메뉴 건너뛰기




Volumn 11, Issue 6, 2000, Pages 2033-2045

The MAL proteolipid is necessary for the overall apical delivery of membrane proteins in the polarized epithelial Madin-Darby canine kidney and Fischer rat thyroid cell lines

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE PLACENTA ISOENZYME; ANTISENSE OLIGONUCLEOTIDE; DIPEPTIDYL PEPTIDASE IV; GLYCOSYLPHOSPHATIDYLINOSITOL; LIPID; MEMBRANE PROTEIN; NEUROTROPHIN RECEPTOR; PROTEOLIPID; VIRUS HEMAGGLUTININ;

EID: 0242668515     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.11.6.2033     Document Type: Article
Times cited : (96)

References (32)
  • 1
    • 0004183876 scopus 로고
    • cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation
    • Alonso, M.A., and Weissman, S.M. (1987). cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation. Proc. Natl. Acad. Sci. USA 84, 1997-2001.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1997-2001
    • Alonso, M.A.1    Weissman, S.M.2
  • 2
    • 0032739854 scopus 로고    scopus 로고
    • Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro
    • Benting, J., Rietveld, A., Ansorge, I., and Simons, K. (1999). Acyl and alkyl chain length of GPI-anchors is critical for raft association in vitro. FEBS Lett. 462, 47-50.
    • (1999) FEBS Lett. , vol.462 , pp. 47-50
    • Benting, J.1    Rietveld, A.2    Ansorge, I.3    Simons, K.4
  • 3
    • 0024433592 scopus 로고
    • Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells
    • Brown, D.A., Crise, B., and Rose, J.K. (1989). Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 245, 1499-1501.
    • (1989) Science , vol.245 , pp. 1499-1501
    • Brown, D.A.1    Crise, B.2    Rose, J.K.3
  • 4
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface
    • Brown, D.A., and Rose, J.K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 5
    • 0001619084 scopus 로고    scopus 로고
    • VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells
    • Cheong, K.H., Zacchetti, D., Schneeberger, E.E., and Simons, K. (1999). VIP17/MAL, a lipid raft-associated protein, is involved in apical transport in MDCK cells. Proc. Natl. Acad. Sci. USA 96, 6241-6248.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6241-6248
    • Cheong, K.H.1    Zacchetti, D.2    Schneeberger, E.E.3    Simons, K.4
  • 6
    • 0029053448 scopus 로고
    • The role of N-glycans in the secretory pathway
    • Fiedler, K., and Simons, K. (1995). The role of N-glycans in the secretory pathway. Cell 81, 309-312.
    • (1995) Cell , vol.81 , pp. 309-312
    • Fiedler, K.1    Simons, K.2
  • 7
    • 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., and Koch-Brandt, C. (1996). Glycolipid-independent sorting of a secretory glycoprotein to the apical surface of polarized epithelial cells. J. Biol. Chem. 273, 15854-15857.
    • (1996) J. Biol. Chem. , vol.273 , pp. 15854-15857
    • Graichen, R.1    Lösch, A.2    Appel, D.3    Koch-Brandt, C.4
  • 8
    • 0032559854 scopus 로고    scopus 로고
    • Cholesterol is required for surface transport of influenza virus hemagglutinin
    • Keller, P., and Simons, K. (1998). Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140, 1357-1367.
    • (1998) J. Cell Biol. , vol.140 , pp. 1357-1367
    • Keller, P.1    Simons, K.2
  • 9
    • 0028875824 scopus 로고
    • Cloning and characterization of MVP17: A developmentally regulated myelin protein in oligodendrocytes
    • Kim, T., Fiedler, K., Madison, D.L., Krueger, W. H., and Pfeiffer, S.E. (1995). Cloning and characterization of MVP17: a developmentally regulated myelin protein in oligodendrocytes. J. Neurosci. Res. 42, 413-422.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 413-422
    • Kim, T.1    Fiedler, K.2    Madison, D.L.3    Krueger, W.H.4    Pfeiffer, S.E.5
  • 10
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin, S., Naim, H.Y., Rodriguez, A.C., and Roth, M.G. (1998). Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell Biol. 142, 51-57.
    • (1998) J. Cell Biol. , vol.142 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 11
    • 0034003908 scopus 로고    scopus 로고
    • Detergent-insoluble 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., and Zurzolo, C. (2000). Detergent-insoluble 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) Mol Biol. Cell , vol.11 , pp. 531-542
    • Lipardi, C.1    Nitsch, L.2    Zurzolo, C.3
  • 12
    • 0024468669 scopus 로고
    • A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells
    • Lisanti, M.P., Caras, I.W., Davitz, M.A., and Rodriguez-Boulan, E. (1989). A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 309, 2145-2156.
    • (1989) J. Cell Biol. , vol.309 , pp. 2145-2156
    • Lisanti, M.P.1    Caras, I.W.2    Davitz, M.A.3    Rodriguez-Boulan, E.4
  • 13
    • 0025133358 scopus 로고
    • Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells
    • Lisanti, M.P., Caras, I.W., Gilbert, T., Hanzel, D., and Rodriguez-Boulan, E. (1990). Vectorial apical delivery and slow endocytosis of a glycolipid-anchored fusion protein in transfected MDCK cells. Proc. Natl. Acad. Sci. USA 87, 7419-7423.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7419-7423
    • Lisanti, M.P.1    Caras, I.W.2    Gilbert, T.3    Hanzel, D.4    Rodriguez-Boulan, E.5
  • 14
    • 0031763488 scopus 로고    scopus 로고
    • Expression of the MAL gene in the thyroid: The MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles
    • Martín-Belmonte, F., Kremer, L., Albar, J.P., Marazuela, M., and Alonso, M.A. (1998). Expression of the MAL gene in the thyroid: the MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles. Endocrinology 139, 2077-2084.
    • (1998) Endocrinology , vol.139 , pp. 2077-2084
    • Martín-Belmonte, F.1    Kremer, L.2    Albar, J.P.3    Marazuela, M.4    Alonso, M.A.5
  • 15
    • 0028068273 scopus 로고
    • Mechanisms of cell polarity: Sorting and transport in epithelial cells
    • Matter, K., and Mellman, I. (1994). Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6, 545-554.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 545-554
    • Matter, K.1    Mellman, I.2
  • 16
    • 0031589155 scopus 로고    scopus 로고
    • Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells
    • Millán, J., Puertollano, R., Fan, L., and Alonso, M.A. (1997). Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells. Biochem. Biophys. Res. Commun. 233, 707-712.
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 707-712
    • Millán, J.1    Puertollano, R.2    Fan, L.3    Alonso, M.A.4
  • 17
    • 0032557440 scopus 로고    scopus 로고
    • A short peptide motif at the carboxyl terminus is required for incorporation of the integral membrane MAL protein to glycolipid-enriched membranes
    • Puertollano, R., and Alonso, M.A. (1998). A short peptide motif at the carboxyl terminus is required for incorporation of the integral membrane MAL protein to glycolipid-enriched membranes. J. Biol. Chem. 233, 12740-12745.
    • (1998) J. Biol. Chem. , vol.233 , pp. 12740-12745
    • Puertollano, R.1    Alonso, M.A.2
  • 18
    • 0032849674 scopus 로고    scopus 로고
    • MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane
    • Puertollano, R., and Alonso, M.A. (1999). MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane. Mol. Biol. Cell 10, 3435-3447.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3435-3447
    • Puertollano, R.1    Alonso, M.A.2
  • 19
    • 0030875553 scopus 로고    scopus 로고
    • Recombinant expression of the MAL proteolipid, a component of glycolipid-enriched membrane microdomains, induces the formation of vesicular structures in insect cells
    • Puertollano, R., Li, S., Lisanti, M.P., and Alonso, M.A. (1997). Recombinant expression of the MAL proteolipid, a component of glycolipid-enriched membrane microdomains, induces the formation of vesicular structures in insect cells. J. Biol. Chem. 272, 18311-18315.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18311-18315
    • Puertollano, R.1    Li, S.2    Lisanti, M.P.3    Alonso, M.A.4
  • 20
    • 0345683542 scopus 로고    scopus 로고
    • The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells
    • Puertollano, R., Martín-Belmonte, F., Millán, J., de Marco, M.C., Albar, J.P., Kremer, L., and Alonso, M.A. (1999). The MAL proteolipid is necessary for normal apical transport and accurate sorting of the influenza virus hemagglutinin in Madin-Darby canine kidney cells. J. Cell Biol. 245, 141-145.
    • (1999) J. Cell Biol. , vol.245 , pp. 141-145
    • Puertollano, R.1    Martín-Belmonte, F.2    Millán, J.3    De Marco, M.C.4    Albar, J.P.5    Kremer, L.6    Alonso, M.A.7
  • 22
    • 0024520841 scopus 로고
    • Integral and peripheral protein composition of the apical and basolateral membrane domains in MDCK cells
    • Sargiacomo, M., Lisanti, M., Graeve, L., Le Bivic, A., and Rodriguez-Boulan, E. (1989). Integral and peripheral protein composition of the apical and basolateral membrane domains in MDCK cells. J. Membr. Biol. 107, 277-286.
    • (1989) J. Membr. Biol. , vol.107 , pp. 277-286
    • Sargiacomo, M.1    Lisanti, M.2    Graeve, L.3    Le Bivic, A.4    Rodriguez-Boulan, E.5
  • 23
    • 0027275642 scopus 로고
    • Signal transducing molecules and glycosyl-phophatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells
    • Sargiacomo, M., Sudol, M., Tang, Z., and Lisanti, M.P. (1993). Signal transducing molecules and glycosyl-phophatidylinositol-linked proteins form a caveolin-rich insoluble complex in MDCK cells. J. Cell Biol. 122, 789-807.
    • (1993) J. Cell Biol. , vol.122 , pp. 789-807
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 24
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele, P., Roth, M.G., and Simons, K. (1998). Interaction of influenza virus hemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J. 16, 5501-5508.
    • (1998) EMBO J. , vol.16 , pp. 5501-5508
    • Scheiffele, P.1    Roth, M.G.2    Simons, K.3
  • 25
    • 0028810337 scopus 로고
    • N-glycans as apical sorting signals in epithelial cells
    • Scheiffele, P., and Simons, K. (1995). N-glycans as apical sorting signals in epithelial cells. Nature 378, 96-98.
    • (1995) Nature , vol.378 , pp. 96-98
    • Scheiffele, P.1    Simons, K.2
  • 26
    • 0025341760 scopus 로고
    • Polarized sorting in epithelia
    • Simons, K., and Wandinger-Ness, A. (1990). Polarized sorting in epithelia. Cell 62, 207-210.
    • (1990) Cell , vol.62 , pp. 207-210
    • Simons, K.1    Wandinger-Ness, A.2
  • 27
    • 0024547523 scopus 로고
    • Differential extract-ability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts
    • Skibbens, J.E., Roth, M.G., and Matlin, K.S. (1989). Differential extract-ability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and nonpolar fibroblasts. J. Cell Biol. 108, 821-832.
    • (1989) J. Cell Biol. , vol.108 , pp. 821-832
    • Skibbens, J.E.1    Roth, M.G.2    Matlin, K.S.3
  • 28
    • 0025153020 scopus 로고
    • Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells
    • Wandinger-Ness, A., Bennett, M.K., Antony, C., and Simons, K. (1990). Distinct transport vesicles mediate the delivery of plasma membrane proteins to the apical and basolateral domains of MDCK cells. J. Cell Biol. 111, 987-1000.
    • (1990) J. Cell Biol. , vol.111 , pp. 987-1000
    • Wandinger-Ness, A.1    Bennett, M.K.2    Antony, C.3    Simons, K.4
  • 29
    • 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, A.H., Baldwin, A.N., Monlauzeur, L., Le Bivic, A., and Rodriguez-Boulan, E. (1997). The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139, 929-940.
    • (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
  • 31
    • 0027315413 scopus 로고
    • Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells
    • Zurzolo, C., Lisanti, M.P., Caras, I.W., Nitsch, L., and Rodriguez-Boulan, E. (1993). Glycosylphosphatidylinositol-anchored proteins are preferentially targeted to the basolateral surface in Fischer rat thyroid epithelial cells. J. Cell Biol. 121, 1031-1039.
    • (1993) J. Cell Biol. , vol.121 , pp. 1031-1039
    • Zurzolo, C.1    Lisanti, M.P.2    Caras, I.W.3    Nitsch, L.4    Rodriguez-Boulan, E.5
  • 32
    • 0028032064 scopus 로고
    • VlP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphophatidylinositol-anchored proteins in epithelial cells
    • Zurzolo, C., van't Hof, W., van Meer, G., and Rodriguez-Boulan, E. (1994). VlP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphophatidylinositol-anchored proteins in epithelial cells. EMBO J. 13, 42-53.
    • (1994) EMBO J. , vol.13 , pp. 42-53
    • Zurzolo, C.1    Van't Hof, W.2    Van Meer, G.3    Rodriguez-Boulan, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.