Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.
about
Arrestins: ubiquitous regulators of cellular signaling pathwaysbeta-Arrestins bind and decrease cell-surface abundance of the Na+/H+ exchanger NHE5 isoformThe structural basis of arrestin-mediated regulation of G-protein-coupled receptorsThe retromer subunit Vps26 has an arrestin fold and binds Vps35 through its C-terminal domainAnalyzing the roles of multi-functional proteins in cells: The case of arrestins and GRKsCrystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual SubtypesHow genetic errors in GPCRs affect their function: Possible therapeutic strategiesOpposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association.Rhodopsin TM6 can interact with two separate and distinct sites on arrestin: evidence for structural plasticity and multiple docking modes in arrestin-rhodopsin bindingFission yeast arrestin-related trafficking adaptor, Arn1/Any1, is ubiquitinated by Pub1 E3 ligase and regulates endocytosis of Cat1 amino acid transporter.Arrestin-related proteins mediate pH signaling in fungi.Identification of receptor binding-induced conformational changes in non-visual arrestins.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.The effect of arrestin conformation on the recruitment of c-Raf1, MEK1, and ERK1/2 activationMonomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 bindingDifferential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin.G-protein-coupled receptor phosphorylation: where, when and by whom.Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins.Identification of arrestin-3-specific residues necessary for JNK3 kinase activationA single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding.The functional cycle of visual arrestins in photoreceptor cells.Conformational dynamics of helix 8 in the GPCR rhodopsin controls arrestin activation in the desensitization process.Each rhodopsin molecule binds its own arrestinRole of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestinsConformation of receptor-bound visual arrestin.Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsinVisual arrestin binding to microtubules involves a distinct conformational changeThe differential engagement of arrestin surface charges by the various functional forms of the receptor.Binding between a distal C-terminus fragment of cannabinoid receptor 1 and arrestin-2.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.GPCR monomers and oligomers: it takes all kinds.Regulation of arrestin binding by rhodopsin phosphorylation level.How and why do GPCRs dimerize?MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization.Rich tapestry of G protein-coupled receptor signaling and regulatory mechanisms.Location, location, location...site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling.The arrestin fold: variations on a theme.The role of arrestin alpha-helix I in receptor binding.Custom-designed proteins as novel therapeutic tools? The case of arrestins.
P2860
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P2860
Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Mapping the arrestin-receptor ...... cificity of arrestin proteins.
@en
type
label
Mapping the arrestin-receptor ...... cificity of arrestin proteins.
@en
prefLabel
Mapping the arrestin-receptor ...... cificity of arrestin proteins.
@en
P2093
P2860
P356
P1476
Mapping the arrestin-receptor ...... cificity of arrestin proteins.
@en
P2093
Jeffrey L Benovic
M Marlene Hosey
Sergey A Vishnivetskiy
Vsevolod V Gurevich
P2860
P304
P356
10.1074/JBC.M308834200
P407
P577
2003-10-06T00:00:00Z