2005
DOI: 10.1073/pnas.0409885102
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Sites of proteolytic processing and noncovalent association of the distal C-terminal domain of CaV1.1 channels in skeletal muscle

Abstract: In skeletal muscle cells, voltage-dependent potentiation of Ca 2؉ channel activity requires phosphorylation by cAMP-dependent protein kinase (PKA) anchored via an A-kinase anchoring protein (AKAP15), and the most rapid sites of phosphorylation are located in the C-terminal domain. Surprisingly, the site of interaction of the complex of PKA and AKAP15 with the ␣1-subunit of CaV1.1 channels lies in the distal C terminus, which is cleaved from the remainder of the channel by in vivo proteolytic processing. Here w… Show more

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Cited by 94 publications
(122 citation statements)
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“…Although another species and time frame, this indicates a putative time-and activity-dependent regulation of CAC-NA1D expression. Indeed, for the related Ca v 1.2 channel, a mechanism has been put forward whereby calpain Ca 2+ dependently cleaves an (among L-type VGCC well conserved [47]) autoinhibitory C-terminal domain of the channel. The cleaved C-terminus disinhibits the channel and acts as a transcription factor that controls expression of the Ca v 1.2 encoding gene CACNA1C [48].…”
Section: Discussionmentioning
confidence: 99%
“…Although another species and time frame, this indicates a putative time-and activity-dependent regulation of CAC-NA1D expression. Indeed, for the related Ca v 1.2 channel, a mechanism has been put forward whereby calpain Ca 2+ dependently cleaves an (among L-type VGCC well conserved [47]) autoinhibitory C-terminal domain of the channel. The cleaved C-terminus disinhibits the channel and acts as a transcription factor that controls expression of the Ca v 1.2 encoding gene CACNA1C [48].…”
Section: Discussionmentioning
confidence: 99%
“…Upon dissociation from the channel, the Asn-Ca v 1.1 fragment migrates to the nucleus and functions as a transcriptional regulator. 97,143,144,145 #7. Arg-GlyT1A is the Ct fragment of the transmembrane GlyT1A glycine transporter.…”
Section: Monitoring Protein Fragments and Reacting To Their Accumulationmentioning
confidence: 99%
“…2). These phosphorylation sites reside in the proximal C-terminal regulatory domain (PCRD), which is responsible for interaction with and regulation by the proteolytically processed dCT of Ca V 1.1 (23). Both phosphorylation sites are present on a single tryptic peptide ( Fig.…”
Section: Resultsmentioning
confidence: 99%
“…Skeletal muscle Ca V 1.1 channels and cardiac Ca V 1.2 channels are both posttranslationally processed in vivo by proteolysis near the center of the 600-amino acid C-terminal domain (17)(18)(19)(20)(21)(22)(23), but proteolytic processing is not observed in transfected nonmuscle cells (24). The C terminus is a substrate for PKA, and the sites of most rapid phosphorylation of purified Ca V 1.1 and Ca V 1.2 in vitro are located in the distal C-terminal domain (19,25,26).…”
mentioning
confidence: 99%
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