Cargando…

Interactions between β-Catenin and the HSlo Potassium Channel Regulates HSlo Surface Expression

BACKGROUND: The large conductance calcium-activated potassium channel alpha-subunit (Slo) is widely distributed throughout the body and plays an important role in a number of diseases. Prior work has shown that Slo, through its S10 region, interacts with β-catenin, a key component of the cytoskeleto...

Descripción completa

Detalles Bibliográficos
Autores principales:	Bian, Shumin, Bai, Jun-Ping, Chapin, Hannah, Le Moellic, Cathy, Dong, Huiping, Caplan, Michael, Sigworth, Fred J., Navaratnam, Dhasakumar S.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2011
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3237428/ https://www.ncbi.nlm.nih.gov/pubmed/22194818 http://dx.doi.org/10.1371/journal.pone.0028264

Ejemplares similares

Intracellular calcium-dependent regulation of the sperm-specific calcium-activated potassium channel, hSlo3, by the BK(Ca) activator LDD175
por: Wijerathne, Tharaka Darshana, et al.
Publicado: (2017)

Interaction of internal Ba2+ with a cloned Ca(2+)-dependent K+ (hslo) channel from smooth muscle
Publicado: (1996)

The complete chloroplast genome of Arcangelisia gusanlung H.S.Lo (Menispermaceae), an important traditional medicine from South China
por: Wen, Guihua, et al.
Publicado: (2021)

HslO ameliorates arrested ΔrecA polA cell growth and reduces DNA damage and oxidative stress responses
por: Kaidow, A., et al.
Publicado: (2022)

Ability of naringenin, a bioflavonoid, to activate M-type potassium current in motor neuron-like cells and to increase BK(Ca)-channel activity in HEK293T cells transfected with α-hSlo subunit
por: Hsu, Hung-Te, et al.
Publicado: (2014)

Vitamin C Maintenance against Cell Growth Arrest and Reactive Oxygen Species Accumulation in the Presence of Redox Molecular Chaperone hslO Gene
por: Kaidow, Akihiro, et al.
Publicado: (2022)

Fragile X mental retardation protein controls gating of the sodium-activated potassium channel Slack
por: Brown, Maile R., et al.
Publicado: (2010)

Current carried by the Slc26 family member prestin does not flow through the transporter pathway
por: Bai, Jun-Ping, et al.
Publicado: (2017)

Single-Channel Properties of I(Ks) Potassium Channels
por: Yang, Youshan, et al.
Publicado: (1998)

Cryo-EM structures of Kv1.2 potassium channels, conducting and non-conducting
por: Wu, Yangyu, et al.
Publicado: (2023)

Real Time Measures of Prestin Charge and Fluorescence during Plasma Membrane Trafficking Reveal Sub-Tetrameric Activity
por: Bian, Shumin, et al.
Publicado: (2013)

Electrostatics and the Gating Pore of Shaker Potassium Channels
por: Islas, Leon D., et al.
Publicado: (2001)

Intermediate Conductances during Deactivation of Heteromultimeric Shaker Potassium Channels
por: Zheng, Jie, et al.
Publicado: (1998)

Selectivity Changes during Activation of Mutant Shaker Potassium Channels
por: Zheng, Jie, et al.
Publicado: (1997)

Can Shaker Potassium Channels be Locked in the Deactivated State?
por: Yang, Youshan, et al.
Publicado: (2004)

Cryo-EM structure of the BK potassium channel in a lipid membrane
por: Wang, Liguo, et al.
Publicado: (2009)

Voltage Sensitivity and Gating Charge in Shaker and Shab Family Potassium Channels
por: Islas, Leon D., et al.
Publicado: (1999)

Role of the S3-S4 Linker in Shaker Potassium Channel Activation
por: Mathur, Rajesh, et al.
Publicado: (1997)

How Does the W434F Mutation Block Current in Shaker Potassium Channels?
por: Yang, Youshan, et al.
Publicado: (1997)

Hidden Markov Model Analysis of Intermediate Gating Steps Associated with the Pore Gate of Shaker Potassium Channels
por: Zheng, Jie, et al.
Publicado: (2001)

Activation of Shaker Potassium Channels : II. Kinetics of the V2 Mutant Channel
por: Schoppa, N.E., et al.
Publicado: (1998)

Activation of Shaker Potassium Channels : I. Characterization of Voltage-dependent Transitions
por: Schoppa, N.E., et al.
Publicado: (1998)

Activation of Shaker Potassium Channels : III. An Activation Gating Model for Wild-Type and V2 Mutant Channels
por: Schoppa, N.E., et al.
Publicado: (1998)

Calcium‐induced calcium release in proximity to hair cell BK channels revealed by PKA activation
por: Bai, Jun‐ping, et al.
Publicado: (2020)

Author Correction: Prestin kinetics and corresponding frequency dependence augment during early development of the outer hair cell within the mouse organ of Corti
por: Bai, Jun-Ping, et al.
Publicado: (2020)

Prestin kinetics and corresponding frequency dependence augment during early development of the outer hair cell within the mouse organ of Corti
por: Bai, Jun-Ping, et al.
Publicado: (2019)

A Genetically-Encoded YFP Sensor with Enhanced Chloride Sensitivity, Photostability and Reduced pH Interference Demonstrates Augmented Transmembrane Chloride Movement by Gerbil Prestin (SLC26a5)
por: Zhong, Sheng, et al.
Publicado: (2014)

State dependent effects on the frequency response of prestin’s real and imaginary components of nonlinear capacitance
por: Santos-Sacchi, Joseph, et al.
Publicado: (2021)

Potassium channel activity controls breast cancer metastasis by affecting β-catenin signaling
por: Breuer, Eun-Kyoung, et al.
Publicado: (2019)

Polycystin-1 Surface Localization Is Stimulated by Polycystin-2 and Cleavage at the G Protein-coupled Receptor Proteolytic Site
por: Chapin, Hannah C., et al.
Publicado: (2010)

Tyrosine motifs are required for prestin basolateral membrane targeting
por: Zhang, Yifan, et al.
Publicado: (2015)

Generation of Functional Fluorescent BK Channels by Random Insertion of GFP Variants
por: Giraldez, Teresa, et al.
Publicado: (2005)

Single particle cryo-EM structure of the outer hair cell motor protein prestin
por: Butan, Carmen, et al.
Publicado: (2022)

Gating of Acid-sensitive Ion Channel-1: Release of Ca(2+) Block vs. Allosteric Mechanism
por: Zhang, Ping, et al.
Publicado: (2006)

Structure and analysis of nanobody binding to the human ASIC1a ion channel
por: Wu, Yangyu, et al.
Publicado: (2021)

When Is a Potassium Channel Not a Potassium Channel?
por: Accili, Eric
Publicado: (2022)

Kcsa: It's a Potassium Channel
por: LeMasurier, Meredith, et al.
Publicado: (2001)

The cell biology of polycystic kidney disease
por: Chapin, Hannah C., et al.
Publicado: (2010)

Seeing the long tail: A novel green fluorescent protein, SiriusGFP, for ultra long timelapse imaging
por: Zhong, Sheng, et al.
Publicado: (2019)

ESCRT regulates surface expression of the Kir2.1 potassium channel
por: Kolb, Alexander R., et al.
Publicado: (2014)

Cannot write session to /tmp/vufind_sessions/sess_fbfuhu86kt7p4mnjjvagl7bgtq