Characterization of the calmodulin-binding site in the N terminus of CaV1.2

Adva Benmocha*, Lior Almagor, Shimrit Oz, Joel A. Hirsch, Nathan Dascal

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

19 Scopus citations

Abstract

Interaction of calmodulin (CaM) with the C-terminus (CT) of the L-type CaV1.2 channel is crucial for Ca2+-dependent inactivation (CDI). CaM also binds to the N-terminus (NT), and a CaM-formed "bridge" between CT and NT has been proposed to control CDI. We characterized the interaction of CaM with its NT-binding peptide. Binding is Ca2+-dependent with an affinity of 0.6 μM. Mutations in NT of CaV1.2 that abolished the binding of CaM only slightly weakened the CDI but also accelerated the VDI. CaM did not foster an interaction between the CaM-binding peptides of NT and CT. Thus, the role of CaM's interaction with the CaV1.2 NT remains to be determined.

Original languageEnglish
JournalChannels
Volume3
Issue number5
DOIs
StatePublished - 2009

Funding

FundersFunder number
United States-Israel Binational Science Foundation2005340
Israel Science Foundation1201/04

    Keywords

    • Binding
    • Ca1.2
    • Calcium channel
    • Calmodulin
    • Inactivation
    • L-type

    Fingerprint

    Dive into the research topics of 'Characterization of the calmodulin-binding site in the N terminus of CaV1.2'. Together they form a unique fingerprint.

    Cite this