메뉴 건너뛰기




Volumn 168, Issue 3, 1999, Pages 275-282

Effect of two tyrosine mutations on the activity and regulation of the renal type II Na/P(i)-cotransporter expressed in oocytes

Author keywords

Endocytosis; Na P(i) cotransporter; PTH; Tyrosine based signals

Indexed keywords

PHOSPHATE; PROTEIN KINASE C; SODIUM ION; TYROSINE;

EID: 0032918073     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900516     Document Type: Article
Times cited : (6)

References (42)
  • 1
    • 0032574725 scopus 로고    scopus 로고
    • Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities
    • Beck, L., Karaplis, A.C., Amizuka, N., Hewson, A.S., Ozawa, H., Tenenhouse, H.S. 1998. Targeted inactivation of Npt2 in mice leads to severe renal phosphate wasting, hypercalciuria, and skeletal abnormalities. Proc. Natl. Acad. Sci. USA 95:5372-5377
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5372-5377
    • Beck, L.1    Karaplis, A.C.2    Amizuka, N.3    Hewson, A.S.4    Ozawa, H.5    Tenenhouse, H.S.6
  • 2
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator
    • Brown, C.R., Hong-Brown, L.Q., Biwersi, J., Verkman, A.S., Welch, W.J. 1996. Chemical chaperones correct the mutant phenotype of the delta F508 cystic fibrosis transmembrane conductance regulator. Cell Stress Chaperons 1:117-125
    • (1996) Cell Stress Chaperons , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 3
    • 0030797573 scopus 로고    scopus 로고
    • A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion
    • Courtois-Coutry, N., Roush, D., Rajendran, V., McCarthy, J.B., Geibel, J., Kashgarian, M., Caplan, M.J. 1997. A tyrosine-based signal targets H/K-ATPase to a regulated compartment and is required for the cessation of gastric acid secretion. Cell 90:501-510
    • (1997) Cell , vol.90 , pp. 501-510
    • Courtois-Coutry, N.1    Roush, D.2    Rajendran, V.3    McCarthy, J.B.4    Geibel, J.5    Kashgarian, M.6    Caplan, M.J.7
  • 5
    • 0022456630 scopus 로고
    • The J.D mutation in familial hypercholesterolemia: Amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors
    • Davis, C.G., Lehrman, M.A., Russell, D.W., Anderson, R.G., Brown, M.S., Goldstein, J.L. 1986. The J.D mutation in familial hypercholesterolemia: amino acid substitution in cytoplasmic domain impedes internalization of LDL receptors. Cell 45:15-24
    • (1986) Cell , vol.45 , pp. 15-24
    • Davis, C.G.1    Lehrman, M.A.2    Russell, D.W.3    Anderson, R.G.4    Brown, M.S.5    Goldstein, J.L.6
  • 6
    • 0028968593 scopus 로고
    • Water channels encoded by mutant aquaporing-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing
    • Deen, P.M., Croes, H., Van Aubel, R.A., Ginsel, L.A., Van Os, C.H. 1995. Water channels encoded by mutant aquaporing-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J. Clin. Invest. 95:2291-2296
    • (1995) J. Clin. Invest. , vol.95 , pp. 2291-2296
    • Deen, P.M.1    Croes, H.2    Van Aubel, R.A.3    Ginsel, L.A.4    Van Os, C.H.5
  • 8
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature sensitive
    • Denning, G.M., Anderson, M.P., Amara, J.F., Marshall, J., Smith, A.E., Welsh, M.J. 1992. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature sensitive. Nature 358:761-764
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 12
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: Retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond, C., Helenius, A. 1994. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J. Cell Biol. 126:41-52
    • (1994) J. Cell Biol. , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 13
    • 0026545549 scopus 로고
    • Transport of the lysosomal membrane glycoprotein Ipg120 (Igp-A) to lysosomes does not require appearance on the plasma membrane
    • Harter, C., Mellman, I. 1992. Transport of the lysosomal membrane glycoprotein Ipg120 (Igp-A) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 117:311-325
    • (1992) J. Cell Biol. , vol.117 , pp. 311-325
    • Harter, C.1    Mellman, I.2
  • 16
    • 0029935911 scopus 로고    scopus 로고
    • In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting
    • Heilker, R., Manning-Krieg, U., Zuber, J.F., Spiess, M. 1996. In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J. 15:2893-2899
    • (1996) EMBO J. , vol.15 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg, U.2    Zuber, J.F.3    Spiess, M.4
  • 17
    • 0028905152 scopus 로고
    • Cloning, sequence analysis and expression of a cDNA encoding a sodium-dependent phosphate transporter from the bovine renal epithelial cell line NBL-1
    • Helps, C., Murer, H., McGivan, J. 1995. Cloning, sequence analysis and expression of a cDNA encoding a sodium-dependent phosphate transporter from the bovine renal epithelial cell line NBL-1. Eur. J. Biochem. 228:927-930
    • (1995) Eur. J. Biochem. , vol.228 , pp. 927-930
    • Helps, C.1    Murer, H.2    McGivan, J.3
  • 18
    • 0028929058 scopus 로고
    • Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat Igp120 (Lamp-I) in MCDK cells
    • Höning, S., Hunziker, W. 1995. Cytoplasmic determinants involved in direct lysosomal sorting, endocytosis, and basolateral targeting of rat Igp120 (Lamp-I) in MCDK cells. J. Cell Biol. 128:321-332
    • (1995) J. Cell Biol. , vol.128 , pp. 321-332
    • Höning, S.1    Hunziker, W.2
  • 19
    • 0028928028 scopus 로고
    • Parathyroid hormone action on phosphate transporter mRNA and protein in rat renal proximal tubules
    • Kempson, S.A., Lötscher, M., Kaissling, B., Biber, J., Murer, H., Levi, M. 1995. Parathyroid hormone action on phosphate transporter mRNA and protein in rat renal proximal tubules. Am. J. Physiol. 268:F784-F791
    • (1995) Am. J. Physiol. , vol.268
    • Kempson, S.A.1    Lötscher, M.2    Kaissling, B.3    Biber, J.4    Murer, H.5    Levi, M.6
  • 22
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., Mellman, I. 1994. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell. Biol. 6:545-554
    • (1994) Curr. Opin. Cell. Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 23
    • 0029034735 scopus 로고
    • A cytoplasmic tyrosine is essential for the basolateral localization of mutants the human nerve growth factor receptor in Madin-Darby canine kidney cells
    • Monlauzeur, L., Rajasekaran, A., Chao, M., Rodriguez-Boulan, E., Le Bivic, A. 1995. A cytoplasmic tyrosine is essential for the basolateral localization of mutants the human nerve growth factor receptor in Madin-Darby canine kidney cells. J. Biol. Chem. 270:12219-12225
    • (1995) J. Biol. Chem. , vol.270 , pp. 12219-12225
    • Monlauzeur, L.1    Rajasekaran, A.2    Chao, M.3    Rodriguez-Boulan, E.4    Le Bivic, A.5
  • 25
    • 0002625435 scopus 로고
    • Renal tubular phosphate transport
    • D.W. Seldin and G. Giebish, editors. Raven Press, New York
    • Murer, H., Biber, J. 1992. Renal tubular phosphate transport. In: The Kidney, Physiology and Pathophysiology. D.W. Seldin and G. Giebish, editors. pp. 2481-2509. Raven Press, New York
    • (1992) The Kidney, Physiology and Pathophysiology , pp. 2481-2509
    • Murer, H.1    Biber, J.2
  • 26
    • 0031022070 scopus 로고    scopus 로고
    • i) reabsorption and ist regulation
    • i) reabsorption and ist regulation. Pfluegers Arch. 433:379-389
    • (1997) Pfluegers Arch. , vol.433 , pp. 379-389
    • Murer, H.1    Biber, J.2
  • 33
    • 0029670902 scopus 로고    scopus 로고
    • The targeting of Lamp I to lysosomes is dependent on the spacing of ist cytoplasmic tail tyrosine sorting motif relative to the membrane
    • Rohrer, J., Schweizer, A., Russell, D., Kornfeld, S. 1996. The targeting of Lamp I to lysosomes is dependent on the spacing of ist cytoplasmic tail tyrosine sorting motif relative to the membrane. J. Cell Biol. 132:565-576
    • (1996) J. Cell Biol. , vol.132 , pp. 565-576
    • Rohrer, J.1    Schweizer, A.2    Russell, D.3    Kornfeld, S.4
  • 37
    • 0030611423 scopus 로고    scopus 로고
    • A mutation in the hamster alplha1B-adrenergic receptor that differentiates two steps in the pathway of receptor internalization
    • Wang, J., Zheng, J., Anderson, J.L., Toews, M.L. 1997. A mutation in the hamster alplha1B-adrenergic receptor that differentiates two steps in the pathway of receptor internalization. Mol. Pharmacol. 52:306-313
    • (1997) Mol. Pharmacol. , vol.52 , pp. 306-313
    • Wang, J.1    Zheng, J.2    Anderson, J.L.3    Toews, M.L.4
  • 38
    • 0025345577 scopus 로고
    • Expression of renal transport systems for inorganic phosphate and sulfate in Xenopus laevis oocytes
    • Werner, A., Biber, J., Forgo, J., Palacin, M., Murer, H. 1990. Expression of renal transport systems for inorganic phosphate and sulfate in Xenopus laevis oocytes. J. Biol. Chem. 265:12331-12336
    • (1990) J. Biol. Chem. , vol.265 , pp. 12331-12336
    • Werner, A.1    Biber, J.2    Forgo, J.3    Palacin, M.4    Murer, H.5
  • 39
    • 0027935256 scopus 로고
    • Cloning and expression of a renal Na-Pi cotransport system from flounder
    • Werner, A., Murer, H., Kinne, R.K.H. 1994. Cloning and expression of a renal Na-Pi cotransport system from flounder. Am. J. Physiol. 267:F311-F317
    • (1994) Am. J. Physiol. , vol.267
    • Werner, A.1    Murer, H.2    Kinne, R.K.H.3
  • 40
    • 0025172954 scopus 로고
    • Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail
    • Williams, M.A., Fukuda, M. 1990. Accumulation of membrane glycoproteins in lysosomes requires a tyrosine residue at a particular position in the cytoplasmic tail. J. Cell Biol. 111:955-966
    • (1990) J. Cell Biol. , vol.111 , pp. 955-966
    • Williams, M.A.1    Fukuda, M.2
  • 41
    • 0030931382 scopus 로고    scopus 로고
    • Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator
    • Xiong, X., Bragin, A., Widdicombe, J.H., Cohn, J., Skach, W.R. 1997. Structural cues involved in endoplasmic reticulum degradation of G85E and G91R mutant cystic fibrosis transmembrane conductance regulator. J. Clin. Invest. 100:1079-1088
    • (1997) J. Clin. Invest. , vol.100 , pp. 1079-1088
    • Xiong, X.1    Bragin, A.2    Widdicombe, J.H.3    Cohn, J.4    Skach, W.R.5
  • 42
    • 0027488993 scopus 로고
    • The common variant of the cystic fibrosis transmembrnae conductance regulator is recognized by hsp70 and degraded in a pre-Golgy nonlysosomal compartment
    • Yang, Y., Janich, S., Cohn, J.A., Wilson, J.M. 1993. The common variant of the cystic fibrosis transmembrnae conductance regulator is recognized by hsp70 and degraded in a pre-Golgy nonlysosomal compartment. Proc. Natl. Acad. Sci. USA 90:9480-9484
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.