scholarly journals N-linked glycosylation of Kv1.2 voltage-gated potassium channel facilitates cell surface expression and enhances the stability of internalized channels

2016 ◽  
Vol 594 (22) ◽  
pp. 6701-6713 ◽  
Author(s):  
Desiree A. Thayer ◽  
Shi-Bing Yang ◽  
Yuh Nung Jan ◽  
Lily Y. Jan
Keyword(s):  
Cell Surface ◽  
Potassium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Voltage Gated ◽  
The Stability

Glycosylation and Cell Surface Expression of Kv1.2 Potassium Channel are Regulated by Determinants in the Pore Region

2006 ◽  
Vol 31 (5) ◽  
pp. 589-596 ◽  
Author(s):  
Tetsuhiro Fujita ◽  
Iku Utsunomiya ◽  
Jin Ren ◽  
Yousuke Matsushita ◽  
Miwa Kawai ◽  
...  
Keyword(s):  
Cell Surface ◽  
Potassium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Pore Region

Identification of amino acids in the pore region of Kv1.2 potassium channel that regulate its glycosylation and cell surface expression

2010 ◽  
Vol 112 (4) ◽  
pp. 913-923 ◽  
Author(s):  
Iku Utsunomiya ◽  
Shinya Tanabe ◽  
Tomonori Terashi ◽  
Souichi Ikeno ◽  
Tadashi Miyatake ◽  
...  
Keyword(s):  
Amino Acids ◽  
Cell Surface ◽  
Potassium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Pore Region

scholarly journals Effect of Cell Cycle on Cell Surface Expression of Voltage-Gated Sodium Channels and Na+,K+-ATPase

2021 ◽  
Author(s):  
Samantha I. Edenfield ◽  
III Harry J. Gould ◽  
Dennis Paul
Keyword(s):  
Cell Cycle ◽  
Cell Surface ◽  
Sodium Channels ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Voltage Gated ◽  
Voltage Gated Sodium Channels ◽  
Dividing Cells ◽  
Immortalized Cell ◽  
Dapi Fluorescence

Abstract Voltage-gated sodium channels (VGSCs) are the target for many therapies. Variation in membrane potential occurs throughout the cell cycle, yet little attention has been devoted to VGSCs and Na+,K+-ATPase in the cell cycle. We hypothesized that in addition to doubling DNA and cell membrane in anticipation of cell division, there should be a doubling of VGSCs and Na+,K+-ATPase compared to non-dividing cells. We tested this hypothesis in eight immortalized cell lines by correlating immunocytofluorescent labeling of VGSCs or Na+,K+-ATPase, with propidium iodide or DAPI fluorescence using flow cytometry. Cell surface expression of VGSCs during phases S through M was double that seen during phases G0 - G1. By contrast, Na+,K+-ATPase expression increased only 1.5-fold. The increases were independent of baseline expression of channels or pumps. The variation in VGSC and Na+,K+-ATPase expression has implications for both our understanding of sodium's role in controlling the cell cycle and variability of treatments targeted at these components of the Na+ handling system.

Role of C-terminus of Kir7.1 potassium channel in cell-surface expression

2006 ◽  
Vol 30 (3) ◽  
pp. 270-277 ◽  
Author(s):  
Toru Tateno ◽  
Nobuhiro Nakamura ◽  
Yukio Hirata ◽  
Shigehisa Hirose
Keyword(s):  
Cell Surface ◽  
Potassium Channel ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
C Terminus

scholarly journals Translocatable voltage-gated Ca2+ channel β subunits in α1–β complexes reveal competitive replacement yet no spontaneous dissociation

2018 ◽  
Vol 115 (42) ◽  
pp. E9934-E9943 ◽  
Author(s):  
Jun-Hee Yeon ◽  
Cheon-Gyu Park ◽  
Bertil Hille ◽  
Byung-Chang Suh
Keyword(s):  
Plasma Membrane ◽  
Channel Gating ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Intracellular Loop ◽  
Drug Induced ◽  
Interaction Domain ◽  
Intact Cells ◽  
Voltage Gated ◽  
The Stability

β subunits of high voltage-gated Ca2+ (CaV) channels promote cell-surface expression of pore-forming α1 subunits and regulate channel gating through binding to the α-interaction domain (AID) in the first intracellular loop. We addressed the stability of CaV α1B–β interactions by rapamycin-translocatable CaV β subunits that allow drug-induced sequestration and uncoupling of the β subunit from CaV2.2 channel complexes in intact cells. Without CaV α1B/α2δ1, all modified β subunits, except membrane-tethered β2a and β2e, are in the cytosol and rapidly translocate upon rapamycin addition to anchors on target organelles: plasma membrane, mitochondria, or endoplasmic reticulum. In cells coexpressing CaV α1B/α2δ1 subunits, the translocatable β subunits colocalize at the plasma membrane with α1B and stay there after rapamycin application, indicating that interactions between α1B and bound β subunits are very stable. However, the interaction becomes dynamic when other competing β isoforms are coexpressed. Addition of rapamycin, then, switches channel gating and regulation by phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2] lipid. Thus, expression of free β isoforms around the channel reveals a dynamic aspect to the α1B–β interaction. On the other hand, translocatable β subunits with AID-binding site mutations are easily dissociated from CaV α1B on the addition of rapamycin, decreasing current amplitude and PI(4,5)P2 sensitivity. Furthermore, the mutations slow CaV2.2 current inactivation and shift the voltage dependence of activation to more positive potentials. Mutated translocatable β subunits work similarly in CaV2.3 channels. In sum, the strong interaction of CaV α1B–β subunits can be overcome by other free β isoforms, permitting dynamic changes in channel properties in intact cells.

Dynamitin affects cell-surface expression of voltage-gated sodium channel Nav1.5

2014 ◽  
Vol 463 (3) ◽  
pp. 339-349 ◽  
Author(s):  
Benoît Chatin ◽  
Pauline Colombier ◽  
Anne Laure Gamblin ◽  
Marie Allouis ◽  
Françoise Le Bouffant
Keyword(s):  
Cell Surface ◽  
Sodium Channel ◽  
Surface Density ◽  
Surface Expression ◽  
Cell Surface Expression ◽  
Voltage Gated ◽  
Channel Regulation ◽  
Voltage Dependent ◽  
Dynactin Complex ◽  
Partner Proteins

Nav1.5 voltage-dependent sodium channel regulation involves interactions with partner proteins. In the present paper we report Nav1.5 association with dynamitin, a member of the microtubule-associated dynactin complex whose disruption affects the channel cell-surface density.

Sign in / Sign up

Export Citation Format

Share Document