Vasopressin regulates renal water homeostasis via Aquaporins (Homo sapiens)

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cytosol cytosol cytoplasmic vesicle lumen Filtrate Bloodstream Proximal tubule, descending thin limb of Henle Collecting duct H2O H2O AQP1 tetramer H2O AVP(20-28) AVPR2 AVPR2:AVP(20-28) G-alpha(s):GDP:G-beta:G-gamma AVPR2:AVP:G-alpha(s):GDP:G-beta:G-gamma GTP GDP AVPR2:AVP:G-alpha(s):GTP:G-beta:G-gamma G-protein alpha (s):GTP Gs-activated adenylate cyclase ATP PPi cAMP PKA tetramer cAMP:PKA regulatory subunit PKA catalytic subunit AQP2 tetramer p-S256-AQP2 p-S256-AQP2 tetramer H2O AQP3 tetramer H2O AQP4 tetramer H2O H2O Adenylate cyclase (Mg2+ cofactor) G-alpha(s):GTP:G-beta:G-gamma G-beta:G-gamma (candidates) MYO5B:RABFIP2:RAB11A AQP1 AVP(20-28) AVPR2 GNGT1 GNG13 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNGT2 GNG10 GNG11 GNG12 GNB3 GNB4 GNB1 GNB2 GNB5 GNAS2 GNAS1 GDP GNGT1 GNG13 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNGT2 GNG10 GNG11 GNG12 GNB3 GNB4 GNB1 GNB2 GNB5 GNAS2 GNAS1 GDP AVP(20-28) AVPR2 AVP(20-28) AVPR2 GNAS2 GNAS1 GTP GNGT1 GNG13 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNGT2 GNG10 GNG11 GNG12 GNB3 GNB4 GNB1 GNB2 GNB5 GNAS2 GNAS1 GTP GNAS2 GNAS1 GTP Mg2+ ADCY2 ADCY3 ADCY4 ADCY6 ADCY7 ADCY9 ADCY1 ADCY5 ADCY8 PRKAR1A PRKAR1B PRKAR2A PRKAR2B PRKACA PRKACB PRKACG PRKAR1A PRKAR1B PRKAR2A PRKAR2B cAMP PRKACA PRKACB PRKACG AQP2 p-S256-AQP2 p-S256-AQP2 AQP3 AQP4 Mg2+ ADCY2 ADCY3 ADCY4 ADCY6 ADCY7 ADCY9 ADCY1 ADCY5 ADCY8 GNAS2 GNAS1 GTP GNGT1 GNG13 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNGT2 GNG10 GNG11 GNG12 GNB3 GNB4 GNB1 GNB2 GNB5 GNGT1 GNG13 GNG2 GNG3 GNG4 GNG5 GNG7 GNG8 GNGT2 GNG10 GNG11 GNG12 GNB3 GNB4 GNB1 GNB2 GNB5 MYO5B RAB11FIP2 RAB11A GTP Name: Vasopressin regulates renal water homeostasis via Aquaporins Organism: Homo sapiens


In the kidney water and solutes are passed out of the bloodstream and into the proximal tubule via the slit-like structure formed by nephrin in the glomerulus. Water is reabsorbed from the filtrate during its transit through the proximal tubule, the descending loop of Henle, the distal convoluted tubule, and the collecting duct.
Aquaporin-1 (AQP1) in the proximal tubule and the descending thin limb of Henle is responsible for about 90% of reabsorption (as estimated from mouse knockouts of AQP1). AQP1 is located on both the apical and basolateral surface of epithelial cells and thus transports water through the epithelium and back into the bloodstream.
In the collecting duct epithelial cells have AQP2 on their apical surface and AQP3 and AQP4 on their basolateral surface to transport water across the epithelium. The permeability of the epithelium is regulated by vasopressin, which activates the phosphorylation and subsequent translocation of AQP2 from intracellular vesicles to the plasma membrane.

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  1. Preston GM, Carroll TP, Guggino WB, Agre P.; ''Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein.''; PubMed
  2. Roudier N, Bailly P, Gane P, Lucien N, Gobin R, Cartron JP, Ripoche P.; ''Erythroid expression and oligomeric state of the AQP3 protein.''; PubMed
  3. Ecelbarger CA, Terris J, Frindt G, Echevarria M, Marples D, Nielsen S, Knepper MA.; ''Aquaporin-3 water channel localization and regulation in rat kidney.''; PubMed
  4. Hub JS, de Groot BL.; ''Mechanism of selectivity in aquaporins and aquaglyceroporins.''; PubMed
  5. Ma T, Frigeri A, Hasegawa H, Verkman AS.; ''Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter.''; PubMed
  6. Marples D, Barber B, Taylor A.; ''Effect of a dynein inhibitor on vasopressin action in toad urinary bladder.''; PubMed
  7. Moeller HB, MacAulay N, Knepper MA, Fenton RA.; ''Role of multiple phosphorylation sites in the COOH-terminal tail of aquaporin-2 for water transport: evidence against channel gating.''; PubMed
  8. Digby GJ, Lober RM, Sethi PR, Lambert NA.; ''Some G protein heterotrimers physically dissociate in living cells.''; PubMed
  9. Nielsen S, King LS, Christensen BM, Agre P.; ''Aquaporins in complex tissues. II. Subcellular distribution in respiratory and glandular tissues of rat.''; PubMed
  10. Gromada J, Brock B, Schmitz O, Rorsman P.; ''Glucagon-like peptide-1: regulation of insulin secretion and therapeutic potential.''; PubMed
  11. Mobasheri A, Wray S, Marples D.; ''Distribution of AQP2 and AQP3 water channels in human tissue microarrays.''; PubMed
  12. Nedvetsky PI, Stefan E, Frische S, Santamaria K, Wiesner B, Valenti G, Hammer JA, Nielsen S, Goldenring JR, Rosenthal W, Klussmann E.; ''A Role of myosin Vb and Rab11-FIP2 in the aquaporin-2 shuttle.''; PubMed
  13. Hendriks G, Koudijs M, van Balkom BW, Oorschot V, Klumperman J, Deen PM, van der Sluijs P.; ''Glycosylation is important for cell surface expression of the water channel aquaporin-2 but is not essential for tetramerization in the endoplasmic reticulum.''; PubMed
  14. Cohly HH, Isokpehi R, Rajnarayanan RV.; ''Compartmentalization of aquaporins in the human intestine.''; PubMed
  15. Bachinsky DR, Sabolic I, Emmanouel DS, Jefferson DM, Carone FA, Brown D, Perrone RD.; ''Water channel expression in human ADPKD kidneys.''; PubMed
  16. Ho JD, Yeh R, Sandstrom A, Chorny I, Harries WE, Robbins RA, Miercke LJ, Stroud RM.; ''Crystal structure of human aquaporin 4 at 1.8 A and its mechanism of conductance.''; PubMed
  17. Takata K, Matsuzaki T, Tajika Y, Ablimit A, Hasegawa T.; ''Localization and trafficking of aquaporin 2 in the kidney.''; PubMed
  18. Doyle ME, Egan JM.; ''Mechanisms of action of glucagon-like peptide 1 in the pancreas.''; PubMed
  19. Liu J, Wess J.; ''Different single receptor domains determine the distinct G protein coupling profiles of members of the vasopressin receptor family.''; PubMed
  20. Erlenbach I, Wess J.; ''Molecular basis of V2 vasopressin receptor/Gs coupling selectivity.''; PubMed
  21. Frigeri A, Gropper MA, Turck CW, Verkman AS.; ''Immunolocalization of the mercurial-insensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes.''; PubMed
  22. de Mattia F, Savelkoul PJ, Kamsteeg EJ, Konings IB, van der Sluijs P, Mallmann R, Oksche A, Deen PM.; ''Lack of arginine vasopressin-induced phosphorylation of aquaporin-2 mutant AQP2-R254L explains dominant nephrogenic diabetes insipidus.''; PubMed
  23. King LS, Nielsen S, Agre P.; ''Aquaporins in complex tissues. I. Developmental patterns in respiratory and glandular tissues of rat.''; PubMed
  24. Sorani MD, Zador Z, Zador Z, Hurowitz E, Yan D, Giacomini KM, Manley GT.; ''Novel variants in human Aquaporin-4 reduce cellular water permeability.''; PubMed
  25. Dessauer CW, Chen-Goodspeed M, Chen J.; ''Mechanism of Galpha i-mediated inhibition of type V adenylyl cyclase.''; PubMed
  26. Burghardt B, Elkaer ML, Kwon TH, Rácz GZ, Varga G, Steward MC, Nielsen S.; ''Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas.''; PubMed
  27. Mobasheri A, Marples D, Young IS, Floyd RV, Moskaluk CA, Frigeri A.; ''Distribution of the AQP4 water channel in normal human tissues: protein and tissue microarrays reveal expression in several new anatomical locations, including the prostate gland and seminal vesicles.''; PubMed
  28. Mohr E, Hillers M, Ivell R, Haulica ID, Richter D.; ''Expression of the vasopressin and oxytocin genes in human hypothalami.''; PubMed
  29. Nedvetsky PI, Tamma G, Beulshausen S, Valenti G, Rosenthal W, Klussmann E.; ''Regulation of aquaporin-2 trafficking.''; PubMed
  30. Martin BR, Farndale RW, Wong SK.; ''The role of Gs in activation of adenylate cyclase.''; PubMed
  31. Tsunoda SP, Wiesner B, Lorenz D, Rosenthal W, Pohl P.; ''Aquaporin-1, nothing but a water channel.''; PubMed
  32. Nielsen S, Smith BL, Christensen EI, Knepper MA, Agre P.; ''CHIP28 water channels are localized in constitutively water-permeable segments of the nephron.''; PubMed
  33. Nielsen S, Kwon TH, Frøkiaer J, Agre P.; ''Regulation and dysregulation of aquaporins in water balance disorders.''; PubMed
  34. Echeverría V, Hinrichs MV, Torrejón M, Ropero S, Martinez J, Toro MJ, Olate J.; ''Mutagenesis in the switch IV of the helical domain of the human Gsalpha reduces its GDP/GTP exchange rate.''; PubMed
  35. Meinild AK, Klaerke DA, Zeuthen T.; ''Bidirectional water fluxes and specificity for small hydrophilic molecules in aquaporins 0-5.''; PubMed
  36. Mobasheri A, Marples D.; ''Expression of the AQP-1 water channel in normal human tissues: a semiquantitative study using tissue microarray technology.''; PubMed
  37. Kuwahara M, Gu Y, Ishibashi K, Marumo F, Sasaki S.; ''Mercury-sensitive residues and pore site in AQP3 water channel.''; PubMed
  38. Birnbaumer M, Seibold A, Gilbert S, Ishido M, Barberis C, Antaramian A, Brabet P, Rosenthal W.; ''Molecular cloning of the receptor for human antidiuretic hormone.''; PubMed
  39. Walz T, Hirai T, Murata K, Heymann JB, Mitsuoka K, Fujiyoshi Y, Smith BL, Agre P, Engel A.; ''The three-dimensional structure of aquaporin-1.''; PubMed
  40. Sasaki S, Fushimi K, Saito H, Saito F, Uchida S, Ishibashi K, Kuwahara M, Ikeuchi T, Inui K, Nakajima K.; ''Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct.''; PubMed
  41. Gullingsrud J, Kim C, Taylor SS, McCammon JA.; ''Dynamic binding of PKA regulatory subunit RI alpha.''; PubMed
  42. Nejsum LN.; ''The renal plumbing system: aquaporin water channels.''; PubMed
  43. Zeidel ML, Ambudkar SV, Smith BL, Agre P.; ''Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein.''; PubMed
  44. Thorens B, Porret A, Bühler L, Deng SP, Morel P, Widmann C.; ''Cloning and functional expression of the human islet GLP-1 receptor. Demonstration that exendin-4 is an agonist and exendin-(9-39) an antagonist of the receptor.''; PubMed
  45. Kamsteeg EJ, Heijnen I, van Os CH, Deen PM.; ''The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers.''; PubMed
  46. Lu M, Lee MD, Smith BL, Jung JS, Agre P, Verdijk MA, Merkx G, Rijss JP, Deen PM.; ''The human AQP4 gene: definition of the locus encoding two water channel polypeptides in brain.''; PubMed
  47. Lambert NA.; ''Dissociation of heterotrimeric g proteins in cells.''; PubMed
  48. Wu B, Steinbronn C, Alsterfjord M, Zeuthen T, Beitz E.; ''Concerted action of two cation filters in the aquaporin water channel.''; PubMed
  49. de Groot BL, Engel A, Grubmüller H.; ''A refined structure of human aquaporin-1.''; PubMed
  50. Denker BM, Smith BL, Kuhajda FP, Agre P.; ''Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules.''; PubMed
  51. van Balkom BW, Savelkoul PJ, Markovich D, Hofman E, Nielsen S, van der Sluijs P, Deen PM.; ''The role of putative phosphorylation sites in the targeting and shuttling of the aquaporin-2 water channel.''; PubMed
  52. Murata K, Mitsuoka K, Hirai T, Walz T, Agre P, Heymann JB, Engel A, Fujiyoshi Y.; ''Structural determinants of water permeation through aquaporin-1.''; PubMed
  53. Brito M, Guzmán L, Romo X, Soto X, Hinrichs MV, Olate J.; ''S111N mutation in the helical domain of human Gs(alpha) reduces its GDP/GTP exchange rate.''; PubMed
  54. Beitz E, Wu B, Holm LM, Schultz JE, Zeuthen T.; ''Point mutations in the aromatic/arginine region in aquaporin 1 allow passage of urea, glycerol, ammonia, and protons.''; PubMed
  55. Nielsen S, Frøkiaer J, Marples D, Kwon TH, Agre P, Knepper MA.; ''Aquaporins in the kidney: from molecules to medicine.''; PubMed
  56. Echevarria M, Windhager EE, Tate SS, Frindt G.; ''Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney.''; PubMed
  57. Bedford JJ, Leader JP, Walker RJ.; ''Aquaporin expression in normal human kidney and in renal disease.''; PubMed
  58. Sausville E, Carney D, Battey J.; ''The human vasopressin gene is linked to the oxytocin gene and is selectively expressed in a cultured lung cancer cell line.''; PubMed
  59. Katsura T, Gustafson CE, Ausiello DA, Brown D.; ''Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells.''; PubMed
  60. Huber VJ, Tsujita M, Yamazaki M, Sakimura K, Nakada T.; ''Identification of arylsulfonamides as Aquaporin 4 inhibitors.''; PubMed
  61. Tesmer JJ, Sunahara RK, Gilman AG, Sprang SR.; ''Crystal structure of the catalytic domains of adenylyl cyclase in a complex with Gsalpha.GTPgammaS.''; PubMed
  62. Winzell MS, Ahrén B.; ''G-protein-coupled receptors and islet function-implications for treatment of type 2 diabetes.''; PubMed
  63. Deen PM, Verdijk MA, Knoers NV, Wieringa B, Monnens LA, van Os CH, van Oost BA.; ''Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.''; PubMed
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93786view 06:36, 16 August 2017ReactomeTeamreactome version 61
93319view 04:20, 9 August 2017ReactomeTeamreactome version 61
88349view 09:17, 1 August 2016FehrhartOntology Term : 'water transport pathway' added !
88348view 09:16, 1 August 2016FehrhartOntology Term : 'vasopressin signaling pathway' added !
86404view 02:17, 11 July 2016ReactomeTeamreactome version 56
83089view 02:57, 18 November 2015ReactomeTeamVersion54
81747view 01:20, 26 August 2015ReactomeTeamVersion53
76842view 01:06, 17 July 2014ReactomeTeamFixed remaining interactions
76546view 04:53, 16 July 2014ReactomeTeamFixed remaining interactions
75879view 02:53, 11 June 2014ReactomeTeamRe-fixing comment source
75579view 03:41, 10 June 2014ReactomeTeamReactome 48 Update
74934view 06:46, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74578view 01:37, 30 April 2014ReactomeTeamNew pathway

External references


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NameTypeDatabase referenceComment
ADCY1 ProteinQ08828 (Uniprot-TrEMBL)
ADCY2 ProteinQ08462 (Uniprot-TrEMBL)
ADCY3 ProteinO60266 (Uniprot-TrEMBL)
ADCY4 ProteinQ8NFM4 (Uniprot-TrEMBL)
ADCY5 ProteinO95622 (Uniprot-TrEMBL)
ADCY6 ProteinO43306 (Uniprot-TrEMBL)
ADCY7 ProteinP51828 (Uniprot-TrEMBL)
ADCY8 ProteinP40145 (Uniprot-TrEMBL)
ADCY9 ProteinO60503 (Uniprot-TrEMBL)
AQP1 ProteinP29972 (Uniprot-TrEMBL)
AQP1 tetramerComplexR-HSA-432246 (Reactome)
AQP2 ProteinP41181 (Uniprot-TrEMBL)
AQP2 tetramerComplexR-HSA-432228 (Reactome)
AQP3 ProteinQ92482 (Uniprot-TrEMBL)
AQP3 tetramerComplexR-HSA-432250 (Reactome)
AQP4 ProteinP55087 (Uniprot-TrEMBL)
AQP4 tetramerComplexR-HSA-432252 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
AVP(20-28) ProteinP01185 (Uniprot-TrEMBL)
AVP(20-28)ProteinP01185 (Uniprot-TrEMBL)
AVPR2 ProteinP30518 (Uniprot-TrEMBL)
AVPR2:AVP(20-28)ComplexR-HSA-392261 (Reactome)
AVPR2:AVP:G-alpha(s):GDP:G-beta:G-gammaComplexR-HSA-432197 (Reactome)
AVPR2:AVP:G-alpha(s):GTP:G-beta:G-gammaComplexR-HSA-432187 (Reactome)
AVPR2ProteinP30518 (Uniprot-TrEMBL)
Adenylate cyclase (Mg2+ cofactor)ComplexR-HSA-170665 (Reactome)
G-alpha(s):GDP:G-beta:G-gammaComplexR-HSA-432200 (Reactome)
G-alpha(s):GTP:G-beta:G-gammaComplexR-HSA-422322 (Reactome)
G-beta:G-gamma (candidates)ComplexR-HSA-400034 (Reactome)
G-protein alpha (s):GTPComplexR-HSA-164358 (Reactome)
GDP MetaboliteCHEBI:17552 (ChEBI)
GDPMetaboliteCHEBI:17552 (ChEBI)
GNAS1 ProteinQ5JWF2 (Uniprot-TrEMBL)
GNAS2 ProteinP63092 (Uniprot-TrEMBL)
GNB1 ProteinP62873 (Uniprot-TrEMBL)
GNB2 ProteinP62879 (Uniprot-TrEMBL)
GNB3 ProteinP16520 (Uniprot-TrEMBL)
GNB4 ProteinQ9HAV0 (Uniprot-TrEMBL)
GNB5 ProteinO14775 (Uniprot-TrEMBL)
GNG10 ProteinP50151 (Uniprot-TrEMBL)
GNG11 ProteinP61952 (Uniprot-TrEMBL)
GNG12 ProteinQ9UBI6 (Uniprot-TrEMBL)
GNG13 ProteinQ9P2W3 (Uniprot-TrEMBL)
GNG2 ProteinP59768 (Uniprot-TrEMBL)
GNG3 ProteinP63215 (Uniprot-TrEMBL)
GNG4 ProteinP50150 (Uniprot-TrEMBL)
GNG5 ProteinP63218 (Uniprot-TrEMBL)
GNG7 ProteinO60262 (Uniprot-TrEMBL)
GNG8 ProteinQ9UK08 (Uniprot-TrEMBL)
GNGT1 ProteinP63211 (Uniprot-TrEMBL)
GNGT2 ProteinO14610 (Uniprot-TrEMBL)
GTP MetaboliteCHEBI:15996 (ChEBI)
GTPMetaboliteCHEBI:15996 (ChEBI)
Gs-activated adenylate cyclaseComplexR-HSA-163622 (Reactome)
H2OMetaboliteCHEBI:15377 (ChEBI)
MYO5B ProteinQ9ULV0 (Uniprot-TrEMBL)
MYO5B:RABFIP2:RAB11AComplexR-HSA-2028701 (Reactome)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
PKA catalytic subunitComplexR-HSA-111920 (Reactome)
PKA tetramerComplexR-HSA-111922 (Reactome)
PPiMetaboliteCHEBI:29888 (ChEBI)
PRKACA ProteinP17612 (Uniprot-TrEMBL)
PRKACB ProteinP22694 (Uniprot-TrEMBL)
PRKACG ProteinP22612 (Uniprot-TrEMBL)
PRKAR1A ProteinP10644 (Uniprot-TrEMBL)
PRKAR1B ProteinP31321 (Uniprot-TrEMBL)
PRKAR2A ProteinP13861 (Uniprot-TrEMBL)
PRKAR2B ProteinP31323 (Uniprot-TrEMBL)
RAB11A ProteinP62491 (Uniprot-TrEMBL)
RAB11FIP2 ProteinQ7L804 (Uniprot-TrEMBL)
cAMP MetaboliteCHEBI:17489 (ChEBI)
cAMP:PKA regulatory subunitComplexR-HSA-111923 (Reactome)
cAMPMetaboliteCHEBI:17489 (ChEBI)
p-S256-AQP2 ProteinP41181 (Uniprot-TrEMBL)
p-S256-AQP2 tetramerComplexR-HSA-432226 (Reactome)
p-S256-AQP2ComplexR-HSA-432217 (Reactome)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
AQP1 tetramermim-catalysisR-HSA-432010 (Reactome)
AQP1 tetramermim-catalysisR-HSA-432054 (Reactome)
AQP2 tetramerR-HSA-432232 (Reactome)
AQP3 tetramermim-catalysisR-HSA-445714 (Reactome)
AQP4 tetramermim-catalysisR-HSA-432067 (Reactome)
ATPR-HSA-164377 (Reactome)
AVP(20-28)R-HSA-392263 (Reactome)
AVPR2:AVP(20-28)ArrowR-HSA-392263 (Reactome)
AVPR2:AVP(20-28)R-HSA-432188 (Reactome)
AVPR2:AVP:G-alpha(s):GDP:G-beta:G-gammaArrowR-HSA-432188 (Reactome)
AVPR2:AVP:G-alpha(s):GDP:G-beta:G-gammaR-HSA-432195 (Reactome)
AVPR2:AVP:G-alpha(s):GTP:G-beta:G-gammaArrowR-HSA-432195 (Reactome)
AVPR2R-HSA-392263 (Reactome)
Adenylate cyclase (Mg2+ cofactor)R-HSA-163617 (Reactome)
G-alpha(s):GDP:G-beta:G-gammaR-HSA-432188 (Reactome)
G-alpha(s):GTP:G-beta:G-gammaR-HSA-422320 (Reactome)
G-beta:G-gamma (candidates)ArrowR-HSA-422320 (Reactome)
G-protein alpha (s):GTPArrowR-HSA-422320 (Reactome)
G-protein alpha (s):GTPR-HSA-163617 (Reactome)
GDPArrowR-HSA-432195 (Reactome)
GTPR-HSA-432195 (Reactome)
Gs-activated adenylate cyclaseArrowR-HSA-163617 (Reactome)
Gs-activated adenylate cyclasemim-catalysisR-HSA-164377 (Reactome)
H2OArrowR-HSA-432010 (Reactome)
H2OArrowR-HSA-432054 (Reactome)
H2OArrowR-HSA-432065 (Reactome)
H2OArrowR-HSA-432067 (Reactome)
H2OArrowR-HSA-445714 (Reactome)
H2OR-HSA-432010 (Reactome)
H2OR-HSA-432054 (Reactome)
H2OR-HSA-432065 (Reactome)
H2OR-HSA-432067 (Reactome)
H2OR-HSA-445714 (Reactome)
MYO5B:RABFIP2:RAB11Amim-catalysisR-HSA-432237 (Reactome)
PKA catalytic subunitArrowR-HSA-111925 (Reactome)
PKA catalytic subunitmim-catalysisR-HSA-432232 (Reactome)
PKA tetramerR-HSA-111925 (Reactome)
PPiArrowR-HSA-164377 (Reactome)
R-HSA-111925 (Reactome)The four protein kinase A (PKA) regulatory subunit isoforms differ in their tissue specificity and functional characteristics. The specific isoform activated in response to glucagon signalling is not known. The PKA kinase is a tetramer of two regulatory and two catalytic. The regulatory subunits block the catalytic subunits. Binding of cAMP to the regulatory subunit leads to the dissociation of the tetramer into two active dimers made up of a regulatory and a catalytic subunit.
R-HSA-163617 (Reactome)G(s)-alpha:GTP binds to inactive adenylate cyclase, causing a conformational transition in adenylate cyclase exposing the catalytic site and activating it.
R-HSA-164377 (Reactome)Activated adenylate cyclase associated with the plasma membrane catalyzes the reaction of cytosolic ATP to form 3',5'-cyclicAMP and pyrophosphate ().
R-HSA-392263 (Reactome)Arginine vasopressin receptor 2 (AVPR2) (Birnbaumer et al. 1992) is expressed in the kidneys and can bind the signal peptide Arg-vasopressin (AVP(20-28)), a cleaved peptide from the precursor AVP protein (Mohr et al. 1985, Sausville et al. 1985). This receptor uses the G protein alpha s subunit as its second messenger system.
R-HSA-422320 (Reactome)The binding of GTP by G(s) alpha causes the heterotrimeric G-protein complex to reorientate, exposing previously bound faces of the G(s) alpha:GTP complex and the G-beta: G-gamma complex. Unlike the case with Gi/o heterotrimers, Gs heterotrimers are not observed to significantly dissociate in living cells.
R-HSA-432010 (Reactome)Aquaporin-1 (AQP1) passively transports water across the plasma membrane according to the osmotic gradient. In the kidney AQP1 is expressed in endothelial cells of the vasa recta, the proximal tubule, and thin descending limb of Henle, where it functions to recover water from filtrate during urine formation. AQP1 is expressed in many other tissues, such as red blood cells, pancreas, and choroid plexus. AQP1 plays a role in forming cerebrospinal fluid.
R-HSA-432054 (Reactome)Aquaporin-1 (AQP1) passively transports water across the plasma membrane according to the osmotic gradient. In the kidney AQP1 is expressed in endothelial cells of the vasa recta, the proximal tubule, and thin descending limb of Henle, where it functions to recover water from filtrate during urine formation. AQP1 is expressed in many other tissues, such as red blood cells, pancreas, and choroid plexus. AQP1 plays a role in forming cerebrospinal fluid.
R-HSA-432065 (Reactome)Aquaporin-2 (AQP2) passively transports water across membranes according to the osmotic gradient. AQP2 is mainly expressed in principal cells of the collecting duct and connecting tubule in the kidney. AQP2 function is acutely regulated by the antidiuretc hormone vasopressin. In the presence of vasopressin AQP is phosphorylated at Ser256, As inferred from rat and mouse Ser261, Ser264, and Thr269 may also be phosphorylated. These phosphorylations are thought to influence AQP2 trafficking and compartmentalization.
R-HSA-432067 (Reactome)Aquaporin-4 (AQP4) passively transports water across the plasma membrane according to the osmotic gradient. AQP4 is expressed in the collecting duct of the kidney and in astroglial cells at the blood-brain barrier and ependymal cells lining the ventricles of the brain.
R-HSA-432188 (Reactome)The vasopressin receptor type 2 (AVPR2) interacts with G-protein alpha s via the third intracellular loop of AVPR2.
R-HSA-432195 (Reactome)The AVP:AVPR2 complex activates G-protein alpha s by causing a conformational change in G-protein alpha s that causes it to release GDP and bind GTP.
R-HSA-432232 (Reactome)Activated Protein Kinase A phosphorylates Aquaporin-2 at Serine 256. The phosphorylated form of AQP2 then traffics from intracellular vesicles to the apical plasma membrane.
R-HSA-432237 (Reactome)Intracellular vesicles bearing phosphorylated Aquaporin-2 tetramers are transported to the plasma membrane by a mechanism that may involve motor activity of myosin VB (inferred from rat, Nedvetsky et al. 2007) and dynein (inferred from toad bladder, Marples et al. 1996).
R-HSA-445714 (Reactome)Aquaporin-3 (AQP3) passively transports water and glycerol across the plasma membrane according to the osmotic gradient. AQP3 is expressed in airway epithelia, secretory glands, skin, the collecting ducts of the kidney, and the basolateral surface of intestinal epithelium..
cAMP:PKA regulatory subunitArrowR-HSA-111925 (Reactome)
cAMPArrowR-HSA-164377 (Reactome)
cAMPR-HSA-111925 (Reactome)
p-S256-AQP2 tetramerArrowR-HSA-432237 (Reactome)
p-S256-AQP2 tetramermim-catalysisR-HSA-432065 (Reactome)
p-S256-AQP2ArrowR-HSA-432232 (Reactome)
p-S256-AQP2R-HSA-432237 (Reactome)