Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2.
about
The structural basis of arrestin-mediated regulation of G-protein-coupled receptorsA dopamine D2 receptor mutant capable of G protein-mediated signaling but deficient in arrestin bindingSignal transduction by protease-activated receptorsHuman chorionic gonadotropin stimulates trophoblast invasion through extracellularly regulated kinase and AKT signaling.ARF6: a newly appreciated player in G protein-coupled receptor desensitization.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.The functional cycle of visual arrestins in photoreceptor cells.Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors.Arrestin-dependent but G-protein coupled receptor kinase-independent uncoupling of D2-dopamine receptors.Critical role of the central 139-loop in stability and binding selectivity of arrestin-1.G protein-coupled receptor kinase-mediated phosphorylation regulates post-endocytic trafficking of the D2 dopamine receptor.Location, location, location...site-specific GPCR phosphorylation offers a mechanism for cell-type-specific signalling.Sphingosine 1-Phosphate Receptor 1 Signaling in Mammalian Cells.CK2 phosphorylation of an acidic Ser/Thr di-isoleucine motif in the Na+/H+ exchanger NHE5 isoform promotes association with beta-arrestin2 and endocytosis.The effect of phosphorylation on arrestin-rhodopsin interaction in the squid visual system.Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteins.Targeting individual GPCRs with redesigned nonvisual arrestins.Termination of protease-activated receptor-1 signaling by beta-arrestins is independent of receptor phosphorylation.Dopamine D1 receptor interaction with arrestin3 in neostriatal neurons.Intracellular Trafficking of Gonadotropin Receptors in Health and Disease.
P2860
Q24657537-3B979DCF-9081-45F0-86ED-85D6983CDFB5Q28569075-6E2FD926-9D70-4216-A1DD-357717D58DD1Q33870369-41104C06-6757-4107-9491-6D4DC77C85EDQ34280674-8E5CD0BE-8463-4EB3-855C-3EB0A9D39BE7Q34688600-8EF2B217-E186-4083-AACC-B0B7914FEA92Q34735704-51C111B8-4C26-4959-9A83-6212355480D7Q35085144-8B126AF9-8E46-4376-9594-F96AEBA39E61Q35387361-8926534E-6B29-4A1E-A4F7-F13C47AD8AFFQ35841895-3CCC6527-E8AD-4729-ACDA-2981F783B8C0Q36779793-76FF8668-5A36-41F0-8156-7CC9195A7997Q36796795-3B58721E-4071-4DAE-AB0B-A66273BDB19AQ37200868-464B17C7-3932-4D77-ADC5-4D5CBAD27785Q37209196-2F8C6571-94DC-4442-B313-C5B1DF41DCEBQ39152899-BF904E15-319A-4E2C-9242-80C228A74AFBQ39597237-F31CFE19-CD1E-4D6A-AEA7-C05A3CC25651Q40534961-4FAD2EEA-4F4F-4E20-8161-3165A956AFBEQ40628650-53699F93-B33A-43CA-A8D8-EC88B8B9B826Q41872788-322ABFDA-4DEC-4209-B271-1BBDEF553D83Q44709098-F4AAE696-FCE4-471D-969C-C01DEC712736Q46386547-07415A96-AB45-4E2E-B5A8-F10AFF6534ADQ47612221-401A0AC2-121E-4A4E-8DFA-25FA981B7227
P2860
Aspartic acid 564 in the third cytoplasmic loop of the luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
2002年论文
@zh
2002年论文
@zh-cn
name
Aspartic acid 564 in the third ...... nt interaction with arrestin2.
@en
type
label
Aspartic acid 564 in the third ...... nt interaction with arrestin2.
@en
prefLabel
Aspartic acid 564 in the third ...... nt interaction with arrestin2.
@en
P2093
P2860
P356
P1476
Aspartic acid 564 in the third ...... nt interaction with arrestin2.
@en
P2093
Anita Preninger
Asgerally T Fazleabas
Heidi E Hamm
Lutz Birnbaumer
Marie-France Bader
Mary Hunzicker-Dunn
Sutapa Mukherjee
Vsevolod V Gurevich
P2860
P304
17916-17927
P356
10.1074/JBC.M110479200
P407
P577
2002-02-26T00:00:00Z