Binding of protein phosphatase 2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation
about
Obscurin targets ankyrin-B and protein phosphatase 2A to the cardiac M-lineCyclin G2 is a centrosome-associated nucleocytoplasmic shuttling protein that influences microtubule stability and induces a p53-dependent cell cycle arrestCounteracting Protein Kinase Activity in the Heart: The Multiple Roles of Protein PhosphatasesCaV1.2 signaling complexes in the heartStructure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylationCapping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic releasemiR-1 overexpression enhances Ca(2+) release and promotes cardiac arrhythmogenesis by targeting PP2A regulatory subunit B56alpha and causing CaMKII-dependent hyperphosphorylation of RyR2Molecular basis for PP2A regulatory subunit B56alpha targeting in cardiomyocytesAKAP79/150 anchoring of calcineurin controls neuronal L-type Ca2+ channel activity and nuclear signalingPhysical and functional interaction between calcineurin and the cardiac L-type Ca2+ channelAssembly of a beta2-adrenergic receptor--GluR1 signalling complex for localized cAMP signallingDiversity in genomic organisation, developmental regulation and distribution of the murine PR72/B" subunits of protein phosphatase 2AModulation of calcium-dependent inactivation of L-type Ca2+ channels via β-adrenergic signaling in thalamocortical relay neuronsChronic stress targets posttranscriptional mechanisms to rapidly upregulate α1C-subunit of Cav1.2b calcium channels in colonic smooth muscle cellsCardiac function is regulated by B56α-mediated targeting of protein phosphatase 2A (PP2A) to contractile relevant substrates.Targeting of protein phosphatases PP2A and PP2B to the C-terminus of the L-type calcium channel Ca v1.2.The PDZ motif of the α1C subunit is not required for surface trafficking and adrenergic modulation of CaV1.2 channel in the heart.The B''/PR72 subunit mediates Ca2+-dependent dephosphorylation of DARPP-32 by protein phosphatase 2A.β2-Adrenergic receptor supports prolonged theta tetanus-induced LTPCompetition between α-actinin and Ca²⁺-calmodulin controls surface retention of the L-type Ca²⁺ channel Ca(V)1.2.Age-dependent requirement of AKAP150-anchored PKA and GluR2-lacking AMPA receptors in LTP.Increased intracellular magnesium attenuates β-adrenergic stimulation of the cardiac Ca(V)1.2 channel.Pyruvate restores β-adrenergic sensitivity of L-type Ca(2+) channels in failing rat heart: role of protein phosphatasep21-Activated kinase-1 and its role in integrated regulation of cardiac contractility.Cardiomyocyte specific deletion of PP2A causes cardiac hypertrophy.Adenylyl cyclase anchoring by a kinase anchor protein AKAP5 (AKAP79/150) is important for postsynaptic β-adrenergic signaling.Expression of active p21-activated kinase-1 induces Ca2+ flux modification with altered regulatory protein phosphorylation in cardiac myocytesRegulation of cardiac excitation and contraction by p21 activated kinase-1Calcineurin-dependent ion channel regulation in heart.Supramolecular assemblies and localized regulation of voltage-gated ion channels.Hippocampal 'zipper' slice studies reveal a necessary role for calcineurin in the increased activity of L-type Ca(2+) channels with aging.Ser1928 phosphorylation by PKA stimulates the L-type Ca2+ channel CaV1.2 and vasoconstriction during acute hyperglycemia and diabetes.Phosphorylation of Ser1928 mediates the enhanced activity of the L-type Ca2+ channel Cav1.2 by the β2-adrenergic receptor in neurons.Signaling complexes of voltage-gated calcium channelsA macromolecular trafficking complex composed of β₂-adrenergic receptors, A-Kinase Anchoring Proteins and L-type calcium channels.miRNA in the regulation of ion channel/transporter expression.L-type CaV1.2 calcium channels: from in vitro findings to in vivo function.Modulation by the BK accessory β4 subunit of phosphorylation-dependent changes in excitability of dentate gyrus granule neurons.Regulation of Ca(2+) transient by PP2A in normal and failing heart.PP2A as a master regulator of the cell cycle.
P2860
Q24311794-BC4A85CC-AE22-4D53-AF7E-0560FAB3023DQ24675495-239DC404-D84D-4DCB-9BD4-BF4A45271D21Q26776182-A88BDB16-F1ED-489F-8A0F-D9CCC79B6839Q26828050-9076F9E9-C1B5-4ACE-8F36-92DFCE5A376AQ27678559-17AD7FCC-3C46-45EC-BBB2-5049874AA281Q27683002-02076153-A8A1-4171-80AC-7AC9B5CA2CF8Q28117385-E7B45E5B-2243-4A96-A747-2BE9A9CC660CQ28505912-B5438EBF-14EF-42E3-A6BC-A8623F4243BDQ28567111-A2458582-5E59-4C96-A7A6-04C89EB8D1D4Q28576891-AEF754A8-BFFE-4DEF-B2D9-C43521DCE91DQ28581205-DF21B113-9CA9-4C99-9C28-C4DC4B0B58B5Q28588371-6E144885-2420-4059-A3D6-D34B57DBB6E4Q34098896-EDA526FB-3312-4138-824C-4355A29FDBF3Q34513550-0A722FAE-876D-4365-AAC9-F7DE4A45B4CEQ34634141-2BE29852-0797-404C-A834-A652F30760D2Q34787777-B9F03558-AA84-4A13-A03B-4DB99186A018Q35002868-AE592B1B-92D3-4E7E-A174-1030BAE2C6A4Q35834456-7224CFB7-4C78-49FC-8593-82554DDFD196Q35994868-7DB8048D-EB2F-4130-9CD6-16E68B555CCDQ36062292-B1B19D36-B847-4E67-9555-D1D55537CD72Q36177209-493FB98D-FEBA-4B5C-8E10-2CE6D812DE47Q36507205-6307677D-FF91-4BF3-B1DD-D4A42046A975Q36837883-07C26E97-E689-4DD2-B43E-74E9742B0F26Q36869603-E2F49C14-431C-4621-85CE-B28B89644DB5Q36879581-D4D77DD8-CB7F-4569-BF2C-01A1D715A402Q36929153-EA702473-E6DB-4AEE-BE43-9AC75EAFF42FQ37086451-DD519B13-BA58-42FB-AA32-8C841BF85C3FQ37259560-1452C427-BAF6-4775-9B11-A999AED81403Q37315915-C9CDF9AF-BE9B-48D9-8880-8176D9F24D83Q37322293-0995D421-0F99-4F89-8F1B-582498A5A7BCQ37480434-C1FF5C48-A7AA-4EEB-BEA9-809E89CA7770Q37631275-57F5C788-1F3E-40E9-8BBB-5CF3D9D24907Q37643798-83A55A46-165E-4A64-8FAD-2F52B52B277CQ37915192-C1D7D419-6E2C-40CA-8F7B-6A7195140F0EQ38096009-4F3105D5-3639-4122-9D39-718153DFD66DQ38110520-B6C8F491-CEFE-4A8E-BF2F-E038FDC5FAEEQ38175138-33A5DECF-5A8F-4E2F-B195-605C0454D7E6Q38341387-9BF482DD-A357-482F-B0EA-D01660966871Q38358069-64707D7C-5278-4E48-B41B-C9F24F4BAE86Q38746849-E6899B94-81F0-41FD-9CE8-D2CC571A90B7
P2860
Binding of protein phosphatase 2A to the L-type calcium channel Cav1.2 next to Ser1928, its main PKA site, is critical for Ser1928 dephosphorylation
description
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2006
@ast
im März 2006 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2006/03/14)
@sk
vědecký článek publikovaný v roce 2006
@cs
wetenschappelijk artikel (gepubliceerd op 2006/03/14)
@nl
наукова стаття, опублікована в березні 2006
@uk
مقالة علمية (نشرت في 14-3-2006)
@ar
name
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@ast
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@en
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@nl
type
label
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@ast
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@en
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@nl
prefLabel
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@ast
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@en
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@nl
P2093
P356
P1433
P1476
Binding of protein phosphatase ...... for Ser1928 dephosphorylation
@en
P2093
Aruni S. Arachchige Don
Duane D. Hall
Gerald W. Zamponi
Jawed Hamid
Joel A. Feekes
Johannes W. Hell
Mary C. Horne
Stefan Strack
P304
P356
10.1021/BI051593Z
P407
P577
2006-03-14T00:00:00Z