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Volumn 57, Issue 1, 2000, Pages 44-52

Microtubule-dependent regulation of α(2B) adrenergic receptors in polarized MDCKII cells requires the third intracellular loop but not G protein coupling

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE A1 RECEPTOR; ALPHA 2 ADRENERGIC RECEPTOR; ALPHA 2A ADRENERGIC RECEPTOR; ALPHA 2B ADRENERGIC RECEPTOR; ALPHA 2C ADRENERGIC RECEPTOR; COLCHICINE; GUANINE NUCLEOTIDE BINDING PROTEIN; PERTUSSIS TOXIN;

EID: 0033986625     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (16)

References (46)
  • 1
    • 0029829896 scopus 로고    scopus 로고
    • Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages
    • Allen LA and Aderem A (1996) Molecular definition of distinct cytoskeletal structures involved in complement- and Fc receptor-mediated phagocytosis in macrophages. J Exp Med 184:627-637.
    • (1996) J Exp Med , vol.184 , pp. 627-637
    • Allen, L.A.1    Aderem, A.2
  • 2
    • 0028889344 scopus 로고
    • Sorting and intracellular trafficking of a glycosylphosphatidylinositol-anchored protein and two hybrid transmembrane proteins with the same ectodomain in Madin-Darby canine kidney epithelial cells
    • Arreaza G and Brown DA (1995) Sorting and intracellular trafficking of a glycosylphosphatidylinositol-anchored protein and two hybrid transmembrane proteins with the same ectodomain in Madin-Darby canine kidney epithelial cells. J Biol Chem 270:23641-23647.
    • (1995) J Biol Chem , vol.270 , pp. 23641-23647
    • Arreaza, G.1    Brown, D.A.2
  • 3
    • 0031417469 scopus 로고    scopus 로고
    • Redistribution of villin to proximal tubule basolateral membranes after ischemia and reperfusion
    • Brown D, Lee R and Bonventre JV (1997) Redistribution of villin to proximal tubule basolateral membranes after ischemia and reperfusion. Am J Physiol 273:F1003-F1012.
    • (1997) Am J Physiol , vol.273
    • Brown, D.1    Lee, R.2    Bonventre, J.V.3
  • 5
    • 0023036853 scopus 로고
    • Fractionation of the beta subunit common to guanine nucleotide-binding regulatory proteins with the cytoskeleton
    • Carlson KE, Woolkalis MJ, Newhouse MG and Manning DR (1986) Fractionation of the beta subunit common to guanine nucleotide-binding regulatory proteins with the cytoskeleton. Mol Phamacol 30:463-468.
    • (1986) Mol Phamacol , vol.30 , pp. 463-468
    • Carlson, K.E.1    Woolkalis, M.J.2    Newhouse, M.G.3    Manning, D.R.4
  • 6
    • 0027986462 scopus 로고
    • Mutation of an aspartate residue highly conserved among G-protein-coupled receptors results in nonreciprocal disruption of alpha 2-adrenergic receptor-G-protein interactions. A negative charge at amino acid residue 79 forecasts alpha 2A-adrenergic receptor sensitivity to allosteric modulation by monovalent cations and fully effective receptor/G-protein coupling
    • Ceresa BP and Limbird LE (1994) Mutation of an aspartate residue highly conserved among G-protein-coupled receptors results in nonreciprocal disruption of alpha 2-adrenergic receptor-G-protein interactions. A negative charge at amino acid residue 79 forecasts alpha 2A-adrenergic receptor sensitivity to allosteric modulation by monovalent cations and fully effective receptor/G-protein coupling. J Biol Chem 269:29557-29564.
    • (1994) J Biol Chem , vol.269 , pp. 29557-29564
    • Ceresa, B.P.1    Limbird, L.E.2
  • 7
    • 0031689058 scopus 로고    scopus 로고
    • Effect of hypoxic exposure on Na+/H+ antiport activity, isoform expression, and localization in endothelial cells
    • Cutaia MV, Parks N, Centracchio J, Rounds S, Yip KP and Sun AM (1998) Effect of hypoxic exposure on Na+/H+ antiport activity, isoform expression, and localization in endothelial cells. Am J Physiol 275:L442-L451.
    • (1998) Am J Physiol , vol.275
    • Cutaia, M.V.1    Parks, N.2    Centracchio, J.3    Rounds, S.4    Yip, K.P.5    Sun, A.M.6
  • 8
  • 9
    • 0030042764 scopus 로고    scopus 로고
    • Actin filaments facilitate two steps of endocytosis
    • Durrbach A, Louvard D and Coudrier E (1996) Actin filaments facilitate two steps of endocytosis. J Cell Sci 109:457-465.
    • (1996) J Cell Sci , vol.109 , pp. 457-465
    • Durrbach, A.1    Louvard, D.2    Coudrier, E.3
  • 10
    • 0026469352 scopus 로고
    • Subtype-selective desensitization of alpha 2-adrenergic receptors. Different mechanisms control short and long term agonist-promoted desensitization of alpha 2C10, alpha 2C4, and alpha 2C2
    • Eason MG and Liggett SB (1992) Subtype-selective desensitization of alpha 2-adrenergic receptors. Different mechanisms control short and long term agonist-promoted desensitization of alpha 2C10, alpha 2C4, and alpha 2C2. J Biol Chem 267:25473-25479.
    • (1992) J Biol Chem , vol.267 , pp. 25473-25479
    • Eason, M.G.1    Liggett, S.B.2
  • 13
    • 0032100704 scopus 로고    scopus 로고
    • Deficient peptide loading and MHC class II endosomal sorting in a human genetic immunodeficiency disease: The Chediak-Higashi syndrome
    • Faigle W, Raposo G, Tenza D, Pinet V, Vogt AB, Kropshofer H, Fischer A, de Saint-Basile G and Amigorena S (1998) Deficient peptide loading and MHC class II endosomal sorting in a human genetic immunodeficiency disease: The Chediak-Higashi syndrome. J Cell Biol 141:1121-1134.
    • (1998) J Cell Biol , vol.141 , pp. 1121-1134
    • Faigle, W.1    Raposo, G.2    Tenza, D.3    Pinet, V.4    Vogt, A.B.5    Kropshofer, H.6    Fischer, A.7    De Saint-Basile, G.8    Amigorena, S.9
  • 14
    • 0030482560 scopus 로고    scopus 로고
    • Translocation of src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins
    • Fincham VJ, Unlu M, Brunton VG, Pitts JD, Wyke JA and Frame MC (1996) Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins. J Cell Biol 135:1551-1564.
    • (1996) J Cell Biol , vol.135 , pp. 1551-1564
    • Fincham, V.J.1    Unlu, M.2    Brunton, V.G.3    Pitts, J.D.4    Wyke, J.A.5    Frame, M.C.6
  • 17
    • 0029020791 scopus 로고
    • Ischemia induces early changes to the cytoskeleton and contractile proteins in diseased human myocardium
    • Hein S, Scheffold T and Schaper J (1995) Ischemia induces early changes to the cytoskeleton and contractile proteins in diseased human myocardium. J Thorac Cardiovasc Surg 110:89-98.
    • (1995) J Thorac Cardiovasc Surg , vol.110 , pp. 89-98
    • Hein, S.1    Scheffold, T.2    Schaper, J.3
  • 18
    • 0031941873 scopus 로고    scopus 로고
    • Differential mechanism for the cell surface sorting and agonist-promoted internalization of the alpha1B-adrenoceptor
    • Hirasawa A, Awaji T, Sugawara T, Tsujimoto A and Tsujimoto G (1998) Differential mechanism for the cell surface sorting and agonist-promoted internalization of the alpha1B-adrenoceptor. Br J Pharmacol 124:55-62.
    • (1998) Br J Pharmacol , vol.124 , pp. 55-62
    • Hirasawa, A.1    Awaji, T.2    Sugawara, T.3    Tsujimoto, A.4    Tsujimoto, G.5
  • 19
    • 0031850240 scopus 로고    scopus 로고
    • The cytoskeleton and cell signaling: Component localization and mechanical coupling
    • Janmey PA (1998) The cytoskeleton and cell signaling: component localization and mechanical coupling. Physiol Rev 78:763-781.
    • (1998) Physiol Rev , vol.78 , pp. 763-781
    • Janmey, P.A.1
  • 20
    • 0028178404 scopus 로고
    • Unique structural features important for stabilization versus polarization of the alpha 2A-adrenergic receptor on the basolateral membrane of Madin-Darby canine kidney cells
    • Keefer JR, Kennedy ME and Limbird LE (1994) Unique structural features important for stabilization versus polarization of the alpha 2A-adrenergic receptor on the basolateral membrane of Madin-Darby canine kidney cells. J Biol Chem 269:16425-16432.
    • (1994) J Biol Chem , vol.269 , pp. 16425-16432
    • Keefer, J.R.1    Kennedy, M.E.2    Limbird, L.E.3
  • 21
    • 0027302379 scopus 로고
    • The alpha 2A-adrenergic receptor is targeted directly to the basolateral membrane domain of Madin-Darby canine kidney cells independent of coupling to pertussis toxin-sensitive GTP-binding proteins
    • Keefer JR and Limbird LE (1993) The alpha 2A-adrenergic receptor is targeted directly to the basolateral membrane domain of Madin-Darby canine kidney cells independent of coupling to pertussis toxin-sensitive GTP-binding proteins. J Biol Chem 268:11340-11347.
    • (1993) J Biol Chem , vol.268 , pp. 11340-11347
    • Keefer, J.R.1    Limbird, L.E.2
  • 22
    • 0028365270 scopus 로고
    • Differential desensitization and phosphorylation of three cloned and transfected alpha2-adrenergic receptor subtypes
    • Kurose H and Lefkowitz RJ (1994) Differential desensitization and phosphorylation of three cloned and transfected alpha2-adrenergic receptor subtypes. J Biol Chem 269:10093-10099.
    • (1994) J Biol Chem , vol.269 , pp. 10093-10099
    • Kurose, H.1    Lefkowitz, R.J.2
  • 23
    • 0028595709 scopus 로고
    • Involvement of microtubule motors in basolateral and apical transport in kidney cells
    • Lafont F, Burkhardt JK and Simons K (1994) Involvement of microtubule motors in basolateral and apical transport in kidney cells. Nature (Lond) 372:801-803.
    • (1994) Nature (Lond) , vol.372 , pp. 801-803
    • Lafont, F.1    Burkhardt, J.K.2    Simons, K.3
  • 24
    • 0025184423 scopus 로고
    • Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2)
    • Matter K, Buchner K and Hauri H-P (1990) Microtubule perturbation retards both the direct and the indirect apical pathway but does not affect sorting of plasma membrane proteins in intestinal epithelial cells (Caco-2). EMBO J 9:3163-3170.
    • (1990) EMBO J , vol.9 , pp. 3163-3170
    • Matter, K.1    Buchner, K.2    Hauri, H.-P.3
  • 25
    • 33751318939 scopus 로고    scopus 로고
    • Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations
    • Molitoris BA (1997) Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations. Am J Physiol 272:F430-F433.
    • (1997) Am J Physiol , vol.272
    • Molitoris, B.A.1
  • 26
    • 0343546493 scopus 로고
    • Distribution of endogenous G-protein subunits in the plasma membrane of cultured cells
    • Muntz KH, Gilman AG and Mumby SM (1992) Distribution of endogenous G-protein subunits in the plasma membrane of cultured cells. Circulation 86:764.
    • (1992) Circulation , vol.86 , pp. 764
    • Muntz, K.H.1    Gilman, A.G.2    Mumby, S.M.3
  • 27
    • 0024554715 scopus 로고
    • +-ATPase, ankyrin, and fodrn in Madin-Darby canine kidney (MDCK) cells: Implications for biogenesis of epithelial cell polarity
    • +-ATPase, ankyrin, and fodrn in Madin-Darby canine kidney (MDCK) cells: Implications for biogenesis of epithelial cell polarity. J Cell Biol 108:893-901.
    • (1989) J Cell Biol , vol.108 , pp. 893-901
    • Nelson, W.J.1    Hammerton, R.W.2
  • 28
    • 0023267654 scopus 로고
    • Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells
    • Nelson WJ and Veshnock PJ (1987) Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells. J Cell Biol 104:1527-1537.
    • (1987) J Cell Biol , vol.104 , pp. 1527-1537
    • Nelson, W.J.1    Veshnock, P.J.2
  • 31
    • 0031214961 scopus 로고    scopus 로고
    • Endoplasmic reticulum to Golgi trafficking in multinucleated skeletal muscle fibers
    • Rahkila P, Vaananen K, Saraste J and Metsikko K (1997) Endoplasmic reticulum to Golgi trafficking in multinucleated skeletal muscle fibers. Exp Cell Res 234:452-464.
    • (1997) Exp Cell Res , vol.234 , pp. 452-464
    • Rahkila, P.1    Vaananen, K.2    Saraste, J.3    Metsikko, K.4
  • 33
    • 0033532053 scopus 로고    scopus 로고
    • G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics
    • Roychowdhury S, Panda D, Wilson L and Rasenick MM (1999) G protein alpha subunits activate tubulin GTPase and modulate microtubule polymerization dynamics. J Cell Biol 274:13485-13490.
    • (1999) J Cell Biol , vol.274 , pp. 13485-13490
    • Roychowdhury, S.1    Panda, D.2    Wilson, L.3    Rasenick, M.M.4
  • 34
    • 0031282982 scopus 로고    scopus 로고
    • G protein betalgamma2 subunits promote microtubule assembly
    • Roychowdhury S and Rasenick MM (1997) G protein betalgamma2 subunits promote microtubule assembly. J Biol Chem 272:31576-31581.
    • (1997) J Biol Chem , vol.272 , pp. 31576-31581
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 35
    • 0032508487 scopus 로고    scopus 로고
    • Targeting of G protein-coupled receptors to the basolateral surface of polarized renal epithelial cells involves multiple, non-contiguous structural signals
    • Saunders C, Keefer JR, Bonner CA and Limbird LE (1998) Targeting of G protein-coupled receptors to the basolateral surface of polarized renal epithelial cells involves multiple, non-contiguous structural signals. J Biol Chem 273:24196-24206.
    • (1998) J Biol Chem , vol.273 , pp. 24196-24206
    • Saunders, C.1    Keefer, J.R.2    Bonner, C.A.3    Limbird, L.E.4
  • 36
    • 0030026350 scopus 로고    scopus 로고
    • Receptors coupled to pertussis toxin-sensitive G-proteins traffic to opposite surfaces in Madin-Darby canine kidney cells. A1 adenosine receptors achieve apical and alpha 2A adrenergic receptors achieve basolateral localization
    • Saunders C, Keefer JR, Kennedy AP, Wells JN and Limbird LE (1996) Receptors coupled to pertussis toxin-sensitive G-proteins traffic to opposite surfaces in Madin-Darby canine kidney cells. A1 adenosine receptors achieve apical and alpha 2A adrenergic receptors achieve basolateral localization. J Biol Chem 271:995-1002.
    • (1996) J Biol Chem , vol.271 , pp. 995-1002
    • Saunders, C.1    Keefer, J.R.2    Kennedy, A.P.3    Wells, J.N.4    Limbird, L.E.5
  • 37
    • 0030877171 scopus 로고    scopus 로고
    • Disruption of microtubules reveals two independent apical targeting mechanisms for G-protein-coupled receptors in polarized renal epithelial cells
    • Saunders C and Limbird LE (1997) Disruption of microtubules reveals two independent apical targeting mechanisms for G-protein-coupled receptors in polarized renal epithelial cells. J Biol Chem 272:19035-19045.
    • (1997) J Biol Chem , vol.272 , pp. 19035-19045
    • Saunders, C.1    Limbird, L.E.2
  • 39
    • 0033609825 scopus 로고    scopus 로고
    • 2-adrenergic receptors does not require agonist-elicited endocytosis
    • 2-adrenergic receptors does not require agonist-elicited endocytosis. J Biol Chem 274:24935-24940.
    • (1999) J Biol Chem , vol.274 , pp. 24935-24940
    • Schramm, N.L.1    Limbird, L.E.2
  • 40
    • 0018879675 scopus 로고
    • A high affinity agonist-β-adrenergic receptor complex is an intermediate for catecholamine stimulation of adenylate cyclase in turkey and frog erythrocyte membranes
    • Stadel JM, DeLean A and Lefkowitz RJ (1980) A high affinity agonist-β-adrenergic receptor complex is an intermediate for catecholamine stimulation of adenylate cyclase in turkey and frog erythrocyte membranes. J Biol Chem 255:1436-1441.
    • (1980) J Biol Chem , vol.255 , pp. 1436-1441
    • Stadel, J.M.1    DeLean, A.2    Lefkowitz, R.J.3
  • 41
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H and Takai Y (1997) Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J Biol Chem 139:1047-1059.
    • (1997) J Biol Chem , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 42
    • 0030727170 scopus 로고    scopus 로고
    • Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking
    • Thissen JA, Gross JM, Subramanian K, Meyer T and Casey PJ (1997) Prenylation-dependent association of Ki-Ras with microtubules. Evidence for a role in subcellular trafficking. J Biol Chem 272:30362-30370.
    • (1997) J Biol Chem , vol.272 , pp. 30362-30370
    • Thissen, J.A.1    Gross, J.M.2    Subramanian, K.3    Meyer, T.4    Casey, P.J.5
  • 43
    • 0027396746 scopus 로고
    • Subtype-specific differences in the intracellular sorting of G protein-coupled receptors
    • von Zastrow M, Link R, Daunt D, Barsh G and Kobilka B (1993) Subtype-specific differences in the intracellular sorting of G protein-coupled receptors. J Biol Chem 268:763-766.
    • (1993) J Biol Chem , vol.268 , pp. 763-766
    • Von Zastrow, M.1    Link, R.2    Daunt, D.3    Barsh, G.4    Kobilka, B.5
  • 44
    • 0028284289 scopus 로고
    • Multisite interactions of receptors and G proteins: Enhanced potency of dimeric receptor peptides in modifying G protein function
    • Wade SM, Dalman HM, Yang SZ and Neubig RR (1994) Multisite interactions of receptors and G proteins: enhanced potency of dimeric receptor peptides in modifying G protein function. Mol Pharmacol 45:1191-1197.
    • (1994) Mol Pharmacol , vol.45 , pp. 1191-1197
    • Wade, S.M.1    Dalman, H.M.2    Yang, S.Z.3    Neubig, R.R.4
  • 45
    • 0017671339 scopus 로고
    • Slowly reversible binding of catecholamines to a nucleotide-sensitive state of the beta-adrenergic receptor
    • Williams LT and Lefkowitz RJ (1977) Slowly reversible binding of catecholamines to a nucleotide-sensitive state of the beta-adrenergic receptor. J Biol Chem 252: 7207-7213.
    • (1977) J Biol Chem , vol.252 , pp. 7207-7213
    • Williams, L.T.1    Lefkowitz, R.J.2
  • 46
    • 0029670035 scopus 로고    scopus 로고
    • The three alpha 2-adrenergic receptor subtypes achieve basolateral localization in Madin-Darby canine kidney II cells via different targeting mechanisms
    • Wozniak M and Limbird LE (1996) The three alpha 2-adrenergic receptor subtypes achieve basolateral localization in Madin-Darby canine kidney II cells via different targeting mechanisms. J Biol Chem 271:5017-5024.
    • (1996) J Biol Chem , vol.271 , pp. 5017-5024
    • Wozniak, M.1    Limbird, L.E.2


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