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Volumn 7, Issue 8, 2006, Pages 1078-1091

PKCζ is required for microtubule-based motility of vesicles containing the ntcp transporter

Author keywords

Dynein; Endosomes; Kinesin 1; Microtubules; ntcp; PKC ; Recycling

Indexed keywords

CARRIER PROTEIN; DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; KINESIN 1; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE; PROTEIN KINASE C ZETA; PROTEIN KINASE INHIBITOR; PROTEIN NTCP; TAUROCHOLIC ACID; UNCLASSIFIED DRUG; PROTEIN KINASE C;

EID: 33745757459     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2006.00447.x     Document Type: Article
Times cited : (54)

References (56)
  • 1
    • 0037379362 scopus 로고    scopus 로고
    • Bile salt transporters: Molecular characterization, function, and regulation
    • Trauner M, Boyer JL. Bile salt transporters: Molecular characterization, function, and regulation. Physiol Rev 2003; 83: 633-671.
    • (2003) Physiol Rev , vol.83 , pp. 633-671
    • Trauner, M.1    Boyer, J.L.2
  • 2
    • 0037304264 scopus 로고    scopus 로고
    • Bile acid regulation of hepatic physiology: I. Hepatocyte transport of bile acids
    • Wolkoff AW, Cohen DE. Bile acid regulation of hepatic physiology: I. Hepatocyte transport of bile acids. Am J Physiol Gastrointest Liver Physiol 2003; 284: G175-G179.
    • (2003) Am J Physiol Gastrointest Liver Physiol , vol.284
    • Wolkoff, A.W.1    Cohen, D.E.2
  • 3
    • 0346100571 scopus 로고    scopus 로고
    • Enterohepatic bile salt transporters in normal physiology and liver disease
    • Kullak-Ublick GA, Stieger B, Meier PJ. Enterohepatic bile salt transporters in normal physiology and liver disease. Gastroenterology 2004; 126: 322-342.
    • (2004) Gastroenterology , vol.126 , pp. 322-342
    • Kullak-Ublick, G.A.1    Stieger, B.2    Meier, P.J.3
  • 4
    • 1242317691 scopus 로고    scopus 로고
    • The sodium bile salt cotransport family SLC10
    • Hagenbuch B, Dawson P. The sodium bile salt cotransport family SLC10. Pflugers Arch 2004; 447: 566-570.
    • (2004) Pflugers Arch , vol.447 , pp. 566-570
    • Hagenbuch, B.1    Dawson, P.2
  • 5
    • 0141676333 scopus 로고    scopus 로고
    • Cell surface expression and bile acid transport function of one topological form of m-epoxide hydrolase
    • von Dippe P, Zhu QS, Levy D. Cell surface expression and bile acid transport function of one topological form of m-epoxide hydrolase. Biochem Biophys Res Commun 2003; 309: 804-809.
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 804-809
    • von Dippe, P.1    Zhu, Q.S.2    Levy, D.3
  • 6
    • 0019984161 scopus 로고
    • Hepatic uptake of bile acids in man. Fasting and postprandial concentrations of individual bile acids in portal venous and systemic blood serum
    • Angelin B, Bjorkhem I, Einarsson K, Ewerth S. Hepatic uptake of bile acids in man. Fasting and postprandial concentrations of individual bile acids in portal venous and systemic blood serum. J Clin Invest 1982; 70: 724-731.
    • (1982) J Clin Invest , vol.70 , pp. 724-731
    • Angelin, B.1    Bjorkhem, I.2    Einarsson, K.3    Ewerth, S.4
  • 9
    • 0037047389 scopus 로고    scopus 로고
    • Protein kinase B/Akt mediates cAMP- and cell swelling-stimulated Na+/ taurocholate cotransport and Ntcp translocation
    • Webster CR, Srinivasulu U, Ananthanarayanan M, Suchy FJ, Anwer MS. Protein kinase B/Akt mediates cAMP- and cell swelling-stimulated Na+/ taurocholate cotransport and Ntcp translocation. J Biol Chem 2002; 277: 28578-28583.
    • (2002) J Biol Chem , vol.277 , pp. 28578-28583
    • Webster, C.R.1    Srinivasulu, U.2    Ananthanarayanan, M.3    Suchy, F.J.4    Anwer, M.S.5
  • 10
    • 0031738338 scopus 로고    scopus 로고
    • Sodium taurocholate cotransporting polypeptide is a serine, threonine phosphoprotein and is dephosphorylated by cyclic adenosine monophosphate
    • Mukhopadhyay S, Ananthanarayanan M, Stieger B, Meier PJ, Suchy FJ, Anwer MS. Sodium taurocholate cotransporting polypeptide is a serine, threonine phosphoprotein and is dephosphorylated by cyclic adenosine monophosphate. Hepatology 1998; 28: 1629-1636.
    • (1998) Hepatology , vol.28 , pp. 1629-1636
    • Mukhopadhyay, S.1    Ananthanarayanan, M.2    Stieger, B.3    Meier, P.J.4    Suchy, F.J.5    Anwer, M.S.6
  • 11
    • 2442681520 scopus 로고    scopus 로고
    • Cross-talk between protein kinases Czeta and B in cyclic AMP-mediated sodium taurocholate co-transporting polypeptide translocation in hepatocytes
    • McConkey M, Gillin H, Webster CR, Anwer MS. Cross-talk between protein kinases Czeta and B in cyclic AMP-mediated sodium taurocholate co-transporting polypeptide translocation in hepatocytes. J Biol Chem 2004; 279: 20882-20888.
    • (2004) J Biol Chem , vol.279 , pp. 20882-20888
    • McConkey, M.1    Gillin, H.2    Webster, C.R.3    Anwer, M.S.4
  • 13
    • 28544450844 scopus 로고    scopus 로고
    • Glucose transporter 4: Cycling, compartments and controversies
    • Dugani CB, Klip A. Glucose transporter 4: Cycling, compartments and controversies. EMBO Rep 2005; 6: 1137-1142.
    • (2005) EMBO Rep , vol.6 , pp. 1137-1142
    • Dugani, C.B.1    Klip, A.2
  • 14
    • 0034624008 scopus 로고    scopus 로고
    • Perinuclear localization and insulin responsiveness of GLUT4 requires cytoskeletal integrity in 3T3-L1 adipocytes
    • Guilherme A, Emoto M, Buxton JM, Bose S, Sabini R, Theurkauf WE, Leszyk J, Czech MP. Perinuclear localization and insulin responsiveness of GLUT4 requires cytoskeletal integrity in 3T3-L1 adipocytes. J Biol Chem 2000; 275: 38151-38159.
    • (2000) J Biol Chem , vol.275 , pp. 38151-38159
    • Guilherme, A.1    Emoto, M.2    Buxton, J.M.3    Bose, S.4    Sabini, R.5    Theurkauf, W.E.6    Leszyk, J.7    Czech, M.P.8
  • 15
    • 0038451252 scopus 로고    scopus 로고
    • Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin
    • Imamura T, Huang J, Usui I, Satoh H, Bever J, Olefsky JM. Insulin-induced GLUT4 translocation involves protein kinase C-lambda-mediated functional coupling between Rab4 and the motor protein kinesin. Mol Cell Biol 2003; 23: 4892-4900.
    • (2003) Mol Cell Biol , vol.23 , pp. 4892-4900
    • Imamura, T.1    Huang, J.2    Usui, I.3    Satoh, H.4    Bever, J.5    Olefsky, J.M.6
  • 16
    • 0033369266 scopus 로고    scopus 로고
    • Role of the PI3K/PKB signaling pathway in cAMP-mediated translocation of rat liver Ntcp
    • Webster CR, Anwer MS. Role of the PI3K/PKB signaling pathway in cAMP-mediated translocation of rat liver Ntcp. Am J Physiol 1999; 277: G1165-G1172.
    • (1999) Am J Physiol , vol.277
    • Webster, C.R.1    Anwer, M.S.2
  • 17
    • 4344644645 scopus 로고    scopus 로고
    • Separation of insulin signaling into distinct GLUT4 translocation and activation steps
    • Funaki M, Randhawa P, Janmey PA. Separation of insulin signaling into distinct GLUT4 translocation and activation steps. Mol Cell Biol 2004; 24: 7567-7577.
    • (2004) Mol Cell Biol , vol.24 , pp. 7567-7577
    • Funaki, M.1    Randhawa, P.2    Janmey, P.A.3
  • 18
    • 23344431984 scopus 로고    scopus 로고
    • Insulin regulates the membrane arrival, fusion, and C-terminal unmasking of glucose transporter-4 via distinct phosphoinositides
    • Ishiki M, Randhawa VK, Poon V, Jebailey L, Klip A. Insulin regulates the membrane arrival, fusion, and C-terminal unmasking of glucose transporter-4 via distinct phosphoinositides. J Biol Chem 2005; 280: 28792-28802.
    • (2005) J Biol Chem , vol.280 , pp. 28792-28802
    • Ishiki, M.1    Randhawa, V.K.2    Poon, V.3    Jebailey, L.4    Klip, A.5
  • 19
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, Shimizu M, Akimoto K, Izumi Y, Ohnishi T, Ohno S. Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J Cell Biol 2001; 152: 1183-1196.
    • (2001) J Cell Biol , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5    Shimizu, M.6    Akimoto, K.7    Izumi, Y.8    Ohnishi, T.9    Ohno, S.10
  • 20
    • 0034004206 scopus 로고    scopus 로고
    • Reconstitution of ATP-dependent movement of endocytic vesicles along microtubules in vitro: An oscillatory bidirectional process
    • Murray JW, Bananis E, Wolkoff AW. Reconstitution of ATP-dependent movement of endocytic vesicles along microtubules in vitro: An oscillatory bidirectional process. Mol Biol Cell 2000; 11: 419-433.
    • (2000) Mol Biol Cell , vol.11 , pp. 419-433
    • Murray, J.W.1    Bananis, E.2    Wolkoff, A.W.3
  • 21
    • 0036605627 scopus 로고    scopus 로고
    • Immunofluorescence microchamber technique for characterizing isolated organelles
    • Murray JW, Bananis E, Wolkoff AW. Immunofluorescence microchamber technique for characterizing isolated organelles. Anal Biochem 2002; 305: 55-67.
    • (2002) Anal Biochem , vol.305 , pp. 55-67
    • Murray, J.W.1    Bananis, E.2    Wolkoff, A.W.3
  • 22
    • 0038106269 scopus 로고    scopus 로고
    • Regulation of early endocytic vesicle motility and fission in a reconstituted system
    • Bananis E, Murray JW, Stockert RJ, Satir P, Wolkoff AW. Regulation of early endocytic vesicle motility and fission in a reconstituted system. J Cell Sci 2003; 116: 2749-2761.
    • (2003) J Cell Sci , vol.116 , pp. 2749-2761
    • Bananis, E.1    Murray, J.W.2    Stockert, R.J.3    Satir, P.4    Wolkoff, A.W.5
  • 23
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11
    • Sonnichsen B, de Renzis S, Nielsen E, Rietdorf J, Zerial M. Distinct membrane domains on endosomes in the recycling pathway visualized by multicolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 2000; 149: 901-914.
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sonnichsen, B.1    de Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 24
    • 0036172652 scopus 로고    scopus 로고
    • Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes
    • De Renzis S, Sonnichsen B, Zerial M. Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes. Nat Cell Biol 2002; 4: 124-133.
    • (2002) Nat Cell Biol , vol.4 , pp. 124-133
    • De Renzis, S.1    Sonnichsen, B.2    Zerial, M.3
  • 25
    • 0021033757 scopus 로고
    • Intracellular routing of transferrin and transferrin receptors in epidermoid carcinoma A431 cells
    • Hopkins CR. Intracellular routing of transferrin and transferrin receptors in epidermoid carcinoma A431 cells. Cell 1983; 35: 321-330.
    • (1983) Cell , vol.35 , pp. 321-330
    • Hopkins, C.R.1
  • 26
    • 0021734410 scopus 로고
    • Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway
    • Yamashiro DJ, Tycko B, Fluss SR, Maxfield FR. Segregation of transferrin to a mildly acidic (pH 6.5) para-Golgi compartment in the recycling pathway. Cell 1984; 37: 789-800.
    • (1984) Cell , vol.37 , pp. 789-800
    • Yamashiro, D.J.1    Tycko, B.2    Fluss, S.R.3    Maxfield, F.R.4
  • 27
    • 0024842857 scopus 로고
    • Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome
    • Dunn KW, McGraw TE, Maxfield FR. Iterative fractionation of recycling receptors from lysosomally destined ligands in an early sorting endosome. J Cell Biol 1989; 109: 3303-3314.
    • (1989) J Cell Biol , vol.109 , pp. 3303-3314
    • Dunn, K.W.1    McGraw, T.E.2    Maxfield, F.R.3
  • 29
    • 3343021872 scopus 로고    scopus 로고
    • Microtubule-dependent movement of late endocytic vesicles in vitro: Requirements for Dynein and Kinesin
    • Bananis E, Nath S, Gordon K, Satir P, Stockert RJ, Murray JW, Wolkoff AW. Microtubule-dependent movement of late endocytic vesicles in vitro: requirements for Dynein and Kinesin. Mol Biol Cell 2004; 15: 3688-3697.
    • (2004) Mol Biol Cell , vol.15 , pp. 3688-3697
    • Bananis, E.1    Nath, S.2    Gordon, K.3    Satir, P.4    Stockert, R.J.5    Murray, J.W.6    Wolkoff, AW.7
  • 31
    • 0031664962 scopus 로고    scopus 로고
    • In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes
    • Fullerton AT, Bau MY, Conrad PA, Bloom GS. In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes. Mol Biol Cell 1998; 9: 2699-2714.
    • (1998) Mol Biol Cell , vol.9 , pp. 2699-2714
    • Fullerton, A.T.1    Bau, M.Y.2    Conrad, P.A.3    Bloom, G.S.4
  • 32
    • 0018187740 scopus 로고
    • Inhibition of dynein ATPase by vanadate, and its possible use as a probe for the role of dynein in cytoplasmic motility
    • Kobayashi T, Martensen T, Nath J, Flavin M. Inhibition of dynein ATPase by vanadate, and its possible use as a probe for the role of dynein in cytoplasmic motility. Biochem Biophys Res Commun 1978; 81: 1313-1318.
    • (1978) Biochem Biophys Res Commun , vol.81 , pp. 1313-1318
    • Kobayashi, T.1    Martensen, T.2    Nath, J.3    Flavin, M.4
  • 33
    • 2342640469 scopus 로고    scopus 로고
    • A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity
    • Ligon LA, Tokito M, Finklestein JM, Grossman FE, Holzbaur EL. A direct interaction between cytoplasmic dynein and kinesin I may coordinate motor activity. J Biol Chem 2004; 279: 19201-19208.
    • (2004) J Biol Chem , vol.279 , pp. 19201-19208
    • Ligon, L.A.1    Tokito, M.2    Finklestein, J.M.3    Grossman, F.E.4    Holzbaur, E.L.5
  • 34
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Czeta (PKCzeta): Activation mechanisms and cellular functions
    • Hirai T, Chida K. Protein kinase Czeta (PKCzeta): Activation mechanisms and cellular functions. J Biochem (Tokyo) 2003; 133: 1-7.
    • (2003) J Biochem (Tokyo) , vol.133 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 36
    • 27644545878 scopus 로고    scopus 로고
    • Degradation of the sodium taurocholate cotransporting polypeptide (NTCP) by the ubiquitin-proteasome system
    • Kuhlkamp T, Keitel V, Helmer A, Haussinger D, Kubitz R. Degradation of the sodium taurocholate cotransporting polypeptide (NTCP) by the ubiquitin-proteasome system. Biol Chem 2005; 386: 1065-1074.
    • (2005) Biol Chem , vol.386 , pp. 1065-1074
    • Kuhlkamp, T.1    Keitel, V.2    Helmer, A.3    Haussinger, D.4    Kubitz, R.5
  • 37
    • 0034971039 scopus 로고    scopus 로고
    • Cell-specific basolateral membrane sorting of the human liver Na(+)-dependent bile acid cotransporter
    • Sun AQ, Swaby I, Xu S, Suchy FJ. Cell-specific basolateral membrane sorting of the human liver Na(+)-dependent bile acid cotransporter. Am J Physiol Gastrointest Liver Physiol 2001; 280: G1305-G1313.
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.280
    • Sun, A.Q.1    Swaby, I.2    Xu, S.3    Suchy, F.J.4
  • 38
    • 0034611001 scopus 로고    scopus 로고
    • Dynein-mediated cargo transport in vivo. A switch controls travel distance
    • Gross SP, Welte MA, Block SM, Wieschaus EF. Dynein-mediated cargo transport in vivo. A switch controls travel distance. J Cell Biol 2000; 148: 945-956.
    • (2000) J Cell Biol , vol.148 , pp. 945-956
    • Gross, S.P.1    Welte, M.A.2    Block, S.M.3    Wieschaus, E.F.4
  • 39
    • 9244232349 scopus 로고    scopus 로고
    • Molecular motors: Strategies to get along
    • Mallik R, Gross SP. Molecular motors: Strategies to get along. Curr Biol 2004; 14: R971-R982.
    • (2004) Curr Biol , vol.14
    • Mallik, R.1    Gross, S.P.2
  • 40
    • 0027070849 scopus 로고
    • Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins
    • Vale RD, Malik F, Brown D. Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins. J Cell Biol 1992; 119: 1589-1596.
    • (1992) J Cell Biol , vol.119 , pp. 1589-1596
    • Vale, R.D.1    Malik, F.2    Brown, D.3
  • 41
    • 0034079578 scopus 로고    scopus 로고
    • The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity
    • Wang Z, Sheetz MP. The C-terminus of tubulin increases cytoplasmic dynein and kinesin processivity. Biophys J 2000; 78: 1955-1964.
    • (2000) Biophys J , vol.78 , pp. 1955-1964
    • Wang, Z.1    Sheetz, M.P.2
  • 42
    • 0033789351 scopus 로고    scopus 로고
    • Dynactin increases the processivity of the cytoplasmic dynein motor
    • King SJ, Schroer TA. Dynactin increases the processivity of the cytoplasmic dynein motor. Nat Cell Biol 2000; 2: 20-24.
    • (2000) Nat Cell Biol , vol.2 , pp. 20-24
    • King, S.J.1    Schroer, T.A.2
  • 43
    • 0025021497 scopus 로고
    • A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm
    • Brady ST, Pfister KK, Bloom GS. A monoclonal antibody against kinesin inhibits both anterograde and retrograde fast axonal transport in squid axoplasm. Proc Natl Acad Sci USA 1990; 87: 1061-1065.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1061-1065
    • Brady, S.T.1    Pfister, K.K.2    Bloom, G.S.3
  • 44
    • 0032741064 scopus 로고    scopus 로고
    • Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport
    • Martin M, Iyadurai SJ, Gassman A, Gindhart JG Jr, Hays TS, Saxton WM. Cytoplasmic dynein, the dynactin complex, and kinesin are interdependent and essential for fast axonal transport. Mol Biol Cell 1999; 10: 3717-3728.
    • (1999) Mol Biol Cell , vol.10 , pp. 3717-3728
    • Martin, M.1    Iyadurai, S.J.2    Gassman, A.3    Gindhart Jr., J.G.4    Hays, T.S.5    Saxton, W.M.6
  • 45
    • 12544252706 scopus 로고    scopus 로고
    • Impairment of anterograde and retrograde neurofilament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia
    • Theiss C, Napirei M, Meller K. Impairment of anterograde and retrograde neurofilament transport after anti-kinesin and anti-dynein antibody microinjection in chicken dorsal root ganglia. Eur J Cell Biol 2005; 84: 29-43.
    • (2005) Eur J Cell Biol , vol.84 , pp. 29-43
    • Theiss, C.1    Napirei, M.2    Meller, K.3
  • 46
    • 0024997819 scopus 로고
    • Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo
    • Hirokawa N, Sato-Yoshitake R, Yoshida T, Kawashima T. Brain dynein (MAP1C) localizes on both anterogradely and retrogradely transported membranous organelles in vivo. J Cell Biol 1990; 111: 1027-1037.
    • (1990) J Cell Biol , vol.111 , pp. 1027-1037
    • Hirokawa, N.1    Sato-Yoshitake, R.2    Yoshida, T.3    Kawashima, T.4
  • 47
    • 0036538577 scopus 로고    scopus 로고
    • Cytoplasmic dynein-associated structures move bidirectionally in vivo
    • Ma S, Chisholm RL. Cytoplasmic dynein-associated structures move bidirectionally in vivo. J Cell Sci 2002; 115: 1453-1460.
    • (2002) J Cell Sci , vol.115 , pp. 1453-1460
    • Ma, S.1    Chisholm, R.L.2
  • 48
    • 0029872015 scopus 로고    scopus 로고
    • Localization of kinesin and cytoplasmic dynein in cultured melanophores from Atlantic cod, Gadus morhua
    • Nilsson H, Rutberg M, Wallin M. Localization of kinesin and cytoplasmic dynein in cultured melanophores from Atlantic cod, Gadus morhua. Cell Motil Cytoskeleton 1996; 33: 183-196.
    • (1996) Cell Motil Cytoskeleton , vol.33 , pp. 183-196
    • Nilsson, H.1    Rutberg, M.2    Wallin, M.3
  • 49
    • 0027295492 scopus 로고
    • Role of intracellular calcium and protein kinases in the activation of hepatic Na+/taurocholate cotransport by cyclic AMP
    • Grune S, Engelking LR, Anwer MS. Role of intracellular calcium and protein kinases in the activation of hepatic Na+/taurocholate cotransport by cyclic AMP. J Biol Chem 1993; 268: 17734-17741.
    • (1993) J Biol Chem , vol.268 , pp. 17734-17741
    • Grune, S.1    Engelking, L.R.2    Anwer, M.S.3
  • 51
    • 0028889112 scopus 로고
    • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA. Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci USA 1995; 92: 1013-1017.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 52
    • 3042720029 scopus 로고    scopus 로고
    • Intracellular trafficking of bile salt export pump (ABCB11) in polarized hepatic cells: Constitutive cycling between the canalicular membrane and rab11-positive endosomes
    • Wakabayashi Y, Lippincott-Schwartz J, Arias IM. Intracellular trafficking of bile salt export pump (ABCB11) in polarized hepatic cells: Constitutive cycling between the canalicular membrane and rab11-positive endosomes. Mol Biol Cell 2004; 15: 3485-3496.
    • (2004) Mol Biol Cell , vol.15 , pp. 3485-3496
    • Wakabayashi, Y.1    Lippincott-Schwartz, J.2    Arias, I.M.3
  • 53
    • 0028941998 scopus 로고
    • The activation of protein kinase A pathway selectively inhibits anterograde axonal transport of vesicles but not mitochondria transport or retrograde transport in vivo
    • Okada Y, Sato-Yoshitake R, Hirokawa N. The activation of protein kinase A pathway selectively inhibits anterograde axonal transport of vesicles but not mitochondria transport or retrograde transport in vivo. J Neurosci 1995; 15: 3053-3064.
    • (1995) J Neurosci , vol.15 , pp. 3053-3064
    • Okada, Y.1    Sato-Yoshitake, R.2    Hirokawa, N.3
  • 54
    • 0028091983 scopus 로고
    • Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles
    • Dillman JF III, Pfister KK. Differential phosphorylation in vivo of cytoplasmic dynein associated with anterogradely moving organelles. J Cell Biol 1994; 127: 1671-1681.
    • (1994) J Cell Biol , vol.127 , pp. 1671-1681
    • Dillman III, J.F.1    Pfister, K.K.2
  • 55
    • 0033567183 scopus 로고    scopus 로고
    • Increased protein phosphorylation of cytoplasmic dynein results in impaired motor function
    • Runnegar MT, Wei X, Hamm-Alvarez SF. Increased protein phosphorylation of cytoplasmic dynein results in impaired motor function. Biochem J 1999; 342: 1-6.
    • (1999) Biochem J , vol.342 , pp. 1-6
    • Runnegar, M.T.1    Wei, X.2    Hamm-Alvarez, S.F.3


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