The RGK family of GTP-binding proteins: regulators of voltage-dependent calcium channels and cytoskeleton remodeling. - Wikidata - awgldk - TriplyDB

The RGK family of GTP-binding proteins: regulators of voltage-dependent calcium channels and cytoskeleton remodeling.

The RGK family of GTP-binding proteins: regulators of voltage-dependent calcium channels and cytoskeleton remodeling.

http://www.wikidata.org/entity/Q36478004

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Molecular mechanisms of activity-dependent changes in dendritic morphology: role of RGK proteins Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channels Activity-dependent subcellular cotrafficking of the small GTPase Rem2 and Ca2+/CaM-dependent protein kinase IIα Structure of the GDP-bound G domain of the RGK protein Rem2 Evolutionary expansion of the Ras switch regulatory module in eukaryotes The ß subunit of voltage-gated Ca2+ channels Direct inhibition of P/Q-type voltage-gated Ca2+ channels by Gem does not require a direct Gem/Cavbeta interaction A loss-of-function analysis reveals that endogenous Rem2 promotes functional glutamatergic synapse formation and restricts dendritic complexity Ancient origins of RGK protein function: modulation of voltage-gated calcium channels preceded the protostome and deuterostome split.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 blockers Mice deficient in GEM GTPase show abnormal glucose homeostasis due to defects in beta-cell calcium handling Topological and functional properties of the small GTPases protein interaction network.Rem GTPase interacts with the proximal CaV1.2 C-terminus and modulates calcium-dependent channel inactivation Gem-induced cytoskeleton remodeling increases cellular migration of HTLV-1-infected cells, formation of infected-to-target T-cell conjugates and viral transmission.Regulation of voltage-gated calcium channels by proteolysis.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+ currents Isolation and molecular characterization of Rem2 isoforms in the rainbow trout (Oncorhynchus mykiss): Tissue and central nervous system expression Comparison of the neutrophil proteome in trauma patients and normal controls.Molecular determinants of Gem protein inhibition of P/Q-type Ca2+ channels Differentially expressed genes linked to natural variation in long-term memory formation in Cotesia parasitic wasps Rem-GTPase regulates cardiac myocyte L-type calcium current.Rem2, a member of the RGK family of small GTPases, is enriched in nuclei of the basal ganglia.CaMKII-dependent phosphorylation of the GTPase Rem2 is required to restrict dendritic complexity.Similar molecular determinants on Rem mediate two distinct modes of inhibition of CaV1.2 channels.Rem2 is an activity-dependent negative regulator of dendritic complexity in vivo.Engineering proteins for custom inhibition of Ca(V) channels.Rem2 in the bullfrog (Rana catesbeiana): Patterns of expression within the central nervous system and brain expression at different ontogenetic stages Gonadotrophin-releasing hormone signalling downstream of calmodulin.Regulation of voltage-dependent calcium channels by RGK proteins.RGK regulation of voltage-gated calcium channels.The GTPase Rem2 regulates synapse development and dendritic morphology The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels.Localization of rem2 in the central nervous system of the adult rainbow trout (Oncorhynchus mykiss).Rem, a member of the RGK GTPases, inhibits recombinant CaV1.2 channels using multiple mechanisms that require distinct conformations of the GTPase.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.A presynaptic homeostatic signaling system composed of the Eph receptor, ephexin, Cdc42, and CaV2.1 calcium channels.Adrenergic signaling controls RGK-dependent trafficking of cardiac voltage-gated L-type Ca2+ channels through PKD1.Nuclear envelope proteins Nesprin2 and LaminA regulate proliferation and apoptosis of vascular endothelial cells in response to shear stress.Acquired expression of CblQ367P in mice induces dysplastic myelopoiesis mimicking chronic myelomonocytic leukemia.

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P2860

The RGK family of GTP-binding proteins: regulators of voltage-dependent calcium channels and cytoskeleton remodeling.

http://www.wikidata.org/entity/Q36478004

description

2007 nî lūn-bûn

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2007年の論文

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年学术文章

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2007年學術文章

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2007年學術文章

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2007年學術文章

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name

The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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type

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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J.CELLSIG.2007.10.028

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Cellular Signalling

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The RGK family of GTP-binding ...... s and cytoskeleton remodeling.

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Brian S Finlin

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Chunyan Pang

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Dana M Niedowicz

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Douglas A Andres

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Robert N Correll

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P2860

A novel Rho GTPase-activating-protein interacts with Gem, a member of the Ras superfamily of GTPases

14-3-3 and calmodulin control subcellular distribution of Kir/Gem and its regulation of cell shape and calcium channel activity

Phosphorylation of critical serine residues in Gem separates cytoskeletal reorganization from down-regulation of calcium channel activity

Dominant negative suppression of Rad leads to QT prolongation and causes ventricular arrhythmias via modulation of L-type Ca2+ channels in the heart

Structure-function studies of the G-domain from human gem, a novel small G-protein

Biochemical and structural characterization of the gem GTPase

Gem: an induced, immediate early protein belonging to the Ras family

Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans

Effects of phosphorylation on function of the Rad GTPase

Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for 'front-back' communication.

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292-300

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