메뉴 건너뛰기




Volumn 276, Issue 4 45-4, 1999, Pages

Modulation of renal tubular cell function by RGS3

Author keywords

Chemotaxis; G protein; Kidney development; Regulators of G protein signaling; Renal tubular epithelial cells

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 0032957837     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.1999.276.4.f535     Document Type: Article
Times cited : (14)

References (62)
  • 1
    • 0028236960 scopus 로고
    • The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions
    • Barry, S. T., and D. R. Critchley. The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and the recruitment of both pp125FAK and protein kinase C-delta to focal adhesions. J. Cell Sci. 107: 2033-2045, 1994.
    • (1994) J. Cell Sci. , vol.107 , pp. 2033-2045
    • Barry, S.T.1    Critchley, D.R.2
  • 2
    • 0027059342 scopus 로고
    • Phospholipids regulate growth and function of MDCK cells in hormonally defined serum free medium
    • Bashir, N., K. Kuhen, and M. Taub. Phospholipids regulate growth and function of MDCK cells in hormonally defined serum free medium. In Vitro Cell. Dev. Biol. 28: 663-668, 1992.
    • (1992) In Vitro Cell. Dev. Biol. , vol.28 , pp. 663-668
    • Bashir, N.1    Kuhen, K.2    Taub, M.3
  • 3
    • 0031916822 scopus 로고    scopus 로고
    • Mammalian RGS proteins: Barbarians at the gate
    • Berman, D. M., and A. G. Gilman. Mammalian RGS proteins: barbarians at the gate. J. Biol. Chem. 273: 1269-1272, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1269-1272
    • Berman, D.M.1    Gilman, A.G.2
  • 4
    • 0029861417 scopus 로고    scopus 로고
    • The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis
    • Berman, D. M., T. Kozasa, and A. G. Gilman. The GTPase-activating protein RGS4 stabilizes the transition state for nucleotide hydrolysis. J. Biol. Chem. 271: 27209-27212, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27209-27212
    • Berman, D.M.1    Kozasa, T.2    Gilman, A.G.3
  • 5
    • 0032561305 scopus 로고    scopus 로고
    • Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members
    • Bowman, E. P., J. J. Campbell, K. M. Druey, A. Scheschonka, J. H. Kehrl, and E. C. Butcher. Regulation of chemotactic and proadhesive responses to chemoattractant receptors by RGS (regulator of G-protein signaling) family members. J. Biol. Chem. 273: 28040-28048, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28040-28048
    • Bowman, E.P.1    Campbell, J.J.2    Druey, K.M.3    Scheschonka, A.4    Kehrl, J.H.5    Butcher, E.C.6
  • 7
    • 0031958786 scopus 로고    scopus 로고
    • Regulators of G protein signaling: Rapid changes in mRNA abundance in response to amphetamine
    • Burchett, S. A., M. L. Volk, M. J. Bannon, and J. G. Granneman. Regulators of G protein signaling: rapid changes in mRNA abundance in response to amphetamine. J. Neurochem. 70: 2216-2219, 1998.
    • (1998) J. Neurochem. , vol.70 , pp. 2216-2219
    • Burchett, S.A.1    Volk, M.L.2    Bannon, M.J.3    Granneman, J.G.4
  • 9
    • 0031006273 scopus 로고    scopus 로고
    • A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C
    • Chatterjee, T. K., A. K. Eapen, and R. A. Fisher. A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C. J. Biol. Chem. 272: 15481-15487, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15481-15487
    • Chatterjee, T.K.1    Eapen, A.K.2    Fisher, R.A.3
  • 10
    • 0030933718 scopus 로고    scopus 로고
    • Characterization of a novel mammalian RGS protein that binds to Gα proteins and inhibits pheromone signaling in yeast
    • Chen, C., B. Zheng, J. Han, and S. C. Lin. Characterization of a novel mammalian RGS protein that binds to Gα proteins and inhibits pheromone signaling in yeast. J. Biol. Chem. 272: 8679-8685, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8679-8685
    • Chen, C.1    Zheng, B.2    Han, J.3    Lin, S.C.4
  • 11
    • 0029843409 scopus 로고    scopus 로고
    • RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling
    • Chen, C. K., T. Wieland, and M. I. Simon. RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. Proc. Natl. Acad. Sci. USA 93: 12885-12889, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12885-12889
    • Chen, C.K.1    Wieland, T.2    Simon, M.I.3
  • 12
    • 0028557424 scopus 로고
    • Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation
    • Chrzanowska-Wodnicka, M., and K. Burridge. Tyrosine phosphorylation is involved in reorganization of the actin cytoskeleton in response to serum or LPA stimulation. J. Cell Sci. 107: 3643-3654, 1994.
    • (1994) J. Cell Sci. , vol.107 , pp. 3643-3654
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 13
    • 0031021528 scopus 로고    scopus 로고
    • The heterotrimeric G protein Gαi2 mediates lysophosphatidic acid-stimulated induction of the c-fos gene in mouse fibroblasts
    • Chuprun, J. K., J. R. Raymond, and P. J. Blackshear. The heterotrimeric G protein Gαi2 mediates lysophosphatidic acid-stimulated induction of the c-fos gene in mouse fibroblasts. J. Biol. Chem. 272: 773-781, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 773-781
    • Chuprun, J.K.1    Raymond, J.R.2    Blackshear, P.J.3
  • 14
    • 0032486476 scopus 로고    scopus 로고
    • Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway
    • Cunnick, J. M., J. F. Dorsey, T. Standley, J. Turkson, A. J. Kraker, D. W. Fry, R. Jove, and J. Wu. Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway. J. Biol. Chem. 273: 14468-14475, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14468-14475
    • Cunnick, J.M.1    Dorsey, J.F.2    Standley, T.3    Turkson, J.4    Kraker, A.J.5    Fry, D.W.6    Jove, R.7    Wu, J.8
  • 15
    • 0030448762 scopus 로고    scopus 로고
    • GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits
    • De Vries, L., E. Elenko, L. Hubler, T. L. Jones, and M. G. Farquhar. GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits. Proc. Natl. Acad. Sci. USA 93: 15203-15208, 1996.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 15203-15208
    • De Vries, L.1    Elenko, E.2    Hubler, L.3    Jones, T.L.4    Farquhar, M.G.5
  • 16
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain
    • De Vries, L., M. Mousli, A. Wurmser, and M. G. Farquhar. GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. USA 92: 11916-11920, 1995.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 17
    • 0030028220 scopus 로고    scopus 로고
    • An 11-amino acid sequence from c-met initiates epithelial chemotaxis via phosphatidylinositol 3-kinase and phospholipase C
    • Derman, M. P., J. Y. Chen, K. C. Spokes, Z. Songyang, and L. G. Cantley. An 11-amino acid sequence from c-met initiates epithelial chemotaxis via phosphatidylinositol 3-kinase and phospholipase C. J. Biol. Chem. 271: 4251-4255, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4251-4255
    • Derman, M.P.1    Chen, J.Y.2    Spokes, K.C.3    Songyang, Z.4    Cantley, L.G.5
  • 20
    • 0031041306 scopus 로고    scopus 로고
    • RGS proteins and signaling by heterotrimeric G proteins
    • Dohlman, H. G., and J. Thorner. RGS proteins and signaling by heterotrimeric G proteins. J. Biol. Chem. 272: 3871-384, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 3871-4384
    • Dohlman, H.G.1    Thorner, J.2
  • 22
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey, K. M., K. J. Blumer, V. H. Kang, and J. H. Kehrl. Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. Nature 379: 742-746, 1996.
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 25
    • 0030953032 scopus 로고    scopus 로고
    • The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro
    • Faurobert, E., and J. B. Hurley. The core domain of a new retina specific RGS protein stimulates the GTPase activity of transducin in vitro. Proc. Natl. Acad. Sci. USA 94: 2945-2950, 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2945-2950
    • Faurobert, E.1    Hurley, J.B.2
  • 27
    • 0030952894 scopus 로고    scopus 로고
    • Dual effect of lysophosphatidic acid on proliferation of glomerular mesangial cells
    • Gaits, F., J. P. Salles, and H. Chap. Dual effect of lysophosphatidic acid on proliferation of glomerular mesangial cells. Kidney Int. 51: 1022-1027, 1997.
    • (1997) Kidney Int. , vol.51 , pp. 1022-1027
    • Gaits, F.1    Salles, J.P.2    Chap, H.3
  • 28
    • 0030764226 scopus 로고    scopus 로고
    • Regulators of G-protein signaling (RGS) proteins: Region-specific expression of nine subtypes in rat brain
    • Gold, S. J., Y. G. Ni, H. G. Dohlman, and E. J. Nestler. Regulators of G-protein signaling (RGS) proteins: region-specific expression of nine subtypes in rat brain. J. Neurosci. 17: 8024-8037, 1997.
    • (1997) J. Neurosci. , vol.17 , pp. 8024-8037
    • Gold, S.J.1    Ni, Y.G.2    Dohlman, H.G.3    Nestler, E.J.4
  • 29
    • 0031936503 scopus 로고    scopus 로고
    • RGS9, a GTPase accelerator for phototransduction
    • He, W., C. W. Cowan, and T. G. Wensel. RGS9, a GTPase accelerator for phototransduction. Neuron 20: 95-102, 1998.
    • (1998) Neuron , vol.20 , pp. 95-102
    • He, W.1    Cowan, C.W.2    Wensel, T.G.3
  • 32
    • 0031931196 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling: Roles in immune function and fine-tuning by RGS proteins
    • Kehrl, J. H. Heterotrimeric G protein signaling: roles in immune function and fine-tuning by RGS proteins. Immunity 8: 1-10, 1998.
    • (1998) Immunity , vol.8 , pp. 1-10
    • Kehrl, J.H.1
  • 33
    • 0030907376 scopus 로고    scopus 로고
    • A new family of G-protein regulators - The RGS proteins
    • Koelle, M. R. A new family of G-protein regulators - the RGS proteins. Curr. Opin. Cell Biol. 9: 143-147, 1997.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 143-147
    • Koelle, M.R.1
  • 34
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
    • Koelle, M. R., and H. R. Horvitz. EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84: 115-125, 1996.
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 35
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg, O., M. Poland, M. Gebbink, L. Oomen, and W. H. Moolenaar. Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J. Cell Sci. 110: 2417-2427, 1997.
    • (1997) J. Cell Sci. , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenaar, W.H.5
  • 36
    • 0030665658 scopus 로고    scopus 로고
    • Lysophosphatidic acid: A novel growth and survival factor for renal proximal tubular cells
    • Renal Physiol. 42
    • Levine, J. S., J. S. Koh, V. Triaca, and W. Lieberthal. Lysophosphatidic acid: a novel growth and survival factor for renal proximal tubular cells. Am. J. Physiol. 273 (Renal Physiol. 42): F575-F585, 1997.
    • (1997) Am. J. Physiol. , vol.273
    • Levine, J.S.1    Koh, J.S.2    Triaca, V.3    Lieberthal, W.4
  • 37
    • 0030907130 scopus 로고    scopus 로고
    • Glomerular number and size following chronic angiotensin II blockade in the postnatal rat
    • McCausland, J. E., J. F. Bertram, G. B. Ryan, and D. Alcorn. Glomerular number and size following chronic angiotensin II blockade in the postnatal rat. Exp. Nephrol. 5: 201-209, 1997.
    • (1997) Exp. Nephrol. , vol.5 , pp. 201-209
    • McCausland, J.E.1    Bertram, J.F.2    Ryan, G.B.3    Alcorn, D.4
  • 38
    • 0029032202 scopus 로고
    • Lysophosphatidic acid, a multifunctional phospholipid messenger
    • Moolenaar, W. H. Lysophosphatidic acid, a multifunctional phospholipid messenger. J. Biol. Chem. 270: 12949-12952, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12949-12952
    • Moolenaar, W.H.1
  • 41
    • 0031053536 scopus 로고    scopus 로고
    • Potential role for a regulator of G protein signaling (RGS3) in gonadotropin-releasing hormone (GnRH) stimulated desensitization
    • Neill, J. D., L. W. Duck, J. C. Sellers, L. C. Musgrove, A. Scheschonka, K. M. Druey, and J. H. Kehrl. Potential role for a regulator of G protein signaling (RGS3) in gonadotropin-releasing hormone (GnRH) stimulated desensitization. Endocrinology 138: 843-846, 1997.
    • (1997) Endocrinology , vol.138 , pp. 843-846
    • Neill, J.D.1    Duck, L.W.2    Sellers, J.C.3    Musgrove, L.C.4    Scheschonka, A.5    Druey, K.M.6    Kehrl, J.H.7
  • 42
    • 0031858969 scopus 로고    scopus 로고
    • Intercellular signaling by lysophosphatidate
    • Nietgen, G. W., and M. E. Durieux. Intercellular signaling by lysophosphatidate. Cell Adhes. Commun. 5: 221-235, 1998.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 221-235
    • Nietgen, G.W.1    Durieux, M.E.2
  • 44
    • 0031015426 scopus 로고    scopus 로고
    • Vascular system defects and impaired cell chemokinesis as a result of Gα13 deficiency
    • Offermanns, S., V. Mancino, J. P. Revel, and M. I. Simon. Vascular system defects and impaired cell chemokinesis as a result of Gα13 deficiency. Science 275: 533-536, 1997.
    • (1997) Science , vol.275 , pp. 533-536
    • Offermanns, S.1    Mancino, V.2    Revel, J.P.3    Simon, M.I.4
  • 45
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in Gα(q)-deficient mice
    • Offermanns, S., C. F. Toombs, Y. H. Hu, and M. I. Simon. Defective platelet activation in Gα(q)-deficient mice. Nature 389: 183-186, 1997.
    • (1997) Nature , vol.389 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.H.3    Simon, M.I.4
  • 46
    • 0031080174 scopus 로고    scopus 로고
    • Endothelial cell mitogenesis induced by LPA: Inhibition by thrombospondin-1 and thrombospondin-2
    • Panetti, T. S., H. Chen, T. M. Misenheimer, S. B. Getzler, and D. F. Mosher. Endothelial cell mitogenesis induced by LPA: inhibition by thrombospondin-1 and thrombospondin-2. J. Lab. Clin. Med. 129: 208-216, 1997.
    • (1997) J. Lab. Clin. Med. , vol.129 , pp. 208-216
    • Panetti, T.S.1    Chen, H.2    Misenheimer, T.M.3    Getzler, S.B.4    Mosher, D.F.5
  • 47
    • 0031014301 scopus 로고    scopus 로고
    • Signalling properties of lysophosphatidic acid in primary human skin fibroblasts: Role of pertussis toxin-sensitive GTP-binding proteins
    • Pietruck, F., S. Busch, S. Virchow, N. Brockmeyer, and W. Siffert. Signalling properties of lysophosphatidic acid in primary human skin fibroblasts: role of pertussis toxin-sensitive GTP-binding proteins. Naunyn Schmiedebergs Arch. Pharmacol. 355: 1-7, 1997.
    • (1997) Naunyn Schmiedebergs Arch. Pharmacol. , vol.355 , pp. 1-7
    • Pietruck, F.1    Busch, S.2    Virchow, S.3    Brockmeyer, N.4    Siffert, W.5
  • 48
    • 0027525215 scopus 로고
    • An osmotically tolerant inner medullary collecting duct cell line from an SV40 transgenic mouse
    • Renal Fluid Electrolyte Physiol. 34
    • Rauchman, M. I., S. K. Nigam, E. Delpire, and S. R. Gullans. An osmotically tolerant inner medullary collecting duct cell line from an SV40 transgenic mouse. Am. J. Physiol. 265 (Renal Fluid Electrolyte Physiol. 34): F416-F424, 1993.
    • (1993) Am. J. Physiol. , vol.265
    • Rauchman, M.I.1    Nigam, S.K.2    Delpire, E.3    Gullans, S.R.4
  • 50
    • 0032584382 scopus 로고    scopus 로고
    • Restoration of β1A integrins is required for lysophosphatidic acid induced migration of β1-null mouse fibroblastic cells
    • Sakai, T., O. Peyruchaud, R. Fassler, and D. F. Mosher. Restoration of β1A integrins is required for lysophosphatidic acid induced migration of β1-null mouse fibroblastic cells. J. Biol. Chem. 273: 19378-19382, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19378-19382
    • Sakai, T.1    Peyruchaud, O.2    Fassler, R.3    Mosher, D.F.4
  • 52
    • 0032509741 scopus 로고    scopus 로고
    • Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): Genomic structure and chromosomal localization of the human gene
    • Snow, B. E., L. Antonio, S. Suggs, and D. P. Siderovski. Cloning of a retinally abundant regulator of G-protein signaling (RGS-r/RGS16): genomic structure and chromosomal localization of the human gene. Gene 206: 247-253, 1998.
    • (1998) Gene , vol.206 , pp. 247-253
    • Snow, B.E.1    Antonio, L.2    Suggs, S.3    Siderovski, D.P.4
  • 55
    • 0032527809 scopus 로고    scopus 로고
    • Invasion of T-lymphoma cells: Cooperation between rho family GTPases and lysophospholipid receptor signaling
    • Stam, J. C., F. Michiels, R. A. Kammen, W. H. Moolenaar, and J. G. Collard. Invasion of T-lymphoma cells: cooperation between rho family GTPases and lysophospholipid receptor signaling. EMBO J. 17: 4066-4074, 1998.
    • (1998) EMBO J. , vol.17 , pp. 4066-4074
    • Stam, J.C.1    Michiels, F.2    Kammen, R.A.3    Moolenaar, W.H.4    Collard, J.G.5
  • 56
    • 0026344220 scopus 로고
    • Heterogeneous localization of G protein α-subunits in rat kidney
    • Renal Fluid Electrolyte Physiol. 30
    • Stow, J. L., I. Sabolic, and D. Brown. Heterogeneous localization of G protein α-subunits in rat kidney. Am. J. Physiol. 261 (Renal Fluid Electrolyte Physiol. 30): F831-F840, 1991.
    • (1991) Am. J. Physiol. , vol.261
    • Stow, J.L.1    Sabolic, I.2    Brown, D.3
  • 59
    • 0024428410 scopus 로고
    • Lysophosphatidate-induced cell proliferation: Identification and dissection of signaling pathways mediated by G proteins
    • Van Corven, E. J., A. Groenink, K. Jalink, T. Eichholtz, and W. H. Moolenaar. Lysophosphatidate-induced cell proliferation: identification and dissection of signaling pathways mediated by G proteins. Cell 59: 45-54, 1989.
    • (1989) Cell , vol.59 , pp. 45-54
    • Van Corven, E.J.1    Groenink, A.2    Jalink, K.3    Eichholtz, T.4    Moolenaar, W.H.5
  • 61
    • 0030611749 scopus 로고    scopus 로고
    • RGS4 inhibits Gq-mediated activation of mitogen-activated protein kinase and phosphoinositide synthesis
    • Yan, Y., P. P. Chi, and H. R. Bourne. RGS4 inhibits Gq-mediated activation of mitogen-activated protein kinase and phosphoinositide synthesis. J. Biol. Chem. 272: 11924-11927, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11924-11927
    • Yan, Y.1    Chi, P.P.2    Bourne, H.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.