Regulation of the NaV1.5 cytoplasmic domain by calmodulin.
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ABSTRACT:
SUBMITTER: Gabelli SB
PROVIDER: S-EPMC4223872 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Publications
Regulation of the NaV1.5 cytoplasmic domain by calmodulin.
Gabelli Sandra B SB Boto Agedi A Kuhns Victoria Halperin VH Bianchet Mario A MA Farinelli Federica F Aripirala Srinivas S Yoder Jesse J Jakoncic Jean J Tomaselli Gordon F GF Amzel L Mario LM
Nature communications 20141105
Voltage-gated sodium channels (Na(v)) underlie the rapid upstroke of action potentials in excitable tissues. Binding of channel-interactive proteins is essential for controlling fast and long-term inactivation. In the structure of the complex of the carboxy-terminal portion of Na(v)1.5 (CTNa(v)1.5) with calmodulin (CaM)-Mg(2+) reported here, both CaM lobes interact with the CTNa(v)1.5. On the basis of the differences between this structure and that of an inactivated complex, we propose that the ...[more]
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