Rem, a member of the RGK GTPases, inhibits recombinant CaV1.2 channels using multiple mechanisms that require distinct conformations of the GTPase.
about
Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathyL-type calcium channel targeting and local signalling in cardiac myocytesStructure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channelsSmall G proteins in the cardiovascular system: physiological and pathological aspectsBARP suppresses voltage-gated calcium channel activity and Ca2+-evoked exocytosisHomodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.The ß subunit of voltage-gated Ca2+ channelsDirect inhibition of P/Q-type voltage-gated Ca2+ channels by Gem does not require a direct Gem/Cavbeta interactionA loss-of-function analysis reveals that endogenous Rem2 promotes functional glutamatergic synapse formation and restricts dendritic complexityAncient origins of RGK protein function: modulation of voltage-gated calcium channels preceded the protostome and deuterostome split.Differential effects of RGK proteins on L-type channel function in adult mouse skeletal muscleRegulation of high-voltage-activated Ca(2+) channel function, trafficking, and membrane stability by auxiliary subunits.Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation.Gαi2- and Gαi3-specific regulation of voltage-dependent L-type calcium channels in cardiomyocytes.Molecular mechanisms, and selective pharmacological rescue, of Rem-inhibited CaV1.2 channels in heart.Distinct RGK GTPases differentially use α1- and auxiliary β-binding-dependent mechanisms to inhibit CaV1.2/CaV2.2 channels.Bio-inspired voltage-dependent calcium channel blockersLQT1 mutations in KCNQ1 C-terminus assembly domain suppress IKs using different mechanisms.Solution NMR and calorimetric analysis of Rem2 binding to the Ca2+ channel β4 subunit: a low affinity interaction is required for inhibition of Cav2.1 Ca2+ currentsRem uncouples excitation-contraction coupling in adult skeletal muscle fibers.Molecular determinants of Gem protein inhibition of P/Q-type Ca2+ channelsRem-GTPase regulates cardiac myocyte L-type calcium current.Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels.Manipulating L-type calcium channels in cardiomyocytes using split-intein protein transsplicingRegulation of voltage-dependent calcium channels by RGK proteins.Ion channel engineering: perspectives and strategies.RGK regulation of voltage-gated calcium channels.Functional assessment of three Rem residues identified as critical for interactions with Ca(2+) channel β subunits.Quantifying macromolecular interactions in living cells using FRET two-hybrid assays.Rad and Rem are non-canonical G-proteins with respect to the regulatory role of guanine nucleotide binding in Ca(V)1.2 channel regulation.Defining the MO's of RGK proteins.Adrenergic signaling controls RGK-dependent trafficking of cardiac voltage-gated L-type Ca2+ channels through PKD1.Mechanism of auxiliary β-subunit-mediated membrane targeting of L-type (Ca(V)1.2) channels.Sculpting ion channel functional expression with engineered ubiquitin ligases.Molecular mechanisms and physiological relevance of RGK proteins in the heart.Impaired excitation-contraction coupling in muscle fibres from the dynamin2R465W mouse model of centronuclear myopathy.Bilobal architecture is a requirement for calmodulin signaling to CaV1.3 channels.Development of a High-Throughput Flow Cytometry Assay to Monitor Defective Trafficking and Rescue of Long QT2 Mutant hERG Channels.
P2860
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P2860
Rem, a member of the RGK GTPases, inhibits recombinant CaV1.2 channels using multiple mechanisms that require distinct conformations of the GTPase.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@en
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@nl
type
label
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@en
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@nl
prefLabel
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@en
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@nl
P2093
P2860
P1476
Rem, a member of the RGK GTPas ...... t conformations of the GTPase.
@en
P2093
Henry M Colecraft
Timothy Kernan
Tingting Yang
Vincent Wu
Xianghua Xu
P2860
P304
P356
10.1113/JPHYSIOL.2010.187203
P407
P577
2010-03-22T00:00:00Z