Ca2+-independent Activation of Ca2+/Calmodulin-dependent Protein Kinase II Bound to the C-terminal Domain of CaV2.1 Calcium Channels

Magupalli, Venkat Giri; Mochida, Sumiko; Jin, Yan; Jiang, Xin; Westenbroek, Ruth E.; Nairn, Angus C.; Scheuer, Todd; Catterall, William A.

doi:10.1074/jbc.m112.369058

Cited by 35 publications

(26 citation statements)

References 61 publications

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“…Cultured SCG neurons transfected with wild-type or mutant calcium channels are an advantageous experimental system for studies of the role of calcium channel regulation in synaptic plasticity (Leal et al, 2012; Magupalli et al, 2013; Mochida et al, 2008; Mochida et al, 2003). Endogenous neurotransmission in cultured SCG neurons is mediated by N-type Ca 2+ currents, which can be blocked by ω-conotoxin GVIA (Mochida et al, 2008; Mochida et al, 2003).…”

Section: Resultsmentioning

confidence: 99%

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Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Jin

Leal

Magupalli

et al. 2014

Molecular and Cellular Neuroscience

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Facilitation and inactivation of P/Q-type Ca2+ currents mediated by Ca2+/calmodulin binding to CaV2.1 channels contribute to facilitation and rapid depression of synaptic transmission, respectively. Other calcium sensor proteins displace calmodulin from its binding site and differentially modulate P/Q-type Ca2+ currents, resulting in diverse patterns of short-term synaptic plasticity. Neuronal calcium sensor-1 (NCS-1, frequenin) has been shown to enhance synaptic facilitation, but the underlying mechanism is unclear. We report here that NCS-1 directly interacts with IQ-like motif and calmodulin-binding domain in the C-terminal domain of CaV2.1 channel. NCS-1 reduces Ca2+-dependent inactivation of P/Q-type Ca2+ current through interaction with the IQ-like motif and calmodulin-binding domain without affecting peak current or activation kinetics. Expression of NCS-1 in presynaptic superior cervical ganglion neurons has no effect on synaptic transmission, eliminating effects of this calcium sensor protein on endogenous N-type Ca2+ currents and the endogenous neurotransmitter release machinery. However, in superior cervical ganglion neurons expressing wild-type CaV2.1 channels, co-expression of NCS-1 induces facilitation of synaptic transmission in response to paired pulses and trains of depolarizing stimuli, and this effect is lost in CaV2.1 channels with mutations in the IQ-like motif and calmodulin-binding domain. These results reveal that NCS-1 directly modulates CaV2.1 channels to induce short-term synaptic facilitation and further demonstrate that CaS proteins are crucial in fine-tuning short-term synaptic plasticity.

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Section: Resultsmentioning

confidence: 99%

“…Binding assays were performed as previously described (Magupalli et al, 2013; Nanou et al, 2012). NCS-1-MBP or MBP alone was immobilized on amylose beads (New England Biolabs, Beverly, MA) that were extensively washed with PBS buffer.…”

Section: Experimental Methodsmentioning

confidence: 99%

Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Jin

Leal

Magupalli

et al. 2014

Molecular and Cellular Neuroscience

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“…This suggested that the 'urea wash' process successfully reduced the number of cytoplasmic proteins. Nevertheless, calcium/calmodulin-dependent protein kinase II type b (CAMK2B) and type d (CAMK2D), cytoplasmic proteins that interact with membrane proteins (Muthalif et al, 1996;Lisman et al, 2002;Thalhammer et al, 2006;Abiria & Colbran, 2010;Magupalli et al, 2013;Doroudi et al, 2015), were detected in all mass spectrometry analyses of 'no urea wash' and 'urea wash' samples. Furthermore, because the membrane fractions were prepared after sonication of the tissues (see Materials and methods), the samples should contain whole membrane proteins of all cellular compartments, including the mitochondria and endoplasmic reticulum, in addition to the plasma membrane.…”

Section: Proteome Analysis Of the Stria Vascularismentioning

confidence: 99%

Molecular architecture of the stria vascularis membrane transport system, which is essential for physiological functions of the mammalian cochlea

Uetsuka

Ogata

Nagamori

et al. 2015

Eur J of Neuroscience

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Stria vascularis of the mammalian cochlea transports K(+) to establish the electrochemical property in the endolymph crucial for hearing. This epithelial tissue also transports various small molecules. To clarify the profile of proteins participating in the transport system in the stria vascularis, membrane components purified from the stria of adult rats were analysed by liquid chromatography tandem mass spectrometry. Of the 3236 proteins detected in the analysis, 1807 were membrane proteins. Ingenuity Knowledge Base and literature data identified 513 proteins as being expressed on the 'plasma membrane', these included 25 ion channels and 79 transporters. Sixteen of the former and 62 of the latter had not yet been identified in the stria. Unexpectedly, many Cl(-) and Ca(2+) transport systems were found, suggesting that the dynamics of these ions play multiple roles. Several transporters for organic substances were also detected. Network analysis demonstrated that a few kinases, including protein kinase A, and Ca(2+) were key regulators for the strial transports. In the library of channels and transporters, 19 new candidates for uncloned deafness-related genes were identified. These resources provide a platform for understanding the molecular mechanisms underlying the epithelial transport essential for cochlear function and the pathophysiological processes involved in hearing disorders.

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“…There are many examples in different signaling pathways, including those regulating VDCCs. The phosphatase calcineurin has been shown to regulate Ca V 1.2 by a direct interaction 189 ; CaMKII is activated after direct binding to Ca V 2.1 channels 190 ; AKAP5 directly interacts with several cytosolic segments of α 1C and was hypothesized to regulate the channel's function. 15 Extensive use of specific phosphorylation and protein interaction inhibitors is a powerful and discriminatory approach to address these options.…”

Section: Concluding Remarks and Perspectivesmentioning

confidence: 99%

Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

Weiss

Benmocha

et al. 2013

Circulation Research

101

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Abstract:In the heart, adrenergic stimulation activates the β-adrenergic receptors coupled to the heterotrimeric stimulatory G s protein, followed by subsequent activation of adenylyl cyclase, elevation of cyclic AMP levels, and protein kinase A (PKA) activation. One of the main targets for PKA modulation is the cardiac L-type Ca 2+ channel (Ca V 1.2) located in the plasma membrane and along the T-tubules, which mediates Ca 2+ entry into cardiomyocytes. β-Adrenergic receptor activation increases the Ca 2+ current via Ca V 1.2 channels and is responsible for the positive ionotropic effect of adrenergic stimulation. Despite decades of research, the molecular mechanism underlying this modulation has not been fully resolved. On the contrary, initial reports of identification of key components in this modulation were later refuted using advanced model systems, especially transgenic animals. Some of the cardinal debated issues include details of specific subunits and residues in Ca

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Ca2+-independent Activation of Ca2+/Calmodulin-dependent Protein Kinase II Bound to the C-terminal Domain of CaV2.1 Calcium Channels

Cited by 35 publications

References 61 publications

Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Molecular architecture of the stria vascularis membrane transport system, which is essential for physiological functions of the mammalian cochlea

Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

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Ca2+-independent Activation of Ca2+/Calmodulin-dependent Protein Kinase II Bound to the C-terminal Domain of CaV2.1 Calcium Channels

Cited by 35 publications

References 61 publications

Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Modulation of CaV2.1 channels by neuronal calcium sensor-1 induces short-term synaptic facilitation

Molecular architecture of the stria vascularis membrane transport system, which is essential for physiological functions of the mammalian cochlea

Regulation of Cardiac L-Type Ca 2+ Channel Ca V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway

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Regulation of Cardiac L-Type Ca ²⁺ Channel Ca _V 1.2 Via the β-Adrenergic-cAMP-Protein Kinase A Pathway