Cellular and subcellular distribution of Kv4/K+ channel-interacting proteins (KChIP) in the hippocampus

2018 ◽  
Author(s):  
Rocio Alfaro ◽  
Carolina Aguado ◽  
Alejandro Martin
Keyword(s):  
Subcellular Distribution ◽  
K Channel ◽  
Interacting Proteins

scholarly journals Emerging crosstalk between two signaling pathways coordinates K+ and Na+ homeostasis in the halophyte Hordeum brevisubulatum

2020 ◽  
Vol 71 (14) ◽  
pp. 4345-4358
Author(s):  
Haiwen Zhang ◽  
Hao Feng ◽  
Junwen Zhang ◽  
Rongchao Ge ◽  
Liyuan Zhang ◽  
...  
Keyword(s):  
Signaling Pathways ◽  
Regulatory Mechanisms ◽  
K Channel ◽  
Interacting Proteins ◽  
The Novel ◽  
Voltage Gated ◽  
Primary Core ◽  
High Salt Stress ◽  
Hordeum Brevisubulatum

Abstract K+/Na+ homeostasis is the primary core response for plant to tolerate salinity. Halophytes have evolved novel regulatory mechanisms to maintain a suitable K+/Na+ ratio during long-term adaptation. The wild halophyte Hordeum brevisubulatum can adopt efficient strategies to achieve synergistic levels of K+ and Na+ under high salt stress. However, little is known about its molecular mechanism. Our previous study indicated that HbCIPK2 contributed to prevention of Na+ accumulation and K+ reduction. Here, we further identified the HbCIPK2-interacting proteins including upstream Ca2+ sensors, HbCBL1, HbCBL4, and HbCBL10, and downstream phosphorylated targets, the voltage-gated K+ channel HbVGKC1 and SOS1-like transporter HbSOS1L. HbCBL1 combined with HbCIPK2 could activate HbVGKC1 to absorb K+, while the HbCBL4/10–HbCIPK2 complex modulated HbSOS1L to exclude Na+. This discovery suggested that crosstalk between the sodium response and the potassium uptake signaling pathways indeed exists for HbCIPK2 as the signal hub, and paved the way for understanding the novel mechanism of K+/Na+ homeostasis which has evolved in the halophytic grass.

scholarly journals Specific effects of KChIP3/calsenilin/DREAM, but not KChIPs 1, 2 and 4, on calcium signalling and regulated secretion in PC12 cells

2008 ◽  
Vol 413 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Neil Venn ◽  
Lee P. Haynes ◽  
Robert D. Burgoyne
Keyword(s):  
Pc12 Cells ◽  
Purinergic Receptors ◽  
Regulatory Element ◽  
Calcium Signalling ◽  
K Channel ◽  
Interacting Proteins ◽  
Regulated Secretion ◽  
Specific Effects ◽  
Cellular Context ◽  
Neuronal Calcium Sensor Protein

The KChIPs (K+ channel-interacting proteins) are members of the NCS (neuronal calcium sensor) protein family of Ca2+-binding proteins. It is unclear to what extent the KChIPs have distinct functions although they all interact with Kv4 K+ channels. KChIP3 has also been shown to repress transcription of specific genes via binding to DRE (downstream regulatory element) motifs and all KChIPs may share this function. In the present study, we have compared the function of isoforms of the four KChIPs. KChIPs 1–4 were found to stimulate the traffic of Kv4.2 channels to the plasma membrane. KChIP3 expression in PC12 cells resulted in an increase in exocytosis evoked by activation of purinergic receptors. In contrast, KChIPs 1, 2 and 4, although expressed to the same extent, had no effect on secretion. In addition, KChIP3 but not KChIPs 1, 2 and 4 modified the ATP-induced Ca2+ signal resulting in a delay in recovery after the peak Ca2+ elevation and also specifically resulted in down-regulation of the Na+/Ca2+ exchanger NCX3, which could explain the effects on the Ca2+ signal and secretion. Regulation of NCX3 by KChIP3 has been shown to occur via its DREAM (DRE antagonist modulator) function [Gomez-Villafuertes, Torres, Barrio, Savignac, Gabellini, Rizzato, Pintado, Gutierrez-Adan, Mellstrom, Carafoli and Naranjo (2005) J. Neurosci. 25, 10822–10830] suggesting that this activity might depend on the cellular context of expression of the various KChIPs. These results reveal a new role for KChIP3 in the regulation of Ca2+-regulated secretion and also suggest that the functions of each of the KChIPs may be more specialized than previously appreciated.

Regulation of the human ether-a-go-go-related gene (hERG) potassium channel by Nedd4 family interacting proteins (Ndfips)

2015 ◽  
Vol 472 (1) ◽  
pp. 71-82 ◽  
Author(s):  
Yudi Kang ◽  
Jun Guo ◽  
Tonghua Yang ◽  
Wentao Li ◽  
Shetuan Zhang
Keyword(s):  
Potassium Channel ◽  
Precursor Cell ◽  
K Channel ◽  
Neural Precursor ◽  
Cardiac Repolarization ◽  
Interacting Proteins ◽  
Neural Precursor Cell ◽  
Related Gene ◽  
Cellular Compartments ◽  
Herg Channels

The human ether-a-go-go-related gene (hERG)-encoded K+ channel is critical for cardiac repolarization. In the present study, we demonstrate that the E3 ubiquitin (Ub) ligase neural precursor cell expressed developmentally down-regulated protein 4-2 (Nedd4-2) is directed to specific cellular compartments by Nedd4 family-interacting proteins (Ndfips) to selectively target the mature hERG channels for degradation.

scholarly journals Voltage-gated Ca2+ and K+ channel coupling regulates CA1 hippocampal synaptic filtering and spine excitability

2020 ◽  
Author(s):  
Jonathan G. Murphy ◽  
Jakob J. Gutzmann ◽  
Lin Lin ◽  
Jiahua Hu ◽  
Ronald S. Petralia ◽  
...  
Keyword(s):  
Hippocampal Neurons ◽  
Pyramidal Neurons ◽  
Surface Expression ◽  
K Channel ◽  
Interacting Proteins ◽  
Channel Coupling ◽  
Whole Cell ◽  
Hippocampal Pyramidal Neurons ◽  
Voltage Gated ◽  
Cell Current

ABSTRACTThe transient voltage-gated K+ current (IA) mediated by Kv4.2 in CA1 hippocampal pyramidal neurons regulates dendritic excitability, synaptic plasticity, and learning. Here we report that Ca2+ entry mediated by the voltage-gated Ca2+ channel subunit Cav2.3 regulates Kv4.2 function in CA1 pyramidal neurons through Ca2+ binding auxiliary subunits known as K+ channel interacting proteins (KChIPs). We characterized an interaction between Cav2.3 and Kv4.2 using immunofluorescence colocalization, coimmunoprecipitation, electron microscopy, FRAP, and FRET. We found that Ca2+-entry via Cav2.3 increases Kv4.2-mediated whole-cell current due in part to an increase in Kv4.2 surface expression. In hippocampal neurons, pharmacological block of Cav2.3 reduced whole-cell IA. We also found reduced IA in Cav2.3 knockout mouse neurons with a loss of the dendritic IA gradient. Furthermore, the Cav2.3-Kv4.2 complex was found to regulate the size of synaptic currents and spine Ca2+ transients. These results reveal an intermolecular Cav2.3-Kv4.2 complex impacting synaptic integration in CA1 hippocampal neurons.

Differences in Subcellular Distribution of Catechol-O-Methyltransferase and Tyrosinase in Malignant Melanoma

1993 ◽  
Vol 100 ◽  
pp. 222S-225S ◽  
Author(s):  
Takakazu Shibata ◽  
Stan Pavel ◽  
Nico P M Smit ◽  
Yutaka Mishima
Keyword(s):  
Malignant Melanoma ◽  
Subcellular Distribution

Molecular analysis of a mutation in the S5-H5 linker of the KCNQ2 K+ channel causing neonatal convulsions

2006 ◽  
Vol 33 (S 1) ◽  
Author(s):  
G. Naros ◽  
O. Yalcin ◽  
S. Maljevic ◽  
T.V. Wuttke ◽  
A. Dervent ◽  
...  
Keyword(s):  
Molecular Analysis ◽  
K Channel ◽  
Neonatal Convulsions
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