scholarly journals Calmodulin regulation (calmodulation) of voltage-gated calcium channels

2014 ◽  
Vol 143 (6) ◽  
pp. 679-692 ◽  
Author(s):  
Manu Ben-Johny ◽  
David T. Yue
Keyword(s):  
Ion Channel ◽  
Molecular Basis ◽  
Ion Channel Regulation ◽  
Therapeutic Implications ◽  
Voltage Gated ◽  
Channel Regulation ◽  
Voltage Gated Calcium Channels ◽  
The Family ◽  
Biological Insight ◽  
Recent Developments

Calmodulin regulation (calmodulation) of the family of voltage-gated CaV1-2 channels comprises a prominent prototype for ion channel regulation, remarkable for its powerful Ca2+ sensing capabilities, deep in elegant mechanistic lessons, and rich in biological and therapeutic implications. This field thereby resides squarely at the epicenter of Ca2+ signaling biology, ion channel biophysics, and therapeutic advance. This review summarizes the historical development of ideas in this field, the scope and richly patterned organization of Ca2+ feedback behaviors encompassed by this system, and the long-standing challenges and recent developments in discerning a molecular basis for calmodulation. We conclude by highlighting the considerable synergy between mechanism, biological insight, and promising therapeutics.

Mechanisms of voltage-gated ion channel regulation: from gene expression to localization

2008 ◽  
Vol 65 (14) ◽  
pp. 2215-2231 ◽  
Author(s):  
D. J. Schulz ◽  
S. Temporal ◽  
D. M. Barry ◽  
M. L. Garcia
Keyword(s):  
Gene Expression ◽  
Ion Channel ◽  
Ion Channel Regulation ◽  
Voltage Gated ◽  
Channel Regulation

scholarly journals Presynaptic Paraneoplastic Disorders of the Neuromuscular Junction: An Update

2021 ◽  
Vol 11 (8) ◽  
pp. 1035
Author(s):  
Maria Pia Giannoccaro ◽  
Patrizia Avoni ◽  
Rocco Liguori
Keyword(s):  
Potassium Channels ◽  
Neuromuscular Junction ◽  
Calcium Channels ◽  
Myasthenia Gravis ◽  
Neuromuscular Transmission ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
Immune Mediated ◽  
Recent Developments ◽  
Myasthenic Syndrome

The neuromuscular junction (NMJ) is the target of a variety of immune-mediated disorders, usually classified as presynaptic and postsynaptic, according to the site of the antigenic target and consequently of the neuromuscular transmission alteration. Although less common than the classical autoimmune postsynaptic myasthenia gravis, presynaptic disorders are important to recognize due to the frequent association with cancer. Lambert Eaton myasthenic syndrome is due to a presynaptic failure to release acetylcholine, caused by antibodies to the presynaptic voltage-gated calcium channels. Acquired neuromyotonia is a condition characterized by nerve hyperexcitability often due to the presence of antibodies against proteins associated with voltage-gated potassium channels. This review will focus on the recent developments in the autoimmune presynaptic disorders of the NMJ.

scholarly journals Assessing the Impact of Calmodulinopathic Mutations on Neuronal Ion Channel Regulation

2021 ◽  
Vol 120 (3) ◽  
pp. 155a
Author(s):  
John W. Hussey ◽  
Emily DeMarco ◽  
Deborah DiSilvestre ◽  
Helene H. Jensen ◽  
Mette Nyegaard ◽  
...  
Keyword(s):  
Ion Channel ◽  
Ion Channel Regulation ◽  
Channel Regulation ◽  
The Impact

Ion channel regulation by G proteins

1995 ◽  
Vol 75 (4) ◽  
pp. 865-885 ◽  
Author(s):  
K. Wickman ◽  
D. E. Clapham
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
G Protein ◽  
G Proteins ◽  
Second Messengers ◽  
Channel Activity ◽  
Ion Channel Regulation ◽  
Protein Subunits ◽  
Channel Regulation ◽  
Intracellular Cascades

Ion channels are poised uniquely to initiate, mediate, or regulate such distinct cellular activities as action potential propagation, secretion, and gene transcription. In retrospect, it is not surprising that studies of ion channels have revealed considerable diversities in their primary structures, regulation, and expression. From a functional standpoint, the various mechanisms coopted by cells to regulate channel activity are particularly fascinating. Extracellular ligands, membrane potential, phosphorylation, ions themselves, and diffusible second messengers are all well-established regulators of ion channel activity. Heterotrimeric GTP-binding proteins (G proteins) mediate many of these types of ion channel regulation by stimulating or inhibiting phosphorylation pathways, initiating intracellular cascades leading to elevation of cytosolic Ca2+ or adenosine 3',5'-cyclic monophosphate levels, or by generating various lipid-derived compounds. In some cases, it seems that activated G protein subunits can interact directly with ion channels to elicit regulation. Although there is currently little direct biochemical evidence to support such a mechanism, it is the working hypothesis for the most-studied G protein-regulated ion channels.

scholarly journals Supramolecular Assemblies and Localized Regulation of Voltage-Gated Ion Channels

2009 ◽  
Vol 89 (2) ◽  
pp. 411-452 ◽  
Author(s):  
Shuiping Dai ◽  
Duane D. Hall ◽  
Johannes W. Hell
Keyword(s):  
Ion Channels ◽  
Glutamate Receptors ◽  
Ryanodine Receptor ◽  
Ion Channel Regulation ◽  
Voltage Gated ◽  
Signaling Complex ◽  
Channel Regulation ◽  
Fight Or Flight Response ◽  
Voltage Gated Ion Channels ◽  
Gated Ion Channels

This review addresses the localized regulation of voltage-gated ion channels by phosphorylation. Comprehensive data on channel regulation by associated protein kinases, phosphatases, and related regulatory proteins are mainly available for voltage-gated Ca2+ channels, which form the main focus of this review. Other voltage-gated ion channels and especially Kv7.1-3 (KCNQ1-3), the large- and small-conductance Ca2+-activated K+ channels BK and SK2, and the inward-rectifying K+ channels Kir3 have also been studied to quite some extent and will be included. Regulation of the L-type Ca2+ channel Cav1.2 by PKA has been studied most thoroughly as it underlies the cardiac fight-or-flight response. A prototypical Cav1.2 signaling complex containing the β2 adrenergic receptor, the heterotrimeric G protein Gs, adenylyl cyclase, and PKA has been identified that supports highly localized via cAMP. The type 2 ryanodine receptor as well as AMPA- and NMDA-type glutamate receptors are in close proximity to Cav1.2 in cardiomyocytes and neurons, respectively, yet independently anchor PKA, CaMKII, and the serine/threonine phosphatases PP1, PP2A, and PP2B, as is discussed in detail. Descriptions of the structural and functional aspects of the interactions of PKA, PKC, CaMKII, Src, and various phosphatases with Cav1.2 will include comparisons with analogous interactions with other channels such as the ryanodine receptor or ionotropic glutamate receptors. Regulation of Na+ and K+ channel phosphorylation complexes will be discussed in separate papers. This review is thus intended for readers interested in ion channel regulation or in localization of kinases, phosphatases, and their upstream regulators.

scholarly journals Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation

2005 ◽  
Vol 24 (4) ◽  
pp. 705-716 ◽  
Author(s):  
Michael Köttgen ◽  
Thomas Benzing ◽  
Thomas Simmen ◽  
Robert Tauber ◽  
Björn Buchholz ◽  
...  
Keyword(s):  
Ion Channel ◽  
Ion Channel Regulation ◽  
Channel Regulation

Regulation of ion transport by oxidants

2013 ◽  
Vol 305 (9) ◽  
pp. L595-L603 ◽  
Author(s):  
Charles A. Downs ◽  
My N. Helms
Keyword(s):  
Oxidative Stress ◽  
Ion Channels ◽  
Ion Channel ◽  
Redox Regulation ◽  
Experimental Biology ◽  
Cellular Functions ◽  
Ion Channel Regulation ◽  
Channel Regulation ◽  
Made In

Ion channels perform a variety of cellular functions in lung epithelia. Oxidant- and antioxidant-mediated mechanisms (that is, redox regulation) of ion channels are areas of intense research. Significant progress has been made in our understanding of redox regulation of ion channels since the last Experimental Biology report in 2003. Advancements include: 1) identification of nonphagocytic NADPH oxidases as sources of regulated reactive species (RS) production in epithelia, 2) an understanding that excessive treatment with antioxidants can result in greater oxidative stress, and 3) characterization of novel RS signaling pathways that converge upon ion channel regulation. These advancements, as discussed at the 2013 Experimental Biology Meeting in Boston, MA, impact our understanding of oxidative stress in the lung, and, in particular, illustrate that the redox state has profound effects on ion channel and cellular function.

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