scholarly journals Hyperactivation of L-type voltage-gated Ca2+ channels in Caenorhabditis elegans striated muscle can result from point mutations in the IS6 or the IIIS4 segment of the  1 subunit

2014 ◽  
Vol 217 (21) ◽  
pp. 3805-3814 ◽  
Author(s):  
V. Laine ◽  
J. R. Segor ◽  
H. Zhan ◽  
J.-L. Bessereau ◽  
M. Jospin
Keyword(s):  
Caenorhabditis Elegans ◽  
Striated Muscle ◽  
Point Mutations ◽  
Voltage Gated ◽  
Ca2 Channels

scholarly journals A Region of the Myosin Rod Important for Interaction With Paramyosin in Caenorhabditis elegans Striated Muscle

Genetics ◽  
2000 ◽  
Vol 156 (2) ◽  
pp. 631-643
Author(s):  
Pamela E Hoppe ◽  
Robert H Waterston
Keyword(s):  
Caenorhabditis Elegans ◽  
Heavy Chain ◽  
Molecular Interaction ◽  
Striated Muscle ◽  
Genetic Interaction ◽  
Specific Interaction ◽  
Thick Filament ◽  
Parallel Arrangement ◽  
Myosin Rod

Abstract The precise arrangement of molecules within the thick filament, as well as the mechanisms by which this arrangement is specified, remains unclear. In this article, we have exploited a unique genetic interaction between one isoform of myosin heavy chain (MHC) and paramyosin in Caenorhabditis elegans to probe the molecular interaction between MHC and paramyosin in vivo. Using chimeric myosin constructs, we have defined a 322-residue region of the MHC A rod critical for suppression of the structural and motility defects associated with the unc-15(e73) allele. Chimeric constructs lacking this region of MHC A either fail to suppress, or act as dominant enhancers of, the e73 phenotype. Although the 322-residue region is required for suppression activity, our data suggest that sequences along the length of the rod also play a role in the isoform-specific interaction between MHC A and paramyosin. Our genetic and cell biological analyses of construct behavior suggest that the 322-residue region of MHC A is important for thick filament stability. We present a model in which this region mediates an avid interaction between MHC A and paramyosin in parallel arrangement in formation of the filament arms.

scholarly journals Role of a conserved glutamine in the function of voltage-gated Ca2+ channels revealed by a mutation in human CACNA1D

2018 ◽  
Vol 293 (37) ◽  
pp. 14444-14454 ◽  
Author(s):  
Edgar Garza-Lopez ◽  
Josue A. Lopez ◽  
Jussara Hagen ◽  
Ruth Sheffer ◽  
Vardiella Meiner ◽  
...  
Keyword(s):  
Voltage Gated ◽  
Ca2 Channels

Antagonist drug selectivity for radioligand binding sites on voltage-gated and receptor-gated Ca2+ channels

1989 ◽  
Vol 105 (1-2) ◽  
pp. 227-232 ◽  
Author(s):  
Drusilla B. Jaffe ◽  
Shelley S. Marks ◽  
David A. Greenberg
Keyword(s):  
Binding Sites ◽  
Radioligand Binding ◽  
Voltage Gated ◽  
Drug Selectivity ◽  
Ca2 Channels

Transcriptional regulation of voltage-gated Ca2+channels

2017 ◽  
Vol 222 (1) ◽  
pp. e12883 ◽  
Author(s):  
R. González-Ramírez ◽  
R. Felix
Keyword(s):  
Transcriptional Regulation ◽  
Voltage Gated ◽  
Ca2 Channels

Targeting voltage-gated Ca2+ channels

The Lancet ◽  
2001 ◽  
Vol 357 (9264) ◽  
pp. 1294 ◽  
Author(s):  
Jörg Striessnig
Keyword(s):  
Voltage Gated ◽  
Ca2 Channels
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