Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.
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Analyzing 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 SubtypesMultiprotein complexes of Retinitis Pigmentosa GTPase regulator (RPGR), a ciliary protein mutated in X-linked Retinitis Pigmentosa (XLRP).Transport and localization of signaling proteins in ciliated cellsDifferential distribution of proteins and lipids in detergent-resistant and detergent-soluble domains in rod outer segment plasma membranes and disks.Arrestin can act as a regulator of rhodopsin photochemistry.Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery.Robust self-association is a common feature of mammalian visual arrestin-1.Modeling the role of incisures in vertebrate phototransductionInteraction of arrestin with enolase1 in photoreceptors.A role for cytoskeletal elements in the light-driven translocation of proteins in rod photoreceptors.The functional cycle of visual arrestins in photoreceptor cells.Steric volume exclusion sets soluble protein concentrations in photoreceptor sensory cilia.Structural and functional protein network analyses predict novel signaling functions for rhodopsin.Interaction of retinal guanylate cyclase with the alpha subunit of transducin: potential role in transducin localization.Arrestin 1 and Cone Arrestin 4 Have Unique Roles in Visual Function in an All-Cone Mouse Retina.Visual arrestin binding to microtubules involves a distinct conformational changeMechanism of light-induced translocation of arrestin and transducin in photoreceptors: interaction-restricted diffusion.Subunit dissociation and diffusion determine the subcellular localization of rod and cone transducinsLight-dependent phosphorylation of Bardet-Biedl syndrome 5 in photoreceptor cells modulates its interaction with arrestin1Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions.Localization of caveolin-1 and c-src in mature and differentiating photoreceptors: raft proteins co-distribute with rhodopsin during development.Structural determinants of arrestin functionsStructure and function of the visual arrestin oligomer.Arrestins: Critical Players in Trafficking of Many GPCRs.The Diverse Roles of Arrestin Scaffolds in G Protein-Coupled Receptor Signaling.Nonvisual arrestins function as simple scaffolds assembling the MKK4-JNK3α2 signaling complexArrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity.Elucidation of inositol hexaphosphate and heparin interaction sites and conformational changes in arrestin-1 by solution nuclear magnetic resonance.Rapid degeneration of rod photoreceptors expressing self-association-deficient arrestin-1 mutant.Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked events.Interaction of ciliary disease protein retinitis pigmentosa GTPase regulator with nephronophthisis-associated proteins in mammalian retinas.
P2860
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P2860
Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
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2004年学术文章
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2004年学术文章
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2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
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2004年學術文章
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name
Direct binding of visual arres ...... ariants in rod photoreceptors.
@en
type
label
Direct binding of visual arres ...... ariants in rod photoreceptors.
@en
prefLabel
Direct binding of visual arres ...... ariants in rod photoreceptors.
@en
P2093
P2860
P356
P1476
Direct binding of visual arres ...... variants in rod photoreceptors
@en
P2093
James B Hurley
K Saidas Nair
Matthew J Kennedy
Susan M Hanson
Vladlen Z Slepak
P2860
P304
41240-41248
P356
10.1074/JBC.M406768200
P407
P577
2004-07-21T00:00:00Z