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Volumn 25, Issue 7, 2014, Pages 1375-1386

Trafficking to the apical and basolateral membranes in polarized epithelial cells

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84907217196     PISSN: 10466673     EISSN: 15333450     Source Type: Journal    
DOI: 10.1681/ASN.2013080883     Document Type: Review
Times cited : (83)

References (167)
  • 1
    • 0028969528 scopus 로고
    • Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter CE, Connolly CN, Cutler DF, Hopkins CR: Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J BiolChem 270: 10999-11003, 1995
    • (1995) J BiolChem , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 2
    • 0034329456 scopus 로고    scopus 로고
    • A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes
    • Laird V, Spiess M: A novel assay to demonstrate an intersection of the exocytic and endocytic pathways at early endosomes. Exp Cell Res 260: 340-345, 2000
    • (2000) Exp Cell Res , vol.260 , pp. 340-345
    • Laird, V.1    Spiess, M.2
  • 3
    • 16344363943 scopus 로고    scopus 로고
    • Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin
    • Lock JG, Stow JL: Rab11 in recycling endosomes regulates the sorting and basolateral transport of E-cadherin.Mol Biol Cell 16: 1744-1755, 2005
    • (2005) Mol Biol Cell , vol.16 , pp. 1744-1755
    • Lock, J.G.1    Stow, J.L.2
  • 4
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff DR, Daro EA, Hull M, Mellman I: The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J Cell Biol 145: 123-139, 1999
    • (1999) J Cell Biol , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 5
    • 0034139848 scopus 로고    scopus 로고
    • Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membranevolume sorting, polarized sorting and apical recycling
    • Brown PS, Wang E, Aroeti B, Chapin SJ, Mostov KE, Dunn KW: Definition of distinct compartments in polarized Madin-Darby canine kidney (MDCK) cells for membranevolume sorting, polarized sorting and apical recycling. Traffic 1: 124-140, 2000
    • (2000) Traffic , vol.1 , pp. 124-140
    • Brown, P.S.1    Wang, E.2    Aroeti, B.3    Chapin, S.J.4    Mostov, K.E.5    Dunn, K.W.6
  • 6
    • 77958037552 scopus 로고    scopus 로고
    • Sorting it out in endosomes: An emerging concept in renal epithelial cell transport regulation
    • Welling PA, Weisz OA: Sorting it out in endosomes: An emerging concept in renal epithelial cell transport regulation. Physiology (Bethesda) 25: 280-292, 2010
    • (2010) Physiology (Bethesda) , vol.25 , pp. 280-292
    • Welling, P.A.1    Weisz, O.A.2
  • 7
    • 0345687492 scopus 로고    scopus 로고
    • Transport protein trafficking in polarized cells
    • Muth TR, Caplan MJ: Transport protein trafficking in polarized cells. Annu Rev Cell Dev Biol 19: 333-366, 2003
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 333-366
    • Muth, T.R.1    Caplan, M.J.2
  • 8
    • 0026066596 scopus 로고
    • An internal deletion in the cytoplasmic tail reverses the apical localization of human NGF receptor in transfected MDCK cells
    • Le Bivic A, Sambuy Y, Patzak A, Patil N, Chao M, Rodriguez-Boulan E: An internal deletion in the cytoplasmic tail reverses the apical localization of human NGF receptor in transfected MDCK cells. J Cell Biol 115: 607-618, 1991
    • (1991) J Cell Biol , vol.115 , pp. 607-618
    • Le Bivic, A.1    Sambuy, Y.2    Patzak, A.3    Patil, N.4    Chao, M.5    Rodriguez-Boulan, E.6
  • 9
    • 0025939214 scopus 로고
    • Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant
    • Hunziker W, Harter C, Matter K, Mellman I: Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant. Cell 66: 907-920, 1991
    • (1991) Cell , vol.66 , pp. 907-920
    • Hunziker, W.1    Harter, C.2    Matter, K.3    Mellman, I.4
  • 10
    • 0026482992 scopus 로고
    • Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants
    • Matter K, Hunziker W, Mellman I: Basolateral sorting of LDL receptor in MDCK cells: The cytoplasmic domain contains two tyrosine-dependent targeting determinants. Cell 71: 741-753, 1992
    • (1992) Cell , vol.71 , pp. 741-753
    • Matter, K.1    Hunziker, W.2    Mellman, I.3
  • 11
    • 0028200044 scopus 로고
    • A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells
    • Hunziker W, Fumey C: A di-leucine motif mediates endocytosis and basolateral sorting of macrophage IgG Fc receptors in MDCK cells. EMBO J 13: 2963-2969, 1994
    • (1994) EMBO J , vol.13 , pp. 2963-2969
    • Hunziker, W.1    Fumey, C.2
  • 12
    • 0035933872 scopus 로고    scopus 로고
    • A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Miranda KC, Khromykh T, Christy P, Le TL, Gottardi CJ, Yap AS, Stow JL, Teasdale RD: A dileucine motif targets E-cadherin to the basolateral cell surface in Madin-Darby canine kidney and LLC-PK1 epithelial cells. J Biol Chem 276: 22565-22572, 2001
    • (2001) J Biol Chem , vol.276 , pp. 22565-22572
    • Miranda, K.C.1    Khromykh, T.2    Christy, P.3    Le, T.L.4    Gottardi, C.J.5    Yap, A.S.6    Stow, J.L.7    Teasdale, R.D.8
  • 13
    • 0025913946 scopus 로고
    • A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin
    • Brewer CB, Roth MG: A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza virus hemagglutinin. J Cell Biol 114: 413-421, 1991
    • (1991) J Cell Biol , vol.114 , pp. 413-421
    • Brewer, C.B.1    Roth, M.G.2
  • 14
    • 0027276052 scopus 로고
    • The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells
    • Prill V, Lehmann L, von Figura K, Peters C: The cytoplasmic tail of lysosomal acid phosphatase contains overlapping but distinct signals for basolateral sorting and rapid internalization in polarized MDCK cells. EMBO J 12: 2181-2193, 1993
    • (1993) EMBO J , vol.12 , pp. 2181-2193
    • Prill, V.1    Lehmann, L.2    Von Figura, K.3    Peters, C.4
  • 15
    • 0027989516 scopus 로고
    • Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells
    • Matter K, Yamamoto EM, Mellman I: Structural requirements and sequence motifs for polarized sorting and endocytosis of LDL and Fc receptors in MDCK cells. J Cell Biol 126: 991-1004, 1994
    • (1994) J Cell Biol , vol.126 , pp. 991-1004
    • Matter, K.1    Yamamoto, E.M.2    Mellman, I.3
  • 16
    • 0031780959 scopus 로고    scopus 로고
    • The leucine-basedmotif DDQxxLI is recognized both for internalization and basolateral sorting of invariant chain in MDCK cells
    • Simonsen A, Bremnes B, Nordeng TW, BakkeO: The leucine-basedmotif DDQxxLI is recognized both for internalization and basolateral sorting of invariant chain in MDCK cells. Eur J Cell Biol 76: 25-32, 1998
    • (1998) Eur J Cell Biol , vol.76 , pp. 25-32
    • Simonsen, A.1    Bremnes, B.2    Nordeng, T.W.3    Bakke, O.4
  • 17
    • 0028985176 scopus 로고
    • Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals
    • Haass C, Koo EH, Capell A, Teplow DB, Selkoe DJ: Polarized sorting of beta-amyloid precursor protein and its proteolytic products in MDCK cells is regulated by two independent signals. J Cell Biol 128: 537-547, 1995
    • (1995) J Cell Biol , vol.128 , pp. 537-547
    • Haass, C.1    Koo, E.H.2    Capell, A.3    Teplow, D.B.4    Selkoe, D.J.5
  • 18
    • 0028217859 scopus 로고
    • The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities
    • Thomas DC, Roth MG: The basolateral targeting signal in the cytoplasmic domain of glycoprotein G from vesicular stomatitis virus resembles a variety of intracellular targeting motifs related by primary sequence but having diverse targeting activities. J Biol Chem 269: 15732-15739, 1994
    • (1994) J Biol Chem , vol.269 , pp. 15732-15739
    • Thomas, D.C.1    Roth, M.G.2
  • 19
    • 0035918242 scopus 로고    scopus 로고
    • Stem cell factor presentation to c-Kit. Identification of a basolateral targeting domain
    • Wehrle-Haller B, Imhof BA: Stem cell factor presentation to c-Kit. Identification of a basolateral targeting domain. J Biol Chem 276: 12667-12674, 2001
    • (2001) J Biol Chem , vol.276 , pp. 12667-12674
    • Wehrle-Haller, B.1    Imhof, B.A.2
  • 20
    • 4344713234 scopus 로고    scopus 로고
    • The basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium
    • Deora AA, Gravotta D, Kreitzer G, Hu J, Bok D, Rodriguez-Boulan E: The basolateral targeting signal of CD147 (EMMPRIN) consists of a single leucine and is not recognized by retinal pigment epithelium. Mol Biol Cell 15: 4148-4165, 2004
    • (2004) Mol Biol Cell , vol.15 , pp. 4148-4165
    • Deora, A.A.1    Gravotta, D.2    Kreitzer, G.3    Hu, J.4    Bok, D.5    Rodriguez-Boulan, E.6
  • 21
    • 81055156722 scopus 로고    scopus 로고
    • Identification of a novel mono-leucine basolateral sorting motif within the cytoplasmic domain of amphiregulin
    • Gephart JD, Singh B, Higginbotham JN, Franklin JL, González A, Fölsch H, Coffey RJ: Identification of a novel mono-leucine basolateral sorting motif within the cytoplasmic domain of amphiregulin. Traffic 12: 1793-1804, 2011
    • (2011) Traffic , vol.12 , pp. 1793-1804
    • Gephart, J.D.1    Singh, B.2    Higginbotham, J.N.3    Franklin, J.L.4    González, A.5    Fölsch, H.6    Coffey, R.J.7
  • 23
    • 0029379646 scopus 로고
    • Role of the regulatory domain of the EGF-receptor cytoplasmic tail in selective binding of the clathrin-associated complex AP-2
    • Boll W, Gallusser A, Kirchhausen T: Role of the regulatory domain of the EGF-receptor cytoplasmic tail in selective binding of the clathrin-associated complex AP-2. Curr Biol 5: 1168-1178, 1995
    • (1995) Curr Biol , vol.5 , pp. 1168-1178
    • Boll, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 24
    • 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 JF, Spiess M: In vitro binding of clathrin adaptors to sorting signals correlates with endocytosis and basolateral sorting. EMBO J 15: 2893-2899, 1996
    • (1996) EMBO J , vol.15 , pp. 2893-2899
    • Heilker, R.1    Manning-Krieg, U.2    Zuber, J.F.3    Spiess, M.4
  • 25
    • 0024120843 scopus 로고
    • Receptors compete for adaptors found in plasmamembrane coated pits
    • Pearse BM: Receptors compete for adaptors found in plasmamembrane coated pits. EMBO J 7: 3331-3336, 1988
    • (1988) EMBO J , vol.7 , pp. 3331-3336
    • Pearse, B.M.1
  • 26
    • 0024468967 scopus 로고
    • Specificity of binding of clathrin adaptors to signals on themannose-6-phosphate/insulinlikegrowth factor II receptor
    • Glickman JN, Conibear E, Pearse BM: Specificity of binding of clathrin adaptors to signals on themannose-6-phosphate/insulinlikegrowth factor II receptor.EMBOJ 8: 1041-1047, 1989
    • (1989) EMBOJ , vol.8 , pp. 1041-1047
    • Glickman, J.N.1    Conibear, E.2    Pearse, B.M.3
  • 27
    • 0027180886 scopus 로고
    • In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase
    • Sosa MA, Schmidt B, von Figura K, Hille- Rehfeld A: In vitro binding of plasma membrane-coated vesicle adaptors to the cytoplasmic domain of lysosomal acid phosphatase. J Biol Chem 268: 12537-12543, 1993
    • (1993) J Biol Chem , vol.268 , pp. 12537-12543
    • Sosa, M.A.1    Schmidt, B.2    Von Figura, K.3    Hille- Rehfeld, A.4
  • 28
    • 0027249993 scopus 로고
    • Interaction of activated EGF receptors with coated pit adaptins
    • Sorkin A, Carpenter G: Interaction of activated EGF receptors with coated pit adaptins. Science 261: 612-615, 1993
    • (1993) Science , vol.261 , pp. 612-615
    • Sorkin, A.1    Carpenter, G.2
  • 29
    • 0028944988 scopus 로고
    • Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2
    • Sorkin A, McKinsey T, Shih W, Kirchhausen T, Carpenter G: Stoichiometric interaction of the epidermal growth factor receptor with the clathrin-associated protein complex AP-2. J Biol Chem270: 619-625, 1995
    • (1995) J Biol Chem , vol.270 , pp. 619-625
    • Sorkin, A.1    McKinsey, T.2    Shih, W.3    Kirchhausen, T.4    Carpenter, G.5
  • 30
    • 0030794182 scopus 로고    scopus 로고
    • Linking cargo to vesicle formation: Receptor tail interactions with coat proteins
    • Kirchhausen T, Bonifacino JS, Riezman H: Linking cargo to vesicle formation: receptor tail interactions with coat proteins. Curr Opin Cell Biol 9: 488-495, 1997
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 488-495
    • Kirchhausen, T.1    Bonifacino, J.S.2    Riezman, H.3
  • 31
    • 34248175894 scopus 로고    scopus 로고
    • Conformational changes of coat proteins during vesicle formation
    • Langer JD, Stoops EH, Béthune J, Wieland FT: Conformational changes of coat proteins during vesicle formation. FEBS Lett 581: 2083-2088, 2007
    • (2007) FEBS Lett , vol.581 , pp. 2083-2088
    • Langer, J.D.1    Stoops, E.H.2    Béthune, J.3    Wieland, F.T.4
  • 33
    • 0032692619 scopus 로고    scopus 로고
    • A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells
    • Fölsch H, Ohno H, Bonifacino JS, Mellman I: A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99: 189-198, 1999
    • (1999) Cell , vol.99 , pp. 189-198
    • Fölsch, H.1    Ohno, H.2    Bonifacino, J.S.3    Mellman, I.4
  • 35
    • 18144438853 scopus 로고
    • A role for the beta-subunit in the expression of functional Na+-K+-ATPase in Xenopus oocytes
    • Geering K, Theulaz I, Verrey F, Häuptle MT, Rossier BC: A role for the beta-subunit in the expression of functional Na+-K+-ATPase in Xenopus oocytes. Am J Physiol 257: C851-C858, 1989
    • (1989) Am J Physiol , vol.257 , pp. C851-C858
    • Geering, K.1    Theulaz, I.2    Verrey, F.3    Häuptle, M.T.4    Rossier, B.C.5
  • 36
    • 0027210894 scopus 로고
    • Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na, K-ATPase and H, K-ATPase subunit assembly
    • Gottardi CJ, Caplan MJ: Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na, K-ATPase and H, K-ATPase subunit assembly. J BiolChem268: 14342-14347, 1993
    • (1993) J BiolChem , vol.268 , pp. 14342-14347
    • Gottardi, C.J.1    Caplan, M.J.2
  • 37
    • 84863992161 scopus 로고    scopus 로고
    • Scoring a backstage pass: Mechanisms of ciliogenesis and ciliary access
    • Garcia-Gonzalo FR, Reiter JF: Scoring a backstage pass: Mechanisms of ciliogenesis and ciliary access. J Cell Biol 197: 697-709, 2012
    • (2012) J Cell Biol , vol.197 , pp. 697-709
    • Garcia-Gonzalo, F.R.1    Reiter, J.F.2
  • 38
    • 0000441994 scopus 로고
    • Polarized apical distribution of glycosyl-phosphatidylinositolanchored proteins in a renal epithelial cell line
    • Lisanti MP, Sargiacomo M, Graeve L, Saltiel AR, Rodriguez-Boulan E: Polarized apical distribution of glycosyl-phosphatidylinositolanchored proteins in a renal epithelial cell line. Proc Natl Acad SciUS A85: 9557-9561, 1988
    • (1988) Proc Natl Acad SciUS , vol.A85 , pp. 9557-9561
    • Lisanti, M.P.1    Sargiacomo, M.2    Graeve, L.3    Saltiel, A.R.4    Rodriguez-Boulan, E.5
  • 39
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown DA, Crise B, Rose JK: Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 245: 1499-1501, 1989
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 40
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti MP, Caras IW, DavitzMA, Rodriguez- Boulan E: A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J Cell Biol 109: 2145-2156, 1989
    • (1989) J Cell Biol , vol.109 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 41
    • 0036195484 scopus 로고    scopus 로고
    • Detergent- resistant membrane microdomains and apical sorting of GPI-anchored proteins in polarized epithelial cells
    • Paladino S, Sarnataro D, Zurzolo C: Detergent- resistant membrane microdomains and apical sorting of GPI-anchored proteins in polarized epithelial cells. Int J Med Microbiol 291: 439-445, 2002
    • (2002) Int J Med Microbiol , vol.291 , pp. 439-445
    • Paladino, S.1    Sarnataro, D.2    Zurzolo, C.3
  • 42
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown DA, Rose JK: Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68: 533-544, 1992
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 43
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S, Sarnataro D, Pillich R, Tivodar S, Nitsch L, Zurzolo C: Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J Cell Biol 167: 699-709, 2004
    • (2004) J Cell Biol , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 44
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons K, van Meer G: Lipid sorting in epithelial cells. Biochemistry 27: 6197-6202, 1988
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 45
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons K, Wandinger-Ness A: Polarized sorting in epithelia. Cell 62: 207-210, 1990
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 46
    • 0023544865 scopus 로고
    • Constitutive apical secretion of an 80-kD sulfated glycoprotein complex in the polarized epithelial Madin- Darby canine kidney cell line
    • Urban J, Parczyk K, Leutz A, Kayne M, Kondor-Koch C: Constitutive apical secretion of an 80-kD sulfated glycoprotein complex in the polarized epithelial Madin- Darby canine kidney cell line. J Cell Biol 105: 2735-2743, 1987
    • (1987) J Cell Biol , vol.105 , pp. 2735-2743
    • Urban, J.1    Parczyk, K.2    Leutz, A.3    Kayne, M.4    Kondor-Koch, C.5
  • 47
    • 0027478019 scopus 로고
    • Ricin-resistant Madin-Darby canine kidney cells missort a major endogenous apical sialoglycoprotein
    • Le Bivic A, Garcia M, Rodriguez-Boulan E: Ricin-resistant Madin-Darby canine kidney cells missort a major endogenous apical sialoglycoprotein. J Biol Chem 268: 6909-6916, 1993
    • (1993) J Biol Chem , vol.268 , pp. 6909-6916
    • Le Bivic, A.1    Garcia, M.2    Rodriguez-Boulan, E.3
  • 48
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele P, Peränen J, Simons K: N-glycans as apical sorting signals in epithelial cells. Nature 378: 96-98, 1995
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Peränen, J.2    Simons, K.3
  • 50
    • 0035890138 scopus 로고    scopus 로고
    • Competing sorting signals guide endolyn along a novel route to lysosomes in MDCK cells
    • Ihrke G, Bruns JR, Luzio JP, Weisz OA: Competing sorting signals guide endolyn along a novel route to lysosomes in MDCK cells. EMBO J 20: 6256-6264, 2001
    • (2001) EMBO J , vol.20 , pp. 6256-6264
    • Ihrke, G.1    Bruns, J.R.2    Luzio, J.P.3    Weisz, O.A.4
  • 51
    • 0035910514 scopus 로고    scopus 로고
    • The role of N-glycosylation in transport to the plasma membrane and sorting of the neuronal glycine transporter GLYT2
    • Martínez-Maza R, Poyatos I, López-Corcuera B, N úñez E, Giménez C, Zafra F, Aragón C: The role of N-glycosylation in transport to the plasma membrane and sorting of the neuronal glycine transporter GLYT2. J Biol Chem 276: 2168-2173, 2001
    • (2001) J Biol Chem , vol.276 , pp. 2168-2173
    • Martínez-Maza, R.1    Poyatos, I.2    López-Corcuera, B.3    Úñez E, N.4    Giménez, C.5    Zafra, F.6    Aragón, C.7
  • 53
    • 0030726211 scopus 로고    scopus 로고
    • The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells
    • Yeaman C, Le Gall AH, Baldwin AN, Monlauzeur L, Le Bivic A, Rodriguez-Boulan E: The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J Cell Biol 139: 929-940, 1997
    • (1997) J Cell Biol , vol.139 , pp. 929-940
    • Yeaman, C.1    Le Gall, A.H.2    Baldwin, A.N.3    Monlauzeur, L.4    Le Bivic, A.5    Rodriguez-Boulan, E.6
  • 55
    • 0033580927 scopus 로고    scopus 로고
    • Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV
    • Naim HY, Joberty G, Alfalah M, Jacob R: Temporal association of the N- and O-linked glycosylation events and their implication in the polarized sorting of intestinal brush border sucrase-isomaltase, aminopeptidase N, and dipeptidyl peptidase IV. J Biol Chem 274: 17961-17967, 1999
    • (1999) J Biol Chem , vol.274 , pp. 17961-17967
    • Naim, H.Y.1    Joberty, G.2    Alfalah, M.3    Jacob, R.4
  • 56
    • 0033519624 scopus 로고    scopus 로고
    • O-linked glycans mediate apical sorting of human intestinal sucraseisomaltase through associationwith lipidrafts
    • Alfalah M, Jacob R, Preuss U, Zimmer KP, Naim H, Naim HY: O-linked glycans mediate apical sorting of human intestinal sucraseisomaltase through associationwith lipidrafts. Curr Biol 9: 593-596, 1999
    • (1999) Curr Biol , vol.9 , pp. 593-596
    • Alfalah, M.1    Jacob, R.2    Preuss, U.3    Zimmer, K.P.4    Naim, H.5    Naim, H.Y.6
  • 57
    • 0035824619 scopus 로고    scopus 로고
    • Characteristics and structural requirements of apical sorting of the rat growth hormone through the O-glycosylated stalk region of intestinal sucrase-isomaltase
    • Spodsberg N, Alfalah M, Naim HY: Characteristics and structural requirements of apical sorting of the rat growth hormone through the O-glycosylated stalk region of intestinal sucrase-isomaltase. J Biol Chem 276: 46597-46604, 2001
    • (2001) J Biol Chem , vol.276 , pp. 46597-46604
    • Spodsberg, N.1    Alfalah, M.2    Naim, H.Y.3
  • 58
    • 0342323003 scopus 로고    scopus 로고
    • Apical secretion and sialylation of soluble dipeptidyl peptidase IV are two related events
    • Slimane TA, Lenoir C, Sapin C, Maurice M, Trugnan G: Apical secretion and sialylation of soluble dipeptidyl peptidase IV are two related events. Exp Cell Res 258: 184-194, 2000
    • (2000) Exp Cell Res , vol.258 , pp. 184-194
    • Slimane, T.A.1    Lenoir, C.2    Sapin, C.3    Maurice, M.4    Trugnan, G.5
  • 59
    • 66049115017 scopus 로고    scopus 로고
    • Role of Nglycosylation in trafficking of apical membrane proteins in epithelia
    • Vagin O, Kraut JA, Sachs G: Role of Nglycosylation in trafficking of apical membrane proteins in epithelia. Am J Physiol Renal Physiol 296: F459-F469, 2009
    • (2009) Am J Physiol Renal Physiol , vol.296 , pp. F459-F469
    • Vagin, O.1    Kraut, J.A.2    Sachs, G.3
  • 60
    • 70350428098 scopus 로고    scopus 로고
    • The role of galectins in protein trafficking
    • Delacour D, Koch A, Jacob R: The role of galectins in protein trafficking. Traffic 10: 1405-1413, 2009
    • (2009) Traffic , vol.10 , pp. 1405-1413
    • Delacour, D.1    Koch, A.2    Jacob, R.3
  • 63
    • 78049312395 scopus 로고    scopus 로고
    • Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells
    • Mishra R, Grzybek M, Niki T, Hirashima M, Simons K: Galectin-9 trafficking regulates apical-basal polarity in Madin-Darby canine kidney epithelial cells. Proc Natl Acad Sci U S A 107: 17633-17638, 2010
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 17633-17638
    • Mishra, R.1    Grzybek, M.2    Niki, T.3    Hirashima, M.4    Simons, K.5
  • 64
    • 84866351431 scopus 로고    scopus 로고
    • Sialylation of N-linked glycansmediates apical delivery of endolyn in MDCK cells via a galectin-9- dependent mechanism
    • Mo D, Costa SA, Ihrke G, Youker RT, Pastor- Soler N, Hughey RP, Weisz OA: Sialylation of N-linked glycansmediates apical delivery of endolyn in MDCK cells via a galectin-9- dependent mechanism. Mol Biol Cell 23: 3636-3646, 2012
    • (2012) Mol Biol Cell , vol.23 , pp. 3636-3646
    • Mo, D.1    Costa, S.A.2    Ihrke, G.3    Youker, R.T.4    Pastor- Soler, N.5    Hughey, R.P.6    Weisz, O.A.7
  • 66
    • 0033179221 scopus 로고    scopus 로고
    • Glycans in post-Golgi apical targeting: Sorting signals or structural props?
    • Rodriguez-Boulan E, Gonzalez A:Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol 9: 291-294, 1999
    • (1999) Trends Cell Biol , vol.9 , pp. 291-294
    • Rodriguez-Boulan, E.1    Gonzalez, A.2
  • 67
    • 0029839393 scopus 로고    scopus 로고
    • Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
    • Kundu A, Avalos RT, Sanderson CM, Nayak DP: Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells. J Virol 70: 6508-6515, 1996
    • (1996) J Virol , vol.70 , pp. 6508-6515
    • Kundu, A.1    Avalos, R.T.2    Sanderson, C.M.3    Nayak, D.P.4
  • 68
    • 0030736714 scopus 로고    scopus 로고
    • Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase
    • Huang XF, Compans RW, Chen S, Lamb RA, Arvan P: Polarized apical targeting directed by the signal/anchor region of simian virus 5 hemagglutinin-neuraminidase. J BiolChem 272: 27598-27604, 1997
    • (1997) J BiolChem , vol.272 , pp. 27598-27604
    • Huang, X.F.1    Compans, R.W.2    Chen, S.3    Lamb, R.A.4    Arvan, P.5
  • 69
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin inMDCK epithelial cells
    • Lin S, Naim HY, Rodriguez AC, Roth MG: Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin inMDCK epithelial cells. J Cell Biol 142: 51-57, 1998
    • (1998) J Cell Biol , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 70
    • 0033934725 scopus 로고    scopus 로고
    • Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association
    • Barman S, Nayak DP: Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association. J Virol 74: 6538-6545, 2000
    • (2000) J Virol , vol.74 , pp. 6538-6545
    • Barman, S.1    Nayak, D.P.2
  • 71
    • 25144446791 scopus 로고    scopus 로고
    • The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasmamembrane sorting sequence
    • Brock SC, Heck JM, McGraw PA, Crowe JE Jr: The transmembrane domain of the respiratory syncytial virus F protein is an orientation-independent apical plasmamembrane sorting sequence. J Virol 79: 12528-12535, 2005
    • (2005) J Virol , vol.79 , pp. 12528-12535
    • Brock, S.C.1    Heck, J.M.2    McGraw, P.A.3    Crowe, J.E.4
  • 72
    • 0034695917 scopus 로고    scopus 로고
    • A transmembrane segment determines the steadystate localization of an ion-transporting adenosine triphosphatase
    • Dunbar LA, Aronson P, Caplan MJ: A transmembrane segment determines the steadystate localization of an ion-transporting adenosine triphosphatase. J Cell Biol 148: 769-778, 2000
    • (2000) J Cell Biol , vol.148 , pp. 769-778
    • Dunbar, L.A.1    Aronson, P.2    Caplan, M.J.3
  • 73
    • 0022995601 scopus 로고
    • Molecular cloning of the rat stomach (H+ + K+)-ATPase
    • Shull GE, Lingrel JB: Molecular cloning of the rat stomach (H+ + K+)-ATPase. J Biol Chem 261: 16788-16791, 1986
    • (1986) J Biol Chem , vol.261 , pp. 16788-16791
    • Shull, G.E.1    Lingrel, J.B.2
  • 74
    • 0346752326 scopus 로고    scopus 로고
    • Features of influenza HA required for apical sorting differ from those required for association with DRMs orMAL
    • Tall RD, Alonso MA, Roth MG: Features of influenza HA required for apical sorting differ from those required for association with DRMs orMAL. Traffic 4: 838-849, 2003
    • (2003) Traffic , vol.4 , pp. 838-849
    • Tall, R.D.1    Alonso, M.A.2    Roth, M.G.3
  • 75
    • 0034003908 scopus 로고    scopus 로고
    • Detergentinsoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting
    • Lipardi C, Nitsch L, Zurzolo C: Detergentinsoluble GPI-anchored proteins are apically sorted in fischer rat thyroid cells, but interference with cholesterol or sphingolipids differentially affects detergent insolubility and apical sorting. Mol Biol Cell 11: 531-542, 2000
    • (2000) Mol Biol Cell , vol.11 , pp. 531-542
    • Lipardi, C.1    Nitsch, L.2    Zurzolo, C.3
  • 76
    • 8744246234 scopus 로고    scopus 로고
    • N-glycans, not the GPI anchor, mediate the apical targeting of a naturally glycosylated, GPIanchored protein in polarised epithelial cells
    • Pang S, Urquhart P, Hooper NM: N-glycans, not the GPI anchor, mediate the apical targeting of a naturally glycosylated, GPIanchored protein in polarised epithelial cells. J Cell Sci 117: 5079-5086, 2004
    • (2004) J Cell Sci , vol.117 , pp. 5079-5086
    • Pang, S.1    Urquhart, P.2    Hooper, N.M.3
  • 78
    • 0022021158 scopus 로고
    • An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments
    • Fuller SD, Bravo R, Simons K: An enzymatic assay reveals that proteins destined for the apical or basolateral domains of an epithelial cell line share the same late Golgi compartments. EMBOJ 4: 297-307, 1985
    • (1985) EMBOJ , vol.4 , pp. 297-307
    • Fuller, S.D.1    Bravo, R.2    Simons, K.3
  • 79
    • 0021186349 scopus 로고
    • Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells
    • Rindler MJ, Ivanov IE, PleskenH, Rodriguez- Boulan E, Sabatini DD: Viral glycoproteins destined for apical or basolateral plasma membrane domains traverse the same Golgi apparatus during their intracellular transport in doubly infected Madin-Darby canine kidney cells. J Cell Biol 98: 1304-1319, 1984
    • (1984) J Cell Biol , vol.98 , pp. 1304-1319
    • Rindler, M.J.1    Ivanov, I.E.2    Plesken, H.3    Rodriguez-Boulan, E.4    Sabatini, D.D.5
  • 80
    • 23844520920 scopus 로고    scopus 로고
    • A proteoglycan undergoes different modifications en route to the apical and basolateral surfaces of Madin-Darby canine kidney cells
    • Tveit H, Dick G, Skibeli V, Prydz K: A proteoglycan undergoes different modifications en route to the apical and basolateral surfaces of Madin-Darby canine kidney cells. J Biol Chem 280: 29596-29603, 2005
    • (2005) J Biol Chem , vol.280 , pp. 29596-29603
    • Tveit, H.1    Dick, G.2    Skibeli, V.3    Prydz, K.4
  • 81
    • 33645100455 scopus 로고    scopus 로고
    • Differences in the apical and basolateral pathways for glycosaminoglycan biosynthesis in Madin- Darby canine kidney cells
    • Vuong TT, Prydz K, Tveit H: Differences in the apical and basolateral pathways for glycosaminoglycan biosynthesis in Madin- Darby canine kidney cells. Glycobiology 16: 326-332, 2006
    • (2006) Glycobiology , vol.16 , pp. 326-332
    • Vuong, T.T.1    Prydz, K.2    Tveit, H.3
  • 83
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muñiz M, Morsomme P, Riezman H: Protein sorting upon exit from the endoplasmic reticulum. Cell 104: 313-320, 2001
    • (2001) Cell , vol.104 , pp. 313-320
    • Muñiz, M.1    Morsomme, P.2    Riezman, H.3
  • 85
    • 0035908953 scopus 로고    scopus 로고
    • Apical membrane proteins are transported in distinct vesicular carriers
    • Jacob R, Naim HY: Apical membrane proteins are transported in distinct vesicular carriers. Curr Biol 11: 1444-1450, 2001
    • (2001) Curr Biol , vol.11 , pp. 1444-1450
    • Jacob, R.1    Naim, H.Y.2
  • 86
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller P, Toomre D, Díaz E, White J, Simons K: Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol 3: 140-149, 2001
    • (2001) Nat Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Díaz, E.3    White, J.4    Simons, K.5
  • 87
    • 67749145291 scopus 로고    scopus 로고
    • Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells
    • Farr GA, Hull M, Mellman I, Caplan MJ: Membrane proteins follow multiple pathways to the basolateral cell surface in polarized epithelial cells. J Cell Biol 186: 269-282, 2009
    • (2009) J Cell Biol , vol.186 , pp. 269-282
    • Farr, G.A.1    Hull, M.2    Mellman, I.3    Caplan, M.J.4
  • 88
    • 8444221583 scopus 로고    scopus 로고
    • Recycling endosomes can serve as intermediates during transport fromthe Golgi to the plasmamembrane ofMDCK cells
    • Ang AL, Taguchi T, Francis S, Fölsch H, Murrells LJ, Pypaert M, Warren G, Mellman I: Recycling endosomes can serve as intermediates during transport fromthe Golgi to the plasmamembrane ofMDCK cells.JCell Biol 167: 531-543, 2004
    • (2004) JCell Biol , vol.167 , pp. 531-543
    • Ang, A.L.1    Taguchi, T.2    Francis, S.3    Fölsch, H.4    Murrells, L.J.5    Pypaert, M.6    Warren, G.7    Mellman, I.8
  • 90
    • 84875275175 scopus 로고    scopus 로고
    • Arrivals and departures at the plasma membrane: Direct and indirect transport routes
    • Prydz K, Tveit H, Vedeler A, Saraste J: Arrivals and departures at the plasma membrane: direct and indirect transport routes. Cell Tissue Res 352: 5-20, 2013
    • (2013) Cell Tissue Res , vol.352 , pp. 5-20
    • Prydz, K.1    Tveit, H.2    Vedeler, A.3    Saraste, J.4
  • 92
    • 70350632412 scopus 로고    scopus 로고
    • A secretoryGolgi bypass route to the apical surface domain of epithelial MDCK cells
    • Tveit H, Akslen LKA, Fagereng GL, Tranulis MA, Prydz K: A secretoryGolgi bypass route to the apical surface domain of epithelial MDCK cells. Traffic 10: 1685-1695, 2009
    • (2009) Traffic , vol.10 , pp. 1685-1695
    • Tveit, H.1    Akslen, L.K.A.2    Fagereng, G.L.3    Tranulis, M.A.4    Prydz, K.5
  • 94
    • 0023608934 scopus 로고
    • Biogenesis of the rat hepatocyte plasma membrane in vivo: Comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation
    • Bartles JR, Feracci HM, Stieger B, Hubbard AL: Biogenesis of the rat hepatocyte plasma membrane in vivo: comparison of the pathways taken by apical and basolateral proteins using subcellular fractionation. J Cell Biol 105: 1241-1251, 1987
    • (1987) J Cell Biol , vol.105 , pp. 1241-1251
    • Bartles, J.R.1    Feracci, H.M.2    Stieger, B.3    Hubbard, A.L.4
  • 95
    • 0036156444 scopus 로고    scopus 로고
    • Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes
    • Sheff DR, Kroschewski R, Mellman I: Actin dependence of polarized receptor recycling in Madin-Darby canine kidney cell endosomes. Mol Biol Cell 13: 262-275, 2002
    • (2002) Mol Biol Cell , vol.13 , pp. 262-275
    • Sheff, D.R.1    Kroschewski, R.2    Mellman, I.3
  • 97
    • 0142026241 scopus 로고    scopus 로고
    • Rab11b resides in a vesicular compartment distinct from Rab11a in parietal cells and other epithelial cells
    • Lapierre LA, Dorn MC, Zimmerman CF, Navarre J, Burnette JO, Goldenring JR: Rab11b resides in a vesicular compartment distinct from Rab11a in parietal cells and other epithelial cells. ExpCell Res 290: 322-331, 2003
    • (2003) ExpCell Res , vol.290 , pp. 322-331
    • Lapierre, L.A.1    Dorn, M.C.2    Zimmerman, C.F.3    Navarre, J.4    Burnette, J.O.5    Goldenring, J.R.6
  • 99
    • 68149158526 scopus 로고    scopus 로고
    • MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells
    • Mattila PE, Kinlough CL, Bruns JR, Weisz OA, Hughey RP: MUC1 traverses apical recycling endosomes along the biosynthetic pathway in polarized MDCK cells. Biol Chem 390: 551-556, 2009
    • (2009) Biol Chem , vol.390 , pp. 551-556
    • Mattila, P.E.1    Kinlough, C.L.2    Bruns, J.R.3    Weisz, O.A.4    Hughey, R.P.5
  • 100
    • 56149095414 scopus 로고    scopus 로고
    • Apical cargo traverses endosomal compartments on the passage to the cell surface
    • Cramm-Behrens CI, Dienst M, Jacob R: Apical cargo traverses endosomal compartments on the passage to the cell surface. Traffic 9: 2206-2220, 2008
    • (2008) Traffic , vol.9 , pp. 2206-2220
    • Cramm-Behrens, C.I.1    Dienst, M.2    Jacob, R.3
  • 101
    • 0036059819 scopus 로고    scopus 로고
    • Mosaic organization of the endocytic pathway
    • Miaczynska M, Zerial M: Mosaic organization of the endocytic pathway. Exp Cell Res 272: 8-14, 2002
    • (2002) Exp Cell Res , vol.272 , pp. 8-14
    • Miaczynska, M.1    Zerial, M.2
  • 102
    • 0242446165 scopus 로고    scopus 로고
    • Distinct membrane domains on endosomes in the recycling pathway visualized bymulticolor imaging of Rab4, Rab5, and Rab11
    • Sönnichsen B, De Renzis S, Nielsen E, Rietdorf J, Zerial M: Distinct membrane domains on endosomes in the recycling pathway visualized bymulticolor imaging of Rab4, Rab5, and Rab11. J Cell Biol 149: 901-914, 2000
    • (2000) J Cell Biol , vol.149 , pp. 901-914
    • Sönnichsen, B.1    De Renzis, S.2    Nielsen, E.3    Rietdorf, J.4    Zerial, M.5
  • 103
    • 0027243406 scopus 로고
    • Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process
    • Mayor S, Presley JF, Maxfield FR: Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J Cell Biol 121: 1257-1269, 1993
    • (1993) J Cell Biol , vol.121 , pp. 1257-1269
    • Mayor, S.1    Presley, J.F.2    Maxfield, F.R.3
  • 105
    • 34347369621 scopus 로고    scopus 로고
    • Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains
    • Thompson A, Nessler R, Wisco D, Anderson E, Winckler B, Sheff D: Recycling endosomes of polarized epithelial cells actively sort apical and basolateral cargos into separate subdomains. Mol Biol Cell 18: 2687-2697, 2007
    • (2007) Mol Biol Cell , vol.18 , pp. 2687-2697
    • Thompson, A.1    Nessler, R.2    Wisco, D.3    Anderson, E.4    Winckler, B.5    Sheff, D.6
  • 106
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Müsch A, Xu H, Shields D, Rodriguez- Boulan E: Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J Cell Biol 133: 543-558, 1996
    • (1996) J Cell Biol , vol.133 , pp. 543-558
    • Müsch, A.1    Xu, H.2    Shields, D.3    Rodriguez- Boulan, E.4
  • 107
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori T, Keller P, Roth MG, Simons K: Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J Cell Biol 133: 247-256, 1996
    • (1996) J Cell Biol , vol.133 , pp. 247-256
    • Yoshimori, T.1    Keller, P.2    Roth, M.G.3    Simons, K.4
  • 108
    • 0027529492 scopus 로고
    • Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina
    • GundersenD, Powell SK, Rodriguez-Boulan E: Apical polarization of N-CAM in retinal pigment epithelium is dependent on contact with the neural retina. J Cell Biol 121: 335-343, 1993
    • (1993) J Cell Biol , vol.121 , pp. 335-343
    • Gundersen, D.1    Powell, S.K.2    Rodriguez-Boulan, E.3
  • 109
    • 0030479863 scopus 로고    scopus 로고
    • The polarity of the plasma membrane protein RET-PE2 in retinal pigment epithelium is developmentally regulated
    • Marmorstein AD, Bonilha VL, Chiflet S, Neill JM, Rodriguez-Boulan E: The polarity of the plasma membrane protein RET-PE2 in retinal pigment epithelium is developmentally regulated. J Cell Sci 109: 3025-3034, 1996
    • (1996) J Cell Sci , vol.109 , pp. 3025-3034
    • Marmorstein, A.D.1    Bonilha, V.L.2    Chiflet, S.3    Neill, J.M.4    Rodriguez-Boulan, E.5
  • 110
    • 0037377965 scopus 로고    scopus 로고
    • Polarized expression of monocarboxylate transporters in human retinal pigment epithelium and ARPE-19 cells
    • Philp NJ, Wang D, Yoon H, Hjelmeland LM: Polarized expression of monocarboxylate transporters in human retinal pigment epithelium and ARPE-19 cells. Invest Ophthalmol Vis Sci 44: 1716-1721, 2003
    • (2003) Invest Ophthalmol Vis Sci , vol.44 , pp. 1716-1721
    • Philp, N.J.1    Wang, D.2    Yoon, H.3    Hjelmeland, L.M.4
  • 111
    • 0345327620 scopus 로고    scopus 로고
    • MCT1 and its accessory protein CD147 are differentially regulated by TSH in rat thyroid cells
    • Fanelli A, Grollman EF, Wang D, Philp NJ: MCT1 and its accessory protein CD147 are differentially regulated by TSH in rat thyroid cells. Am J Physiol Endocrinol Metab 285: E1223-E1229, 2003
    • (2003) Am J Physiol Endocrinol Metab , vol.285 , pp. E1223-E1229
    • Fanelli, A.1    Grollman, E.F.2    Wang, D.3    Philp, N.J.4
  • 113
    • 0025810410 scopus 로고
    • Apical and basal membrane ion transport mechanisms in bovine retinal pigment epithelium
    • Joseph DP, Miller SS: Apical and basal membrane ion transport mechanisms in bovine retinal pigment epithelium. J Physiol 435: 439-463, 1991
    • (1991) J Physiol , vol.435 , pp. 439-463
    • Joseph, D.P.1    Miller, S.S.2
  • 114
    • 0025327780 scopus 로고
    • Active ion transport pathways in the bovine retinal pigment epithelium
    • Miller SS, Edelman JL: Active ion transport pathways in the bovine retinal pigment epithelium. J Physiol 424: 283-300, 1990
    • (1990) J Physiol , vol.424 , pp. 283-300
    • Miller, S.S.1    Edelman, J.L.2
  • 115
    • 0018409996 scopus 로고
    • The electrogenic sodium pump of the frog retinal pigment epithelium
    • Miller SS, Steinberg RH, Oakley B 2nd: The electrogenic sodium pump of the frog retinal pigment epithelium. J Membr Biol 44: 259-279, 1978
    • (1978) J Membr Biol , vol.44 , pp. 259-279
    • Miller, S.S.1    Steinberg, R.H.2    Oakley, B.3
  • 116
    • 0026618868 scopus 로고
    • Ion transport mechanisms in native human retinal pigment epithelium
    • Quinn RH, Miller SS: Ion transport mechanisms in native human retinal pigment epithelium. Invest Ophthalmol Vis Sci 33: 3513-3527, 1992
    • (1992) Invest Ophthalmol Vis Sci , vol.33 , pp. 3513-3527
    • Quinn, R.H.1    Miller, S.S.2
  • 117
    • 0015894260 scopus 로고
    • Localization of sodium pumps in the choroid plexus epithelium
    • Quinton PM, Wright EM, Tormey JM: Localization of sodium pumps in the choroid plexus epithelium. J Cell Biol 58: 724-730, 1973
    • (1973) J Cell Biol , vol.58 , pp. 724-730
    • Quinton, P.M.1    Wright, E.M.2    Tormey, J.M.3
  • 118
    • 0021206798 scopus 로고
    • Immunohistochemical localization of Na+, K+-ATPase in the choroid plexus
    • Masuzawa T, Ohta T, Kawamura M, Nakahara N, Sato F: Immunohistochemical localization of Na+, K+-ATPase in the choroid plexus. Brain Res 302: 357-362, 1984
    • (1984) Brain Res , vol.302 , pp. 357-362
    • Masuzawa, T.1    Ohta, T.2    Kawamura, M.3    Nakahara, N.4    Sato, F.5
  • 119
    • 33847612320 scopus 로고    scopus 로고
    • Water and solute secretion by the choroid plexus
    • Praetorius J: Water and solute secretion by the choroid plexus. Pflugers Arch 454: 1-18, 2007
    • (2007) Pflugers Arch , vol.454 , pp. 1-18
    • Praetorius, J.1
  • 120
    • 0021678984 scopus 로고
    • Purification ofmousebrain (Na++ K+)-ATPase catalytic unit, characterization of antiserum, and immunocytochemical localization in cerebellum, choroid plexus, and kidney
    • Siegel GJ, Holm C, Schreiber JH, Desmond T, Ernst SA: Purification ofmousebrain (Na++ K+)-ATPase catalytic unit, characterization of antiserum, and immunocytochemical localization in cerebellum, choroid plexus, and kidney. J Histochem Cytochem 32: 1309-1318, 1984
    • (1984) J Histochem Cytochem , vol.32 , pp. 1309-1318
    • Siegel, G.J.1    Holm, C.2    Schreiber, J.H.3    Desmond, T.4    Ernst, S.A.5
  • 122
    • 0018139742 scopus 로고
    • An electrogenic NA +/K+ pump in the choroid plexus
    • Zeuthen T, Wright EM: An electrogenic NA +/K+ pump in the choroid plexus. Biochim Biophys Acta 511: 517-522, 1978
    • (1978) Biochim Biophys Acta , vol.511 , pp. 517-522
    • Zeuthen, T.1    Wright, E.M.2
  • 123
    • 0024554715 scopus 로고
    • A membranecytoskeletal complex containing Na+, K +-ATPase, ankyrin, and fodrin in Madin- Darby canine kidney (MDCK) cells: Implications for the biogenesis of epithelial cell polarity
    • Nelson WJ, Hammerton RW: A membranecytoskeletal complex containing Na+, K +-ATPase, ankyrin, and fodrin in Madin- Darby canine kidney (MDCK) cells: Implications for the biogenesis of epithelial cell polarity. J Cell Biol 108: 893-902, 1989
    • (1989) J Cell Biol , vol.108 , pp. 893-902
    • Nelson, W.J.1    Hammerton, R.W.2
  • 124
    • 0024571516 scopus 로고
    • Ankyrin links fodrin to the alpha subunit of Na, K-ATPase in Madin- Darby canine kidney cells and in intact renal tubule cells
    • Morrow JS, Cianci CD, Ardito T, Mann AS, Kashgarian M: Ankyrin links fodrin to the alpha subunit of Na, K-ATPase in Madin- Darby canine kidney cells and in intact renal tubule cells. J Cell Biol 108: 455-465, 1989
    • (1989) J Cell Biol , vol.108 , pp. 455-465
    • Morrow, J.S.1    Cianci, C.D.2    Ardito, T.3    Mann, A.S.4    Kashgarian, M.5
  • 125
    • 0027515201 scopus 로고
    • Distinguishing roles of the membranecytoskeleton and cadherin mediated cellcell adhesion in generating different Na+, K(+)-ATPase distributions in polarized epithelia
    • Marrs JA, Napolitano EW, Murphy-Erdosh C, Mays RW, Reichardt LF, Nelson WJ: Distinguishing roles of the membranecytoskeleton and cadherin mediated cellcell adhesion in generating different Na+, K(+)-ATPase distributions in polarized epithelia. J Cell Biol 123: 149-164, 1993
    • (1993) J Cell Biol , vol.123 , pp. 149-164
    • Marrs, J.A.1    Napolitano, E.W.2    Murphy-Erdosh, C.3    Mays, R.W.4    Reichardt, L.F.5    Nelson, W.J.6
  • 126
    • 0026085673 scopus 로고
    • Apical polarity of Na, K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submembrane cytoskeleton
    • Gundersen D, Orlowski J, Rodriguez-Boulan E: Apical polarity of Na, K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submembrane cytoskeleton. J Cell Biol 112: 863-872, 1991
    • (1991) J Cell Biol , vol.112 , pp. 863-872
    • Gundersen, D.1    Orlowski, J.2    Rodriguez-Boulan, E.3
  • 127
    • 84870566287 scopus 로고    scopus 로고
    • Culture of choroid plexus epithelial cells and in vitro model of blood-CSF barrier
    • Monnot AD, Zheng W: Culture of choroid plexus epithelial cells and in vitro model of blood-CSF barrier. Methods Mol Biol 945: 13-29, 2013
    • (2013) Methods Mol Biol , vol.945 , pp. 13-29
    • Monnot, A.D.1    Zheng, W.2
  • 130
    • 28044456306 scopus 로고    scopus 로고
    • Mechanisms regulating tissuespecificpolarityofmonocarboxylate transporters and their chaperone CD147 in kidney and retinal epithelia
    • Deora AA, Philp N, Hu J, Bok D, Rodriguez- Boulan E: Mechanisms regulating tissuespecificpolarityofmonocarboxylate transporters and their chaperone CD147 in kidney and retinal epithelia. Proc Natl Acad Sci U S A 102: 16245-16250, 2005
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 16245-16250
    • Deora, A.A.1    Philp, N.2    Hu, J.3    Bok, D.4    Rodriguez- Boulan, E.5
  • 131
    • 0034046294 scopus 로고    scopus 로고
    • High levels of E-/P-cadherin: Correlation with decreased apical polarity of Na/K ATPase in bovine RPE cells in situ
    • Burke JM, Cao F, Irving PE: High levels of E-/P-cadherin: Correlation with decreased apical polarity of Na/K ATPase in bovine RPE cells in situ. Invest Ophthalmol Vis Sci 41: 1945-1952, 2000
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 1945-1952
    • Burke, J.M.1    Cao, F.2    Irving, P.E.3
  • 132
    • 0023191909 scopus 로고
    • Expression of the a-subunit of Na/KATPase in renal collecting duct epithelium during development
    • Minuth WW, Gross P, Gilbert P, Kashgarian M: Expression of the a-subunit of Na/KATPase in renal collecting duct epithelium during development. Kidney Int 31: 1104-1112, 1987
    • (1987) Kidney Int , vol.31 , pp. 1104-1112
    • Minuth, W.W.1    Gross, P.2    Gilbert, P.3    Kashgarian, M.4
  • 133
    • 0033190942 scopus 로고    scopus 로고
    • Expression of the beta2-subunit and apical localization of Na+-K+-ATPase in metanephric kidney
    • Burrow CR, Devuyst O, Li X, Gatti L, Wilson PD: Expression of the beta2-subunit and apical localization of Na+-K+-ATPase in metanephric kidney. Am J Physiol 277: F391-F403, 1999
    • (1999) Am J Physiol , vol.277 , pp. F391-F403
    • Burrow, C.R.1    Devuyst, O.2    Li, X.3    Gatti, L.4    Wilson, P.D.5
  • 134
    • 0025219254 scopus 로고
    • Biosynthesis of the Na, K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery
    • Caplan MJ, Forbush B 3rd, Palade GE, Jamieson JD: Biosynthesis of the Na, K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. J Biol Chem 265: 3528-3534, 1990
    • (1990) J Biol Chem , vol.265 , pp. 3528-3534
    • Caplan, M.J.1    Forbush, B.2    Palade, G.E.3    Jamieson, J.D.4
  • 135
    • 0027749257 scopus 로고
    • Role of the transmembrane and extracytoplasmic domain of beta subunits in subunit assembly, intracellular transport, and functional expression of Na, K-pumps
    • Jaunin P, Jaisser F, Beggah AT, Takeyasu K, Mangeat P, Rossier BC, Horisberger JD, Geering K: Role of the transmembrane and extracytoplasmic domain of beta subunits in subunit assembly, intracellular transport, and functional expression of Na, K-pumps. J Cell Biol 123: 1751-1759, 1993
    • (1993) J Cell Biol , vol.123 , pp. 1751-1759
    • Jaunin, P.1    Jaisser, F.2    Beggah, A.T.3    Takeyasu, K.4    Mangeat, P.5    Rossier, B.C.6    Horisberger, J.D.7    Geering, K.8
  • 136
    • 0039692795 scopus 로고    scopus 로고
    • Endoplasmic reticulum quality control of oligomeric membrane proteins: Topogenic determinants involved in the degradation of the unassembled Na, K-ATPase alpha subunit and in its stabilization by beta subunit assembly
    • Béguin P, Hasler U, Staub O, Geering K: Endoplasmic reticulum quality control of oligomeric membrane proteins: Topogenic determinants involved in the degradation of the unassembled Na, K-ATPase alpha subunit and in its stabilization by beta subunit assembly. Mol Biol Cell 11: 1657-1672, 2000
    • (2000) Mol Biol Cell , vol.11 , pp. 1657-1672
    • Béguin, P.1    Hasler, U.2    Staub, O.3    Geering, K.4
  • 137
    • 0039406106 scopus 로고    scopus 로고
    • Expression and synthesis of the Na, K-ATPase beta 2 subunit in human retinal pigment epithelium
    • Ruiz A, Bhat SP, Bok D: Expression and synthesis of the Na, K-ATPase beta 2 subunit in human retinal pigment epithelium. Gene 176: 237-242, 1996
    • (1996) Gene , vol.176 , pp. 237-242
    • Ruiz, A.1    Bhat, S.P.2    Bok, D.3
  • 138
    • 0025734417 scopus 로고
    • Cell-specific expression of mRNAs encoding Na+, K(+)-ATPase alphaand beta-subunit isoforms within the rat central nervous system
    • Watts AG, Sanchez-Watts G, Emanuel JR, Levenson R: Cell-specific expression of mRNAs encoding Na+, K(+)-ATPase alphaand beta-subunit isoforms within the rat central nervous system. Proc Natl Acad Sci U S A 88: 7425-7429, 1991
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7425-7429
    • Watts, A.G.1    Sanchez-Watts, G.2    Emanuel, J.R.3    Levenson, R.4
  • 139
    • 0033883799 scopus 로고    scopus 로고
    • Apical plasma membrane mispolarization of NaK-ATPase in polycystic kidney disease epithelia is associated with aberrant expression of the beta2 isoform
    • Wilson PD, Devuyst O, Li X, Gatti L, Falkenstein D, Robinson S, Fambrough D, Burrow CR: Apical plasma membrane mispolarization of NaK-ATPase in polycystic kidney disease epithelia is associated with aberrant expression of the beta2 isoform. Am J Pathol 156: 253-268, 2000
    • (2000) Am J Pathol , vol.156 , pp. 253-268
    • Wilson, P.D.1    Devuyst, O.2    Li, X.3    Gatti, L.4    Falkenstein, D.5    Robinson, S.6    Fambrough, D.7    Burrow, C.R.8
  • 140
    • 80052592689 scopus 로고    scopus 로고
    • Mendelian disorders of membrane trafficking
    • De Matteis MA, Luini A: Mendelian disorders of membrane trafficking. N Engl J Med 365: 927-938, 2011
    • (2011) N Engl J Med , vol.365 , pp. 927-938
    • De Matteis, M.A.1    Luini, A.2
  • 141
    • 0032493276 scopus 로고    scopus 로고
    • ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells
    • Günther W, Lüchow A, Cluzeaud F, Vandewalle A, Jentsch TJ: ClC-5, the chloride channel mutated in Dent's disease, colocalizes with the proton pump in endocytotically active kidney cells. Proc Natl Acad Sci U S A 95: 8075-8080, 1998
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8075-8080
    • Günther, W.1    Lüchow, A.2    Cluzeaud, F.3    Vandewalle, A.4    Jentsch, T.J.5
  • 145
    • 0036197218 scopus 로고    scopus 로고
    • Epithelial sodium channel and the control of sodium balance: Interaction between genetic and environmental factors
    • Rossier BC, Pradervand S, Schild L, Hummler E: Epithelial sodium channel and the control of sodium balance: Interaction between genetic and environmental factors. Annu Rev Physiol 64: 877-897, 2002
    • (2002) Annu Rev Physiol , vol.64 , pp. 877-897
    • Rossier, B.C.1    Pradervand, S.2    Schild, L.3    Hummler, E.4
  • 146
    • 0028968593 scopus 로고
    • Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing
    • Deen PM, Croes H, van Aubel RA, Ginsel LA, van Os CH:Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J Clin Invest 95: 2291-2296, 1995
    • (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
  • 148
    • 80052271808 scopus 로고    scopus 로고
    • Apico-basal polarity in polycystic kidney disease epithelia
    • Wilson PD: Apico-basal polarity in polycystic kidney disease epithelia. Biochim Biophys Acta 1812: 1239-1248, 2011
    • (2011) Biochim Biophys Acta , vol.1812 , pp. 1239-1248
    • Wilson, P.D.1
  • 149
    • 0025755515 scopus 로고
    • Reversed polarity of Na(+) -K(+) -ATPase: Mislocation to apical plasma membranes in polycystic kidney disease epithelia
    • Wilson PD, Sherwood AC, Palla K, Du J, Watson R, Norman JT: Reversed polarity of Na(+) -K(+) -ATPase: mislocation to apical plasma membranes in polycystic kidney disease epithelia. Am J Physiol 260: F420-F430, 1991
    • (1991) Am J Physiol , vol.260 , pp. F420-F430
    • Wilson, P.D.1    Sherwood, A.C.2    Palla, K.3    Du, J.4    Watson, R.5    Norman, J.T.6
  • 150
    • 0029082997 scopus 로고
    • Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in humanADPKD
    • Du J, Wilson PD: Abnormal polarization of EGF receptors and autocrine stimulation of cyst epithelial growth in humanADPKD.Am J Physiol 269: C487-C495, 1995
    • (1995) Am J Physiol , vol.269 , pp. C487-C495
    • Du, J.1    Wilson, P.D.2
  • 152
    • 0036045770 scopus 로고    scopus 로고
    • The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane
    • Gan Y, McGraw TE, Rodriguez-Boulan E: The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nat Cell Biol 4: 605-609, 2002
    • (2002) Nat Cell Biol , vol.4 , pp. 605-609
    • Gan, Y.1    McGraw, T.E.2    Rodriguez-Boulan, E.3
  • 153
    • 0027407766 scopus 로고
    • Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine
    • Thomas DC, Brewer CB, RothMG: Vesicular stomatitis virus glycoprotein contains a dominant cytoplasmic basolateral sorting signal critically dependent upon a tyrosine. J Biol Chem 268: 3313-3320, 1993
    • (1993) J Biol Chem , vol.268 , pp. 3313-3320
    • Thomas, D.C.1    Brewer, C.B.2    Roth, M.G.3
  • 154
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Fölsch H, Pypaert M, Maday S, Pelletier L, Mellman I: The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 163: 351-362, 2003
    • (2003) J Cell Biol , vol.163 , pp. 351-362
    • Fölsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 155
    • 0032211788 scopus 로고    scopus 로고
    • Specificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120
    • Stephens DJ, Banting G: Specificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120. Biochem J 335: 567-572, 1998
    • (1998) Biochem J , vol.335 , pp. 567-572
    • Stephens, D.J.1    Banting, G.2
  • 156
    • 0032500602 scopus 로고    scopus 로고
    • Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells
    • Roush DL, Gottardi CJ, Naim HY, Roth MG, Caplan MJ: Tyrosine-based membrane protein sorting signals are differentially interpreted by polarized Madin-Darby canine kidney and LLC-PK1 epithelial cells. J Biol Chem 273: 26862-26869, 1998
    • (1998) J Biol Chem , vol.273 , pp. 26862-26869
    • Roush, D.L.1    Gottardi, C.J.2    Naim, H.Y.3    Roth, M.G.4    Caplan, M.J.5
  • 157
    • 0026806542 scopus 로고
    • A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cationdependent mannose 6-phosphate receptor is necessary for the lysosomal enzymesorting function
    • Johnson KF, Kornfeld S: A His-Leu-Leu sequence near the carboxyl terminus of the cytoplasmic domain of the cationdependent mannose 6-phosphate receptor is necessary for the lysosomal enzymesorting function. J Biol Chem 267: 17110-17115, 1992
    • (1992) J Biol Chem , vol.267 , pp. 17110-17115
    • Johnson, K.F.1    Kornfeld, S.2
  • 158
    • 0031972754 scopus 로고    scopus 로고
    • Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin- Darby canine kidney cells. Identification of a basolateral determinant unrelated to clathrin- coated pit localization signals
    • Distel B, Bauer U, Le Borgne R, Hoflack B: Basolateral sorting of the cation-dependent mannose 6-phosphate receptor in Madin- Darby canine kidney cells. Identification of a basolateral determinant unrelated to clathrin- coated pit localization signals. J Biol Chem 273: 186-193, 1998
    • (1998) J Biol Chem , vol.273 , pp. 186-193
    • Distel, B.1    Bauer, U.2    Le Borgne, R.3    Hoflack, B.4
  • 159
    • 0030038676 scopus 로고    scopus 로고
    • Glycolipid-independent sorting of a secretory glycoprotein to the apical surface of polarized epithelial cells
    • Graichen R, Lösch A, Appel D, Koch-Brandt C: Glycolipid-independent sorting of a secretory glycoprotein to the apical surface of polarized epithelial cells. J Biol Chem 271: 15854-15857, 1996
    • (1996) J Biol Chem , vol.271 , pp. 15854-15857
    • Graichen, R.1    Lösch, A.2    Appel, D.3    Koch-Brandt, C.4
  • 163
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele P, Roth MG, Simons K: Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J 16: 5501-5508, 1997
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 164
    • 4444370896 scopus 로고    scopus 로고
    • Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection
    • Brown G, Jeffree CE, McDonald T, Rixon HWM, Aitken JD, Sugrue RJ: Analysis of the interaction between respiratory syncytial virus and lipid-rafts in Hep2 cells during infection. Virology 327: 175-185, 2004
    • (2004) Virology , vol.327 , pp. 175-185
    • Brown, G.1    Jeffree, C.E.2    McDonald, T.3    Rixon, H.W.M.4    Aitken, J.D.5    Sugrue, R.J.6
  • 165
    • 0034008665 scopus 로고    scopus 로고
    • Structural determinants required for apical sorting of an intestinal brush-border membrane protein
    • Jacob R, Alfalah M, Grünberg J, Obendorf M, Naim HY: Structural determinants required for apical sorting of an intestinal brush-border membrane protein. J Biol Chem 275: 6566-6572, 2000
    • (2000) J Biol Chem , vol.275 , pp. 6566-6572
    • Jacob, R.1    Alfalah, M.2    Grünberg, J.3    Obendorf, M.4    Naim, H.Y.5
  • 167
    • 1542313963 scopus 로고    scopus 로고
    • SpecificN-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol- anchored forms of endolyn inMadin-Darby canine kidney cells
    • Potter BA, Ihrke G, Bruns JR, WeixelKM, Weisz OA: SpecificN-glycans direct apical delivery of transmembrane, but not soluble or glycosylphosphatidylinositol- anchored forms of endolyn inMadin-Darby canine kidney cells. Mol Biol Cell 15: 1407-1416, 2004
    • (2004) Mol Biol Cell , vol.15 , pp. 1407-1416
    • Potter, B.A.1    Ihrke, G.2    Bruns, J.R.3    Weixelkm Weisz, O.A.4


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