Browsing by Author "Micu, Ileana"
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Item Open Access A T-type channel-calmodulin complex triggers αCaMKII activation(2017-08-11) Asmara, Hadhimulya; Micu, Ileana; Rizwan, Arsalan P; Sahu, Giriraj; Simms, Brett A; Zhang, Fang-Xiong; Engbers, Jordan D T; Stys, Peter K; Zamponi, Gerald W; Turner, Ray WAbstract Calmodulin (CaM) is an important signaling molecule that regulates a vast array of cellular functions by activating second messengers involved in cell function and plasticity. Low voltage-activated calcium channels of the Cav3 family have the important role of mediating low threshold calcium influx, but were not believed to interact with CaM. We find a constitutive association between CaM and the Cav3.1 channel at rest that is lost through an activity-dependent and Cav3.1 calcium-dependent CaM dissociation. Moreover, Cav3 calcium influx is sufficient to activate αCaMKII in the cytoplasm in a manner that depends on an intact Cav3.1 C-terminus needed to support the CaM interaction. Our findings thus establish that T-type channel calcium influx invokes a novel dynamic interaction between CaM and Cav3.1 channels to trigger a signaling cascade that leads to αCaMKII activation.Item Open Access Excitatory glycine responses of CNS myelin mediated by NR1/NR3 "NMDA" receptor subunits(Society for Neuroscience, 2010-08-25) Piña-Crespo, Juan C.; Talantova, Maria V.; Micu, Ileana; States, Bradley A.; Chen, Huei Sheng Vincent; Tu, Shichun; Nakanishi, Nobuki; Tong, Gary G.; Zhang, Dongxian; Heinemann, Stephen F.; Zamponi, Gerald W.; Stys, Peter K.; Lipton, Stuart A.NMDA receptors are typically excited by a combination of glutamate and glycine. Here we describe excitatory responses in CNS myelin that are gated by a glycine agonist alone and mediated by NR1/NR3 "NMDA" receptor subunits. Response properties include activation by d-serine, inhibition by the glycine-site antagonist CNQX, and insensitivity to the glutamate-site antagonist d-APV. d-Serine responses were abrogated in NR3A-deficient mice. Our results suggest the presence of functional NR1/NR3 receptors in CNS myelin.