scholarly journals Interactions of disulfide-deficient selenocysteine analogs of μ-conotoxin BuIIIB with the α-subunit of the voltage-gated sodium channel subtype 1.3

FEBS Journal ◽  
2014 ◽  
Vol 281 (13) ◽  
pp. 2885-2898 ◽  
Author(s):  
Brad R. Green ◽  
Min-Min Zhang ◽  
Sandeep Chhabra ◽  
Samuel D. Robinson ◽  
Michael J. Wilson ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated

scholarly journals The voltage-gated sodium channel β2 subunit associates with lipid rafts by S-palmitoylation

2021 ◽  
Vol 134 (6) ◽  
Author(s):  
Eric Cortada ◽  
Robert Serradesanferm ◽  
Ramon Brugada ◽  
Marcel Verges
Keyword(s):  
Sodium Channel ◽  
Lipid Rafts ◽  
Lipid Raft ◽  
Cholesterol Depletion ◽  
Slight Reduction ◽  
Apical Surface ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated ◽  
Partial Overlap

ABSTRACT The voltage-gated sodium channel is critical for cardiomyocyte function. It consists of a protein complex comprising a pore-forming α subunit and associated β subunits. In polarized Madin–Darby canine kidney cells, we show evidence by acyl-biotin exchange that β2 is S-acylated at Cys-182. Interestingly, we found that palmitoylation increases β2 association with detergent-resistant membranes. β2 localizes exclusively to the apical surface. However, depletion of plasma membrane cholesterol, or blocking intracellular cholesterol transport, caused mislocalization of β2, as well as of the non-palmitoylable C182S mutant, to the basolateral domain. Apical β2 did not undergo endocytosis and displayed limited diffusion within the plane of the membrane; such behavior suggests that, at least in part, it is cytoskeleton anchored. Upon acute cholesterol depletion, its mobility was greatly reduced, and a slight reduction was also measured as a result of lack of palmitoylation, supporting β2 association with cholesterol-rich lipid rafts. Indeed, lipid raft labeling confirmed a partial overlap with apical β2. Although β2 palmitoylation was not required to promote surface localization of the α subunit, our data suggest that it is likely implicated in lipid raft association and the polarized localization of β2.

scholarly journals Autosomal Dominant Erythermalgia Associated With a Novel Mutation in the Voltage-Gated Sodium Channel α Subunit Nav1.7

2005 ◽  
Vol 62 (10) ◽  
Author(s):  
Jan J. Michiels ◽  
Rene H. M. te Morsche ◽  
Jan B. M. J. Jansen ◽  
Joost P. H. Drenth
Keyword(s):  
Sodium Channel ◽  
Autosomal Dominant ◽  
Novel Mutation ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated

scholarly journals Trafficking and Function of the Voltage-Gated Sodium Channel β2 Subunit

Biomolecules ◽  
2019 ◽  
Vol 9 (10) ◽  
pp. 604 ◽  
Author(s):  
Eric Cortada ◽  
Ramon Brugada ◽  
Marcel Verges
Keyword(s):  
Sodium Channel ◽  
Electrical Coupling ◽  
Surface Expression ◽  
Current Data ◽  
Cell Surface Expression ◽  
Gene Encoding ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated

The voltage-gated sodium channel is vital for cardiomyocyte function, and consists of a protein complex containing a pore-forming α subunit and two associated β subunits. A fundamental, yet unsolved, question is to define the precise function of β subunits. While their location in vivo remains unclear, large evidence shows that they regulate localization of α and the biophysical properties of the channel. The current data support that one of these subunits, β2, promotes cell surface expression of α. The main α isoform in an adult heart is NaV1.5, and mutations in SCN5A, the gene encoding NaV1.5, often lead to hereditary arrhythmias and sudden death. The association of β2 with cardiac arrhythmias has also been described, which could be due to alterations in trafficking, anchoring, and localization of NaV1.5 at the cardiomyocyte surface. Here, we will discuss research dealing with mechanisms that regulate β2 trafficking, and how β2 could be pivotal for the correct localization of NaV1.5, which influences cellular excitability and electrical coupling of the heart. Moreover, β2 may have yet to be discovered roles on cell adhesion and signaling, implying that diverse defects leading to human disease may arise due to β2 mutations.

scholarly journals Embryonic and larval expression of zebrafish voltage-gated sodium channel α-subunit genes

2006 ◽  
Vol 235 (7) ◽  
pp. 1962-1973 ◽  
Author(s):  
Alicia E. Novak ◽  
Alison D. Taylor ◽  
Ricardo H. Pineda ◽  
Erika L. Lasda ◽  
Melissa A. Wright ◽  
...  
Keyword(s):  
Sodium Channel ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Voltage Gated

scholarly journals Differential Sialylation Modulates Voltage-gated Na+ Channel Gating throughout the Developing Myocardium

2006 ◽  
Vol 127 (3) ◽  
pp. 253-265 ◽  
Author(s):  
Patrick J. Stocker ◽  
Eric S. Bennett
Keyword(s):  
Sialic Acid ◽  
Sodium Channel ◽  
Channel Gating ◽  
Sialic Acids ◽  
Na Channel ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Rat Cardiomyocytes ◽  
Voltage Gated ◽  
Α Subunits

Voltage-gated sodium channel function from neonatal and adult rat cardiomyocytes was measured and compared. Channels from neonatal ventricles required an ∼10 mV greater depolarization for voltage-dependent gating events than did channels from neonatal atria and adult atria and ventricles. We questioned whether such gating shifts were due to developmental and/or chamber-dependent changes in channel-associated functional sialic acids. Thus, all gating characteristics for channels from neonatal atria and adult atria and ventricles shifted significantly to more depolarized potentials after removal of surface sialic acids. Desialylation of channels from neonatal ventricles did not affect channel gating. After removal of the complete surface N-glycosylation structures, gating of channels from neonatal atria and adult atria and ventricles shifted to depolarized potentials nearly identical to those measured for channels from neonatal ventricles. Gating of channels from neonatal ventricles were unaffected by such deglycosylation. Immunoblot gel shift analyses indicated that voltage-gated sodium channel α subunits from neonatal atria and adult atria and ventricles are more heavily sialylated than α subunits from neonatal ventricles. The data are consistent with approximately 15 more sialic acid residues attached to each α subunit from neonatal atria and adult atria and ventricles. The data indicate that differential sialylation of myocyte voltage-gated sodium channel α subunits is responsible for much of the developmental and chamber-specific remodeling of channel gating observed here. Further, cardiac excitability is likely impacted by these sialic acid–dependent gating effects, such as modulation of the rate of recovery from inactivation. A novel mechanism is described by which cardiac voltage-gated sodium channel gating and subsequently cardiac rhythms are modulated by changes in channel-associated sialic acids.

Use of Surface Plasmon Resonance Coupled with Mass Spectrometry Reveals an Interaction between the Voltage-Gated Sodium Channel Type X α-Subunit and Caveolin-1

2008 ◽  
Vol 7 (12) ◽  
pp. 5333-5338 ◽  
Author(s):  
Elisabet Öhman ◽  
Anna Nilsson ◽  
Alexandra Madeira ◽  
Benita Sjögren ◽  
Per E. Andrén ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Surface Plasmon Resonance ◽  
Sodium Channel ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Voltage Gated Sodium Channel ◽  
Α Subunit ◽  
Caveolin 1 ◽  
Voltage Gated ◽  
Channel Type
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