메뉴 건너뛰기




Volumn 10, Issue 9, 2014, Pages 707-709

Endosomal GPCR signaling turned off by negative feedback actions of PKA and v-ATPase

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BAFILOMYCIN; CHOLERA TOXIN; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; G PROTEIN COUPLED RECEPTOR;

EID: 84906305724     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1589     Document Type: Article
Times cited : (72)

References (26)
  • 2
    • 70349309325 scopus 로고    scopus 로고
    • Sustained cyclic AMP production by parathyroid hormone receptor endocytosis
    • Ferrandon, S. et al. Sustained cyclic AMP production by parathyroid hormone receptor endocytosis. Nat. Chem. Biol. 5, 734-742 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 734-742
    • Ferrandon, S.1
  • 3
    • 79955073671 scopus 로고    scopus 로고
    • Retromer terminates the generation of cAMP by internalized PTH receptors
    • Feinstein, T.N. et al. Retromer terminates the generation of cAMP by internalized PTH receptors. Nat. Chem. Biol. 7, 278-284 (2011).
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 278-284
    • Feinstein, T.N.1
  • 4
    • 84884761170 scopus 로고    scopus 로고
    • Noncanonical control of vasopressin receptor type 2 signaling by retromer and arrestin
    • Feinstein, T.N. et al. Noncanonical control of vasopressin receptor type 2 signaling by retromer and arrestin. J. Biol. Chem. 288, 27849-27860 (2013).
    • (2013) J. Biol. Chem. , vol.288 , pp. 27849-27860
    • Feinstein, T.N.1
  • 5
    • 0028261425 scopus 로고
    • Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis
    • Stenmark, H. et al. Inhibition of rab5 GTPase activity stimulates membrane fusion in endocytosis. EMBO J. 13, 1287-1296 (1994).
    • (1994) EMBO J. , vol.13 , pp. 1287-1296
    • Stenmark, H.1
  • 6
    • 0028014372 scopus 로고
    • Vacuolar ATPase activity is required for endosomal carrier vesicle formation
    • Clague, M.J., Urbe, S., Aniento, F. & Gruenberg, J. Vacuolar ATPase activity is required for endosomal carrier vesicle formation. J. Biol. Chem. 269, 21-24 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 21-24
    • Clague, M.J.1    Urbe, S.2    Aniento, F.3    Gruenberg, J.4
  • 7
    • 27644521278 scopus 로고    scopus 로고
    • Turn-on switch in parathyroid hormone receptor by a two-step parathyroid hormone binding mechanism
    • Castro, M., Nikolaev, V.O., Palm, D., Lohse, M.J. & Vilardaga, J.P. Turn-on switch in parathyroid hormone receptor by a two-step parathyroid hormone binding mechanism. Proc. Natl. Acad. Sci. USA 102, 16084-16089 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 16084-16089
    • Castro, M.1    Nikolaev, V.O.2    Palm, D.3    Lohse, M.J.4    Vilardaga, J.P.5
  • 8
    • 0029160297 scopus 로고
    • Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump
    • van Weert, A.W., Dunn, K.W., Geuze, H.J., Maxfield, F.R. & Stoorvogel, W. Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump. J. Cell Biol. 130, 821-834 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 821-834
    • Van Weert, A.W.1    Dunn, K.W.2    Geuze, H.J.3    Maxfield, F.R.4    Stoorvogel, W.5
  • 9
    • 84870295362 scopus 로고    scopus 로고
    • A general path for large-scale solubilization of cellular proteins: From membrane receptors to multiprotein complexes
    • Pullara, F. et al. A general path for large-scale solubilization of cellular proteins: from membrane receptors to multiprotein complexes. Protein Expr. Purif. 87, 111-119 (2013).
    • (2013) Protein Expr. Purif. , vol.87 , pp. 111-119
    • Pullara, F.1
  • 10
    • 4444377903 scopus 로고    scopus 로고
    • Novel single chain cAMP sensors for receptor-induced signal propagation
    • Nikolaev, V.O., Bunemann, M., Hein, L., Hannawacker, A. & Lohse, M.J. Novel single chain cAMP sensors for receptor-induced signal propagation. J. Biol. Chem. 279, 37215-37218 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 37215-37218
    • Nikolaev, V.O.1    Bunemann, M.2    Hein, L.3    Hannawacker, A.4    Lohse, M.J.5
  • 11
    • 84872847980 scopus 로고    scopus 로고
    • Noncanonical GPCR signaling arising from a PTH receptor-arrestin- Gβγ complex
    • Wehbi, V.L. et al. Noncanonical GPCR signaling arising from a PTH receptor-arrestin-Gβγ complex. Proc. Natl. Acad. Sci. USA 110, 1530-1535 (2013).
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 1530-1535
    • Wehbi, V.L.1
  • 12
    • 77955292351 scopus 로고    scopus 로고
    • PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells
    • Alzamora, R. et al. PKA regulates vacuolar H+-ATPase localization and activity via direct phosphorylation of the a subunit in kidney cells. J. Biol. Chem. 285, 24676-24685 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 24676-24685
    • Alzamora, R.1
  • 13
    • 34247626938 scopus 로고    scopus 로고
    • Role of receptor-mediated endocytosis, endosomal acidification and cathepsin D in cholera toxin cytotoxicity
    • El Hage, T., Merlen, C., Fabrega, S. & Authier, F. Role of receptor-mediated endocytosis, endosomal acidification and cathepsin D in cholera toxin cytotoxicity. FEBS J. 274, 2614-2629 (2007).
    • (2007) FEBS J. , vol.274 , pp. 2614-2629
    • El Hage, T.1    Merlen, C.2    Fabrega, S.3    Authier, F.4
  • 14
    • 0019427474 scopus 로고
    • Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts
    • Basu, S.K., Goldstein, J.L., Anderson, R.G. & Brown, M.S. Monensin interrupts the recycling of low density lipoprotein receptors in human fibroblasts. Cell 24, 493-502 (1981).
    • (1981) Cell , vol.24 , pp. 493-502
    • Basu, S.K.1    Goldstein, J.L.2    Anderson, R.G.3    Brown, M.S.4
  • 15
    • 0016679756 scopus 로고
    • Regulation of the activity of the low density lipoprotein receptor in human fibroblasts
    • Brown, M.S. & Goldstein, J.L. Regulation of the activity of the low density lipoprotein receptor in human fibroblasts. Cell 6, 307-316 (1975).
    • (1975) Cell , vol.6 , pp. 307-316
    • Brown, M.S.1    Goldstein, J.L.2
  • 16
    • 0020544493 scopus 로고
    • Separation of Fe+3 from transferrin in endocytosis. Role of the acidic endosome
    • Rao, K., van Renswoude, J., Kempf, C. & Klausner, R.D. Separation of Fe+3 from transferrin in endocytosis. Role of the acidic endosome. FEBS Lett. 160, 213-216 (1983).
    • (1983) FEBS Lett. , vol.160 , pp. 213-216
    • Rao, K.1    Van Renswoude, J.2    Kempf, C.3    Klausner, R.D.4
  • 17
    • 0021099317 scopus 로고
    • Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes. A pH-mediated nonlysosomal event
    • Harford, J., Bridges, K., Ashwell, G. & Klausner, R.D. Intracellular dissociation of receptor-bound asialoglycoproteins in cultured hepatocytes. A pH-mediated nonlysosomal event. J. Biol. Chem. 258, 3191-3197 (1983).
    • (1983) J. Biol. Chem. , vol.258 , pp. 3191-3197
    • Harford, J.1    Bridges, K.2    Ashwell, G.3    Klausner, R.D.4
  • 18
    • 0031036520 scopus 로고    scopus 로고
    • The role of sequestration in G protein-coupled receptor resensitization. Regulation of β2-adrenergic receptor dephosphorylation by vesicular acidification
    • Krueger, K.M., Daaka, Y., Pitcher, J.A. & Lefkowitz, R.J. The role of sequestration in G protein-coupled receptor resensitization. Regulation of β2-adrenergic receptor dephosphorylation by vesicular acidification. J. Biol. Chem. 272, 5-8 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 5-8
    • Krueger, K.M.1    Daaka, Y.2    Pitcher, J.A.3    Lefkowitz, R.J.4
  • 20
    • 38049086228 scopus 로고    scopus 로고
    • Altered selectivity of parathyroid hormone (PTH) and PTH-related protein (PTHrP) for distinct conformations of the PTH/PTHrP receptor
    • Dean, T., Vilardaga, J.P., Potts, J.T. Jr. & Gardella, T.J. Altered selectivity of parathyroid hormone (PTH) and PTH-related protein (PTHrP) for distinct conformations of the PTH/PTHrP receptor. Mol. Endocrinol. 22, 156-166 (2008).
    • (2008) Mol. Endocrinol. , vol.22 , pp. 156-166
    • Dean, T.1    Vilardaga, J.P.2    Potts Jr., J.T.3    Gardella, T.J.4
  • 21
    • 40049099087 scopus 로고    scopus 로고
    • Microscale fluorescent thermal stability assay for membrane proteins
    • Alexandrov, A.I., Mileni, M., Chien, E.Y., Hanson, M.A. & Stevens, R.C. Microscale fluorescent thermal stability assay for membrane proteins. Structure 16, 351-359 (2008).
    • (2008) Structure , vol.16 , pp. 351-359
    • Alexandrov, A.I.1    Mileni, M.2    Chien, E.Y.3    Hanson, M.A.4    Stevens, R.C.5
  • 22
    • 80054775036 scopus 로고    scopus 로고
    • Studying ligand efficacy at G protein-coupled receptors using FRET
    • Vilardaga, J.P. Studying ligand efficacy at G protein-coupled receptors using FRET. Methods Mol. Biol. 756, 133-148 (2011).
    • (2011) Methods Mol. Biol. , vol.756 , pp. 133-148
    • Vilardaga, J.P.1
  • 23
    • 80054723816 scopus 로고    scopus 로고
    • Luminescent biosensors for real-time monitoring of intracellular cAMP
    • Binkowski, B.F., Fan, F. & Wood, K.V. Luminescent biosensors for real-time monitoring of intracellular cAMP. Methods Mol. Biol. 756, 263-271 (2011).
    • (2011) Methods Mol. Biol. , vol.756 , pp. 263-271
    • Binkowski, B.F.1    Fan, F.2    Wood, K.V.3
  • 24
    • 81555208982 scopus 로고    scopus 로고
    • A luminescent biosensor with increased dynamic range for intracellular cAMP
    • Binkowski, B.F. et al. A luminescent biosensor with increased dynamic range for intracellular cAMP. ACS Chem. Biol. 6, 1193-1197 (2011).
    • (2011) ACS Chem. Biol. , vol.6 , pp. 1193-1197
    • Binkowski, B.F.1
  • 25
    • 84862806070 scopus 로고    scopus 로고
    • Regulation of nuclear PKA revealed by spatiotemporal manipulation of cyclic AMP
    • Sample, V. et al. Regulation of nuclear PKA revealed by spatiotemporal manipulation of cyclic AMP. Nat. Chem. Biol. 8, 375-382 (2012).
    • (2012) Nat. Chem. Biol. , vol.8 , pp. 375-382
    • Sample, V.1
  • 26
    • 84884930855 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates the vacuolar H+-ATPase via direct phosphorylation of the A subunit (ATP6V1A) in the kidney
    • Alzamora, R. et al. AMP-activated protein kinase regulates the vacuolar H+-ATPase via direct phosphorylation of the A subunit (ATP6V1A) in the kidney. Am. J. Physiol. Renal Physiol. 305, F943-F956 (2013). Diseases
    • (2013) Am. J. Physiol. Renal Physiol. , vol.305
    • Alzamora, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.