The alpha1-beta-subunit interaction that modulates calcium channel activity is reversible and requires a competent alpha-interaction domain.
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Structure-function of proteins interacting with the α1 pore-forming subunit of high-voltage-activated calcium channelsVoltage gated calcium channels negatively regulate protective immunity to Mycobacterium tuberculosisDirect interaction of CaVβ with actin up-regulates L-type calcium currents in HL-1 cardiomyocytesBARP suppresses voltage-gated calcium channel activity and Ca2+-evoked exocytosisStructural and biophysical analyses of the skeletal dihydropyridine receptor β subunit β1a reveal critical roles of domain interactions for stability.Homodimerization of the Src homology 3 domain of the calcium channel β-subunit drives dynamin-dependent endocytosis.The ß subunit of voltage-gated Ca2+ channelsFunctional dissection of the intramolecular Src homology 3-guanylate kinase domain coupling in voltage-gated Ca2+ channel beta-subunits.Functional modularity of the beta-subunit of voltage-gated Ca2+ channels.The N-terminal domain tethers the voltage-gated calcium channel β2e-subunit to the plasma membrane via electrostatic and hydrophobic interactionsOrientation of palmitoylated CaVbeta2a relative to CaV2.2 is critical for slow pathway modulation of N-type Ca2+ current by tachykinin receptor activation.The Ca2+ channel beta subunit determines whether stimulation of Gq-coupled receptors enhances or inhibits N currentStapled Voltage-Gated Calcium Channel (CaV) α-Interaction Domain (AID) Peptides Act As Selective Protein-Protein Interaction Inhibitors of CaV FunctionPotentiation of high voltage-activated calcium channels by 4-aminopyridine depends on subunit composition.The alpha1 subunit EGL-19, the alpha2/delta subunit UNC-36, and the beta subunit CCB-1 underlie voltage-dependent calcium currents in Caenorhabditis elegans striated muscle.Neuronal ClC-3 Splice Variants Differ in Subcellular Localizations, but Mediate Identical Transport Functions.The guanylate kinase domain of the beta-subunit of voltage-gated calcium channels suffices to modulate gating.Molecular basis for zinc transporter 1 action as an endogenous inhibitor of L-type calcium channels.Structure and function of the β subunit of voltage-gated Ca²⁺ channels.The role of auxiliary subunits for the functional diversity of voltage-gated calcium channels.Nuclear life of the voltage-gated Cacnb4 subunit and its role in gene transcription regulation.Alanine-scanning mutagenesis defines a conserved energetic hotspot in the CaValpha1 AID-CaVbeta interaction site that is critical for channel modulation.Mutations of nonconserved residues within the calcium channel alpha1-interaction domain inhibit beta-subunit potentiation.A short polybasic segment between the two conserved domains of the β2a-subunit modulates the rate of inactivation of R-type calcium channel.Single-channel monitoring of reversible L-type Ca(2+) channel Ca(V)α(1)-Ca(V)β subunit interaction.Molecular determinants of the CaVbeta-induced plasma membrane targeting of the CaV1.2 channel.Stable incorporation versus dynamic exchange of β subunits in a native Ca2+ channel complex.The Src homology 3 domain of the beta-subunit of voltage-gated calcium channels promotes endocytosis via dynamin interaction.Rapid Turnover of the Cardiac L-Type Ca1.2 Channel by Endocytic Recycling Regulates Its Cell Surface Availability
P2860
Q26864613-D248B061-A35C-4BA3-821A-984503050475Q27349699-DDF65019-DA0E-43AC-80D7-A0485D6E1B09Q28119053-19365105-7CDA-4A3A-9195-9DD6915FAF2FQ28512209-88FDC98C-672C-4959-B0D2-13805B10B488Q30008756-BFD90BEC-0F98-4F49-8623-572CA1149C6EQ30155579-0892062D-E1FA-4774-8AB7-FC6B76AF8E25Q30155988-2AA0D01C-533A-43AA-AA1C-1382CE3ADBB8Q30157263-BC8B20A6-116C-4247-B694-DE9FD2DB8DEBQ30157978-A3F553F6-E24D-478E-AFF6-EB6321DB6DF9Q30405831-3DC9C71E-5CD4-41F1-8F0B-B96EE2A5614CQ30436277-A89F8BA4-AF91-4627-832E-2B9CBC1DBFDEQ30436280-F8BA0149-CF8C-4F5C-BF42-E1D8233A4296Q33827087-078D92A4-6F9F-4C3F-8D21-C59799AB4C59Q34573948-B9144F53-BA3C-411B-9FDB-47002B520E1DQ35378929-7316ACA5-D488-4E44-BE9A-09EAFF961996Q36283490-FEC9E317-2EE5-4CE7-84A7-281E7E5909B6Q36893771-B1A0424E-23BA-4F73-81FF-EEEFC5D83114Q37431997-63669856-ADC0-43B1-A41D-AE769272FF53Q38043712-8DE9F576-3F01-47D9-A0EC-C81CCA3844CAQ38395145-88DCE4BE-E702-43C9-9247-FE47699AF98BQ41217397-8CC47141-AD9D-4AB7-AAAC-2B1297A9325CQ41869908-7A6256E4-103A-4712-8E69-15A9FED2FDAFQ41911426-AB0AA960-90A6-4EFB-838B-6107315E53E4Q42532197-117C6CF8-5158-4124-92B1-7CA8D36166D3Q42591638-1FFBD2DF-0911-4F6E-90D2-8962DB672C1BQ42724754-51EC149A-AAF9-46A1-874D-F2F73A995C11Q42849718-23D244FF-E00A-4F40-BEEF-2CF0986C55D1Q50642668-69BDB48F-A736-40AE-8075-9DD8F00C3675Q58772650-F123103E-1B5E-45BF-83A6-8AD7CA5A2458
P2860
The alpha1-beta-subunit interaction that modulates calcium channel activity is reversible and requires a competent alpha-interaction domain.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh-hant
name
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@en
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@nl
type
label
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@en
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@nl
prefLabel
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@en
The alpha1-beta-subunit intera ...... tent alpha-interaction domain.
@nl
P2860
P356
P1476
The alpha1-beta-subunit intera ...... etent alpha-interaction domain
@en
P2093
Alan Neely
Jennie Garcia-Olivares
P2860
P304
24104-24110
P356
10.1074/JBC.M605930200
P407
P577
2006-06-22T00:00:00Z