as a novel binding partner of NaV1.7. 21,22 Specifically, a selective reduction in NaV1.7 surface expression and current density was observed in rodent and human sensory neurons expressing a mutant CRMP2 lacking the SUMO PTM site (lysine 374) in CRMP2.…”
mentioning
confidence: 99%
“…The acceleration of inactivation and the recovery from inactivation of the Na + channel is likely due to increased β3 subunit expression, although steady-state activation and inactivation of this channel were not changed in FoxO1 -/- [31]. β3 regulating Na V 1.5 may have similar mechanisms by which β3 increases both expression of the core-glycosylated form of Na V 1.7 and Na + channel activity [33]. …”
Section: Discussionmentioning
confidence: 99%