Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2. - Wikidata - awgldk - TriplyDB

Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2.

Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2.

http://www.wikidata.org/entity/Q36861467

about

Regulation of renal urea transport by vasopressin Large-scale phosphoproteomic analysis of membrane proteins in renal proximal and distal tubule The Trafficking of the Water Channel Aquaporin-2 in Renal Principal Cells-a Potential Target for Pharmacological Intervention in Cardiovascular Diseases A Minireview on Vasopressin-regulated Aquaporin-2 in Kidney Collecting Duct Cells A novel therapeutic effect of statins on nephrogenic diabetes insipidus Regulation of nephron water and electrolyte transport by adenylyl cyclases X-ray structure of human aquaporin 2 and its implications for nephrogenic diabetes insipidus and trafficking Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating The water channel aquaporin-1 partitions into exosomes during reticulocyte maturation: implication for the regulation of cell volume Serine 269 phosphorylated aquaporin-2 is targeted to the apical membrane of collecting duct principal cells cAMP stimulates apical exocytosis of the renal Na(+)-K(+)-2Cl(-) cotransporter NKCC2 in the thick ascending limb: role of protein kinase A Identification of phosphorylation-dependent binding partners of aquaporin-2 using protein mass spectrometry Impaired water reabsorption in mice deficient in the type VI adenylyl cyclase (AC6)Global analysis of the effects of the V2 receptor antagonist satavaptan on protein phosphorylation in collecting duct A plate reader-based method for cell water permeability measurement.Phosphorylation of aquaporin-2 regulates its endocytosis and protein-protein interactions.Phosphoproteomic profiling reveals vasopressin-regulated phosphorylation sites in collecting duct Quantitative phosphoproteomic analysis reveals vasopressin V2-receptor-dependent signaling pathways in renal collecting duct cells.Role of cAMP/PKA signaling cascade in vasopressin-induced trafficking of TRPC3 channels in principal cells of the collecting duct.Quantitative analysis of aquaporin-2 phosphorylation.Use of LC-MS/MS and Bayes' theorem to identify protein kinases that phosphorylate aquaporin-2 at Ser256.Sensing, signaling and sorting events in kidney epithelial cell physiology.Megalin-mediated specific uptake of chitosan/siRNA nanoparticles in mouse kidney proximal tubule epithelial cells enables AQP1 gene silencing.Vasopressin increases phosphorylation of Ser84 and Ser486 in Slc14a2 collecting duct urea transporters.Differential, phosphorylation dependent trafficking of AQP2 in LLC-PK1 cells Quantitative protein and mRNA profiling shows selective post-transcriptional control of protein expression by vasopressin in kidney cells.Adenylate cyclase 6 determines cAMP formation and aquaporin-2 phosphorylation and trafficking in inner medulla.Bilateral ureteral obstruction induces early downregulation and redistribution of AQP2 and phosphorylated AQP2.Vasopressin-independent targeting of aquaporin-2 by selective E-prostanoid receptor agonists alleviates nephrogenic diabetes insipidus.Expression of a dominant negative PKA mutation in the kidney elicits a diabetes insipidus phenotype Polarized Trafficking of AQP2 Revealed in Three Dimensional Epithelial Culture.Opposing Effects of cAMP and T259 Phosphorylation on Plasma Membrane Diffusion of the Water Channel Aquaporin-5 in Madin-Darby Canine Kidney Cells NSAIDs Alter Phosphorylated Forms of AQP2 in the Inner Medullary Tip.NHLBI-AbDesigner: an online tool for design of peptide-directed antibodies.A Systems Level Analysis of Vasopressin-mediated Signaling Networks in Kidney Distal Convoluted Tubule Cells.Tamm-Horsfall protein and urinary exosome isolation.Phosphoproteomics of vasopressin signaling in the kidney.Characterization of the putative phosphorylation sites of the AQP2 C terminus and their role in AQP2 trafficking in LLC-PK1 cells.Systemic PPARγ deletion causes severe disturbance in fluid homeostasis in mice.Deep proteomic profiling of vasopressin-sensitive collecting duct cells. II. Bioinformatic analysis of vasopressin signaling.

P2860

Q24612409-B4B4AA23-6E39-43AE-9374-6D3D47C4F4A8 Q24619838-45B7A0A0-4997-458C-BD75-ED55BC17FBB7 Q26768170-ED4C046E-60AE-4233-A57C-DDBEF01B73AE Q26799315-59EEC8E8-42F2-4E85-999A-00207517DFCE Q27005638-CFCF2A96-D7BF-41C3-9F21-944AFD0F9DED Q27023655-7B7AF4B6-BBC8-4802-9642-6C3D138A5794 Q27683366-4BDADE42-4F36-46D7-80F7-239ED1A0B5E4 Q27967637-60F5B1A6-E418-4F4B-924D-BDC966E439D9 Q28510229-CAF5543D-B585-4B86-A27C-0B9A27050591 Q28564385-01D4AE98-9DAC-488B-862C-DE9A3690ED58 Q28570785-F6C6C5CC-42F8-41A2-935E-F450A504DE96 Q28578771-5D0E8ABD-54E3-4D28-A347-5D4475F57BAF Q28590267-AB296411-3BDC-4132-A5ED-044E1B1B287D Q28659266-493E949B-74E3-4ED2-A522-58D42D8D2AC9 Q30877393-E4F195F6-E6A4-44FA-822E-21C71DBD801D Q33591562-831F2515-1727-4E71-BDF4-96559D15FDBD Q33711260-CD194EAA-4A23-4210-B94E-524CFB0B06C7 Q33734769-C44764E5-4B3F-4687-9FC8-3FD126F4DF2D Q33783934-E2D684A1-65FC-4C0E-A718-E28993CDD781 Q33783962-13786A7A-4059-47AC-8864-99155250B207 Q33913030-C540A1D3-5E59-439D-80C0-E8491FB738BB Q33961141-03690482-13D5-4F22-BBC5-1545C80A32ED Q34080235-A777B6E1-8F64-45D1-9DBC-B85C5D5402C1 Q34149581-29A7767E-93ED-48A6-940C-B2111E2C74ED Q34189252-18B8744F-FAB9-49EA-A11B-8DA7F36873E0 Q34454965-AA189834-85B9-4BAC-AEFE-76C17F0157FF Q34457128-0B849B0F-1C78-41C3-8838-4BBBCA15B103 Q35086975-7C6F16F6-B0B6-45D0-A540-62100BECA61C Q35149581-C39E8802-C3D0-4FAF-993B-697D3B760619 Q35178630-70F7D323-AE3A-4079-8009-1C17D95F4A25 Q35683439-6A87E8E0-F03F-4CCD-B085-B8A3C903F26E Q35719719-0A227015-D803-4C38-9BF2-1301FA091660 Q35827119-48CB075F-CDDE-470D-85F1-7C215F3EA07D Q35895715-C4AAA2E5-0EAC-4422-9714-AC2189E40F6A Q35913316-13CAE5EF-7844-4C2B-986F-B58E60116C96 Q36100258-A9ADE5DC-6A27-44D5-8745-85B543D838CA Q36124263-FB140121-66C6-4714-9E9F-6334FCB7BD32 Q36174490-E4C32BD5-331E-4834-A0B7-879F3A21A3C3 Q36237301-E48747D1-77DC-4836-BBED-249F816B41F9 Q36381794-F2762930-732B-4319-8A5E-6C8340799770

P2860

Vasopressin-stimulated increase in phosphorylation at Ser269 potentiates plasma membrane retention of aquaporin-2.

http://www.wikidata.org/entity/Q36861467

description

2008 nî lūn-bûn

@nan

2008年の論文

@ja

2008年論文

@yue

2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

@zh-mo

2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Vasopressin-stimulated increas ...... rane retention of aquaporin-2.

@en

type

label

Vasopressin-stimulated increas ...... rane retention of aquaporin-2.

@en

prefLabel

Vasopressin-stimulated increas ...... rane retention of aquaporin-2.

@en

P1433

Q36861467-26FEE1AE-019A-4B7F-A2F6-33021410685A

P1476

Q36861467-22230DAA-7FFD-42F3-AEB2-20ACB03B1418

P2093

Q36861467-02CB9373-D9A0-4BA1-802D-2B38DBA3AD9A

Q36861467-0D30A041-4F6B-4A2D-A1F4-19CBDF978EEC

Q36861467-881F22BB-E0CE-4ADE-9051-FA76583ED2BD

Q36861467-926C557B-18D2-4219-B9EC-2ED92BE43067

Q36861467-DE013524-F104-4FC9-86C1-B9005D3329BE

Q36861467-E62D22FB-794E-403F-A01A-3EFB0F51EEB9

P2860

Q36861467-0028D652-F8B6-45BC-872C-5216AE3CF2E0

Q36861467-049B84D8-FAB9-4D33-A233-BC4DCD9A1444

Q36861467-116B332A-100D-40F3-B686-B7D52559A5BD

Q36861467-164996C9-7CED-4E44-83B3-33CA96B97C9F

Q36861467-16E1C24E-BEF2-4C95-9075-89D4A4929AFD

Q36861467-1DB02521-F41F-4D15-8C96-20C99280F811

Q36861467-1EB1AABE-602C-42D2-9A2D-CC480BEAD050

Q36861467-2A768AA7-2A1D-4264-8D6E-AB71C3891492

Q36861467-31295560-99DE-4A7B-8FF4-B6AE207EA9E4

Q36861467-415F523E-131B-4357-9F39-BC8F6E47378A

P304

Q36861467-95165F0B-E6BD-4508-8BD8-CD629B1125BE

P31

Q36861467-A853939E-3B37-401E-AB2C-882B2C6DC7AC

P356

Q36861467-B0945F49-B794-4396-83C2-425529C3A7B3

P407

Q36861467-3049FFF8-EF63-4107-811C-CE838076C1BF

P433

Q36861467-C8012427-C9A8-4A2D-9F0F-DE6DCFBACB56

P478

Q36861467-A5E89960-28E9-4F5F-B9FD-9E63527D0A55

P50

Q36861467-0008FF31-7A75-45AD-B44C-D79CBD9077F5

Q36861467-28FB91A2-DB6D-4560-B07C-06082140EFBE

Q36861467-9E0C64EE-6B45-4C70-8B93-DCF7E4943FEA

Q36861467-B0C673C9-6623-4980-94AD-F5539AC6A82C

P577

Q36861467-A1CD7D03-490C-4126-A69B-082BA0B9AACE

P5875

Q36861467-69DEB363-F3FB-4CF3-846B-68D51AE5EA63

P698

Q36861467-9485C3DA-131F-47E6-9B59-00D1D628B63A

P921

Q36861467-0e1a7fa3-f25a-4a5d-b2e6-66c6df72d7d6

Q36861467-5080BAEC-5298-48AD-B8E8-C352A2903F68

P932

Q36861467-1BDF5A1A-2B92-4FF7-8B6A-5945C0459CA7

P356

P1433

Journal of Biological Chemistry

P1476

Vasopressin-stimulated increas ...... brane retention of aquaporin-2

@en

P2093

Bradley W McDill

http://www.w3.org/2001/XMLSchema#string

Brigitte Simons

http://www.w3.org/2001/XMLSchema#string

Feng Chen

http://www.w3.org/2001/XMLSchema#string

Hanne B Moeller

http://www.w3.org/2001/XMLSchema#string

Jason D Hoffert

http://www.w3.org/2001/XMLSchema#string

Mark A Knepper

http://www.w3.org/2001/XMLSchema#string

P2860

Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers.

Control of beta-catenin phosphorylation/degradation by a dual-kinase mechanism

The ins and outs of aquaporin-2 trafficking

Phosphorylation of stargazin by protein kinase A regulates its interaction with PSD-95

Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus

Heat shock protein 70 interacts with aquaporin-2 and regulates its trafficking

Non-muscle myosin II and myosin light chain kinase are downstream targets for vasopressin signaling in the renal collecting duct

Aquaporin-2 trafficking is regulated by PDZ-domain containing protein SPA-1

P304

24617-24627

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1074/JBC.M803074200

http://www.w3.org/2001/XMLSchema#string

P407

P433

36

http://www.w3.org/2001/XMLSchema#string

P478

283

http://www.w3.org/2001/XMLSchema#string

P50

Robert A Fenton

Trairak Pisitkun

Dmitry Tchapyjnikov

P577

2008-07-07T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

5245819

http://www.w3.org/2001/XMLSchema#string

P698

18606813

http://www.w3.org/2001/XMLSchema#string

P921

phosphorylation

P932

2528999

http://www.w3.org/2001/XMLSchema#string