145 research outputs found
Cholesterol Sensitivity of Kir2.1 is Modulated by a Cytosolic Belt: Implications for Kir Gating
Revival-collapse phenomenon in the quadrature squeezing of the multiphoton Jaynes-Cummings model with the binomial states
In this paper we study the interaction between two-level atom and quantized
single-mode field, namely, Jaynes-Cummings model (JCM). The field and the atom
are initially prepared in the binomial state and the excited atomic state,
respectively. For this system we prove that the revival-collapse phenomenon
exhibited in the atomic inversion of the standard JCM can be numerically
(naturally) manifested in the evolution of the squeezing factor of the
three-photon (standard) JCM provided that the initial photon-number
distribution of the radiation has a smooth envelope.Comment: 14 pages, 4 figures, Comments are most welcom
Q/R site interactions with the M3 helix in GluK2 kainate receptor channels revealed by thermodynamic mutant cycles
RNA editing at the Q/R site near the apex of the pore loop of AMPA and kainate receptors controls a diverse array of channel properties, including ion selectivity and unitary conductance and susceptibility to inhibition by polyamines and cis-unsaturated fatty acids, as well as subunit assembly into tetramers and regulation by auxiliary subunits. How these different aspects of channel function are all determined by a single amino acid substitution remains poorly understood; however, several lines of evidence suggest that interaction between the pore helix (M2) and adjacent segments of the transmembrane inner (M3) and outer (M1) helices may be involved. In the present study, we have used double mutant cycle analysis to test for energetic coupling between the Q/R site residue and amino acid side chains along the M3 helix. Our results demonstrate interaction with several M3 locations and particularly strong coupling to substitution for L614 at the level of the central cavity. In this location, replacement with smaller side chains completely and selectively reverses the effect of fatty acids on gating of edited channels, converting strong inhibition of wild-type GluK2(R) to nearly 10-fold potentiation of GluK2(R) L614A
Quantum phase properties of two-mode Jaynes-Cummings model for Schr\"odinger-cat states: interference and entanglement
In this paper we investigate the quantum phase properties for the coherent
superposition states (Schr\"odinger-cat states) for two-mode multiphoton
Jaynes-Cummings model in the framework of the Pegg-Barnett formalism. We also
demonstrate the behavior of the Wigner () function at the phase space
origin. We obtain many interesting results such as there is a clear
relationship between the revival-collapse phenomenon occurring in the atomic
inversion (as well as in the evolution of the function) and the behavior of
the phase distribution of both the single-mode and two-mode cases. Furthermore,
we find that the phase variances of the single-mode case can exhibit
revival-collapse phenomenon about the long-time behavior. We show that such
behavior occurs for interaction time several times smaller than that of the
single-mode Jaynes-Cummings model.Comment: 23, 8 figure
The revival-collapse phenomenon in the quadrature field components of the two-mode multiphoton Jaynes-Cummings model
In this paper we consider a system consisting of a two-level atom in an
excited state interacting with two modes of a radiation field prepared
initially in -photon coherent states. This system is described by two-mode
multiphoton (, i.e., ) Jaynes-Cummings model (JCM). For this system
we investigate the occurrence of the revival-collapse phenomenon (RCP) in the
evolution of the single-mode, two-mode, sum and difference quadrature
squeezing. We show that there is a class of states for which all these types of
squeezing exhibit RCP similar to that involved in the corresponding atomic
inversion. Also we show numerically that the single-mode squeezing of the first
mode for provides RCP similar to that of the atomic inversion
of the case , however, sum and difference squeezing give
partial information on that case. Moreover, we show that single-mode, two-mode
and sum squeezing for the case provide information on the
atomic inversion of the single-mode two-photon JCM. We derive the rescaled
squeezing factors giving accurate information on the atomic inversion for all
cases. The consequences of these results are that the homodyne and heterodyne
detectors can be used to detect the RCP for the two-mode JCM.Comment: 18 pages, 6 figure
Selective Phosphorylation Modulates the PIP2 Sensitivity of the CaM-SK Channel Complex
Phosphatidylinositol bisphosphate (PIP2) regulates the activities of many membrane proteins including ion channels through direct interactions. However, the affinity of PIP2 is so high for some channel proteins that its physiological role as a modulator has been questioned. Here we show that PIP2 is an important cofactor for activation of small conductance Ca2+-activated potassium channels (SK) by Ca2+-bound calmodulin (CaM). Removal of the endogenous PIP2 inhibits SK channels. The PIP2-binding site resides at the interface of CaM and the SK C-terminus. We further demonstrate that the affinity of PIP2 for its target proteins can be regulated by cellular signaling. Phosphorylation of CaM T79, located adjacent to the PIP2-binding site, by Casein Kinase 2 reduces the affinity of PIP2 for the CaM-SK channel complex by altering the dynamic interactions among amino acid residues surrounding the PIP2-binding site. This effect of CaM phosphorylation promotes greater channel inhibition by G-protein-mediated hydrolysis of PIP2
Non-equivalent role of TM2 gating hinges in heteromeric Kir4.1/Kir5.1 potassium channels
Comparison of the crystal structures of the KcsA and MthK potassium channels suggests that the process of opening a K+ channel involves pivoted bending of the inner pore-lining helices at a highly conserved glycine residue. This bending motion is proposed to splay the transmembrane domains outwards to widen the gate at the âhelix-bundle crossingâ. However, in the inwardly rectifying (Kir) potassium channel family, the role of this âhingeâ residue in the second transmembrane domain (TM2) and that of another putative glycine gating hinge at the base of TM2 remain controversial. We investigated the role of these two positions in heteromeric Kir4.1/Kir5.1 channels, which are unique amongst Kir channels in that both subunits lack a conserved glycine at the upper hinge position. Contrary to the effect seen in other channels, increasing the potential flexibility of TM2 by glycine substitutions at the upper hinge position decreases channel opening. Furthermore, the contribution of the Kir4.1 subunit to this process is dominant compared to Kir5.1, demonstrating a non-equivalent contribution of these two subunits to the gating process. A homology model of heteromeric Kir4.1/Kir5.1 shows that these upper âhingeâ residues are in close contact with the base of the pore α-helix that supports the selectivity filter. Our results also indicate that the highly conserved glycine at the âlowerâ gating hinge position is required for tight packing of the TM2 helices at the helix-bundle crossing, rather than acting as a hinge residue
A structural model for K2P potassium channels based on 23 pairs of interacting sites and continuum electrostatics
K2PĂ, the two-pore domain potassium background channel that determines cardiac rhythm in Drosophila melanogaster, and its homologues that establish excitable membrane activity in mammals are of unknown structure. K2P subunits have two pore domains flanked by transmembrane (TM) spans: TM1-P1-TM2-TM3-P2-TM4. To establish spatial relationships in K2PĂ, we identified pairs of sites that display electrostatic compensation. Channels silenced by the addition of a charge in pore loop 1 (P1) or P2 were restored to function by countercharges at specific second sites. A three-dimensional homology model was determined using the crystal structure of KV1.2, effects of K2PĂ mutations to establish alignment, and compensatory chargeâcharge pairs. The model was refined and validated by continuum electrostatic free energy calculations and covalent linkage of introduced cysteines. K2P channels use two subunits arranged so that the P1 and P2 loops contribute to one pore, identical P loops face each other diagonally across the pore, and the channel complex has bilateral symmetry with a fourfold symmetric selectivity filter
Voltage- and temperature-dependent activation of TRPV3 channels is potentiated by receptor-mediated PI(4,5)P2 hydrolysis
TRPV3 is a thermosensitive channel that is robustly expressed in skin keratinocytes and activated by innocuous thermal heating, membrane depolarization, and chemical agonists such as 2-aminoethyoxy diphenylborinate, carvacrol, and camphor. TRPV3 modulates sensory thermotransduction, hair growth, and susceptibility to dermatitis in rodents, but the molecular mechanisms responsible for controlling TRPV3 channel activity in keratinocytes remain elusive. We show here that receptor-mediated breakdown of the membrane lipid phosphatidylinositol (4,5) bisphosphate (PI(4,5)P2) regulates the activity of both native TRPV3 channels in primary human skin keratinocytes and expressed TRPV3 in a HEK-293âderived cell line stably expressing muscarinic M1-type acetylcholine receptors. Stimulation of PI(4,5)P2 hydrolysis or pharmacological inhibition of PI 4 kinase to block PI(4,5)P2 synthesis potentiates TRPV3 currents by causing a negative shift in the voltage dependence of channel opening, increasing the proportion of voltage-independent current and causing thermal activation to occur at cooler temperatures. The activity of single TRPV3 channels in excised patches is potentiated by PI(4,5)P2 depletion and selectively decreased by PI(4,5)P2 compared with related phosphatidylinositol phosphates. Neutralizing mutations of basic residues in the TRP domain abrogate the effect of PI(4,5)P2 on channel function, suggesting that PI(4,5)P2 directly interacts with a specific protein motif to reduce TRPV3 channel open probability. PI(4,5)P2-dependent modulation of TRPV3 activity represents an attractive mechanism for acute regulation of keratinocyte signaling cascades that control cell proliferation and the release of autocrine and paracrine factors
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