Determinants for Calmodulin Binding on Voltage-dependent Ca2+ Channels*

@article{Pate2000DeterminantsFC,
  title={Determinants for Calmodulin Binding on Voltage-dependent Ca2+ Channels*},
  author={P. Pate and J. Mochca-Morales and Y. Wu and J. Z. Zhang and G. Rodney and I. Serysheva and B. Williams and M. Anderson and S. Hamilton},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={39786 - 39792}
}
Calmodulin, bound to the α1subunit of the cardiac L-type calcium channel, is required for calcium-dependent inactivation of this channel. Several laboratories have suggested that the site of interaction of calmodulin with the channel is an IQ-like motif in the carboxyl-terminal region of the α1 subunit. Mutations in this IQ motif are linked to L-type Ca2+ current (I Ca) facilitation and inactivation. IQ peptides from L, P/Q, N, and R channels all bind Ca2+calmodulin but not Ca2+-free calmodulin… Expand
Calmodulin interactions with IQ peptides from voltage-dependent calcium channels.
Calmodulin (CaM) functions as a Ca(2+) sensor for inactivation and, in some cases, facilitation of a variety of voltage-dependent Ca(2+) channels. A crucial determinant for CaM binding to theseExpand
Apocalmodulin and Ca2+ calmodulin-binding sites on the CaV1.2 channel.
TLDR
The data are consistent with a model in which apoCaM binding to the region around the IQ motif is necessary for the rapid binding of Ca(2+) to the C-lobe of CaM, which is likely to engage the A-C region. Expand
Lobe-dependent Regulation of Ryanodine Receptor Type 1 by Calmodulin*
TLDR
It is demonstrated that amino acids 2–8 are required for high affinity binding of calmodulin to RYR1 at both nmand μm Ca2+ concentrations and for maximum inhibition of the channel at μmCa 2+ concentrations. Expand
Apo calmodulin binding to the L-type voltage-gated calcium channel Cav1.2 IQ peptide.
TLDR
New data is provided for the structural basis for the interaction of apoCaM with the IQ peptide using NMR, revealing that the apo CaM C-lobe residues are most significantly perturbed upon complex formation. Expand
Structure of calmodulin bound to the hydrophobic IQ domain of the cardiac Ca(v)1.2 calcium channel.
TLDR
A crystal structure of Ca2+-calmodulin bound to a 21 residue peptide corresponding to the IQ domain of Ca(v)1.2.2 channel is presented and it is suggested that this structure could represent the conformation that calmodulin assumes in CDF. Expand
Molecular Basis of Calmodulin Tethering and Ca2+-dependent Inactivation of L-type Ca2+ Channels*
TLDR
It is suggested that apoCaM is tethered at two sites and signals actively to slow inactivation, when the C-terminal lobe of CaM binds to the nearby CaM effector sequence (IQ motif), the braking effect is relieved, and CDI is accelerated. Expand
Caldendrin, a Neuron-specific Modulator of Cav/1.2 (L-type) Ca2+ Channels*
TLDR
Functional diversity within related Ca2-binding proteins is revealed, which may enhance the specificity of Ca2+ signaling by Cav1.2 channels in different cellular contexts. Expand
Interactions of Calmodulin with Two Peptides Derived from the C-terminal Cytoplasmic Domain of the Cav1.2 Ca2+ Channel Provide Evidence for a Molecular Switch Involved in Ca2+-induced Inactivation*
TLDR
Evidence is provided that CB and IQ motifs interacting together with calmodulin constitute a minimal molecular switch leading to Ca2+-induced inactivation, and it is suggested that they could also be the tethering site of cal modulin. Expand
Molecular determinants of Ca2+/calmodulin-dependent regulation of Cav2.1 channels
TLDR
Findings support a model in which Ca2+ binding to the C-terminal EF-hands of preassociated CaM initiates CDF via interaction with the IQ-like domain, which allows positive regulation of Cav2.1 in response to local Ca 2+ increases (CDF) and negative regulation during more global Ca2 + increases (CDI). Expand
Dynamic switching of calmodulin interactions underlies Ca2+ regulation of CaV1.3 channels
TLDR
This work uncovers frank exchange of Ca2+-calmodulin to interfaces beyond the IQ domain, initiating substantial rearrangements of the calmodulin/channel complex, furnishing a next-generation blueprint for CaV channel modulation. Expand
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References

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Calmodulin Is the Ca2+ Sensor for Ca2+-Dependent Inactivation of L-Type Calcium Channels
TLDR
It is found that overexpression of mutant, Ca2+ -insensitive calmodulin (CaM) ablates Ca2- -dependent inactivation in a "dominant-negative" manner, demonstrating that CaM is the actual Ca 2+ sensor for inactivation and suggesting that Ca M is constitutively tethered to the channel complex. Expand
Calmodulin supports both inactivation and facilitation of L-type calcium channels
TLDR
Calmodulin is shown to be a critical Ca2+ sensor for both inactivation and facilitation, and that the nature of the modulatory effect depends on residues within the IQ motif important for calmodulin binding. Expand
Ca2+-induced inhibition of the cardiac Ca2+ channel depends on calmodulin.
TLDR
It is proposed that Ca2- entering through the voltage-gated pore binds to CaM and that the Ca/CaM complex is the mediator of Ca2+ inhibition. Expand
Critical Determinants of Ca2+-Dependent Inactivation within an EF-Hand Motif of L-Type Ca2+ Channels
TLDR
It is demonstrated not only that the consensus EF hand is essential for Ca(2+) inactivation, but that a four-amino acid cluster within the F helix of the EF-hand motif is itself essential for calcium channel inactivation. Expand
Ca2+-sensitive inactivation of L-type Ca2+ channels depends on multiple cytoplasmic amino acid sequences of the alpha1C subunit.
  • R. D. Zühlke, H. Reuter
  • Biology, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
  • 1998
TLDR
It is suggested that Ca2+-dependent inactivation is a cooperative process involving several amino acid sequences in cytoplasmic segments of the alpha1C subunit. Expand
Ca2+/calmodulin binds to and modulates P/Q-type calcium channels
TLDR
A calcium-dependent interaction between calmodulin and a novel site in the carboxy-terminal domain of the α1A subunit of P/Q-type channels is reported that may contribute to calcium- dependent synaptic plasticity. Expand
Mutations in the EF-hand motif impair the inactivation of barium currents of the cardiac alpha1C channel.
TLDR
The results showed that E1537 mutations impaired voltage-dependent inactivation and suggest that the proximal part of the C-terminus may play a role in voltage- dependent inactivation in L-type alpha1C channels. Expand
Essential Ca2+-Binding Motif for Ca2+-Sensitive Inactivation of L-Type Ca2+ Channels
Intracellular calcium (Ca2+) inhibits the opening of L-type (α1C) Ca2+ channels, providing physiological control of Ca2+ entry into a wide variety of cells. A structural determinant of thisExpand
Ca2+-sensitive Inactivation and Facilitation of L-type Ca2+ Channels Both Depend on Specific Amino Acid Residues in a Consensus Calmodulin-binding Motif in theα1C subunit*
TLDR
The functional effects of an extensive series of modifications of the IQ motif aimed at dissecting the structural determinants of the different forms of modulation of L-type Ca2+ channels were reported. Expand
Structural Regions of the Cardiac Ca Channel α1C Subunit Involved in Ca-dependent Inactivation
TLDR
The findings suggest that structural determinants of Ca-dependent inactivation are distributed among several major cytoplasmic domains of α1C, possibly by interacting with other proteins or other regions of the Ca channel. Expand
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