Description
Title: Calmodulin and CaBP1 Regulate L-Type Ca2+ Channels
Abstract: The Ca2+ sensor proteins calmodulin (CaM) and Ca2+ binding Protein 1 (CaBP1) interact with L-type voltage-gated Ca2+ channels (CaV1.2 and CaV1.3, collectively referred to as CaV) to control the opposite of Ca2+ dependent channel activity. Each of CaM and CaBP1’s interactions with the IQ-motif in the C-terminal cytosolic domain of CaV increases the probability that a channel will open in basal conditions. Rapid Ca2+-dependent channel inactivation is promoted by Ca2+-bound CaM binding to CaV at elevated cytosolic Ca2+ levels (caused by CaV channel opening) (CDI). Contrarily, CDI is prevented and Ca2+-induced channel opening is promoted by CaV binding to CaBP1 (called CDF). In order to better understand how CaM promotes CDI while CaBP1 prevents CDI and instead promotes CDF, I give a brief overview of the known structures of CaM and CaBP1 in this review. Ca2+-free forms of CaM and CaBP1 may pre-associate with CaV under basal conditions, according to previous electrophysiology studies. However, previous Ca2+ binding data imply that when CaM or CaBP1 is bound to the IQ-motif, both CaM and CaBP1 are calculated to bind to Ca2+ with an apparent dissociation constant of 100 nM. Since the cytosolic Ca2+ concentration in neuronal basal conditions is less than 100 nM, it is hypothesized that nearly 50% of the neuronal CaV channels are bound to Ca2+-bound forms of either CaM or CaBP1 at basal levels. Here, it is predicted that the pre-association of CaV with calcified forms of CaM or CaBP1 will have functional ramifications. To explain how CaBP1 might prevent CDI, it is proposed that the Ca2+-bound form of CaBP1 binds to CaV under basal conditions to block CaV binding to CaM.
Keywords: calmodulin; CaBP1; CaV1.2; CaV1.3; L-type Ca2+ channel; EF-hand; IQ-motif
Paper Quality: SCOPUS / Web of Science Level Research Paper
Subject: Biomolecules
Writer Experience: 20+ Years
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