CoChat
Sign Up
Cited by 574

The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.

Organization of vesicular trafficking in epithelia

Rodriguez-Boulan, Enrique, Kreitzer, Geri, Müsch, Anne·2005·Nature Reviews Molecular Cell Biology
DOI 10.1038/nrm1593
Open this paper in CoChat — free account

Abstract

Experiments using mammalian epithelial cell lines have elucidated biosynthetic and recycling pathways for apical and basolateral plasma-membrane proteins, and have identified components that guide apical and basolateral proteins along these pathways. These components include apical and basolateral sorting signals, adaptors for basolateral signals, and docking and fusion proteins for vesicular trafficking. Recent live-cell-imaging studies provide a real-time view of sorting processes in epithelial cells, including key roles for actin, microtubules and motors in the organization of post-Golgi trafficking.

Overview

Integrity signals

Registry

Crossref · 10.1038/nrm1593

Cites

4 of 4 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 155

  1. Cereijido, M., Contreras, R. G. & Shoshani, L. Cell adhesion, polarity, and epithelia in the dawn of metazoans. Physiol. Rev. 84, 1229–1262 (2004). · DOI
  2. Palade, G. E. Intracellular aspects of the process of protein secretion. Science 189, 374–358 (1975). · DOI
  3. Farquhar, M. G. & Palade, G. E. Junctional complexes in various epithelia. J. Cell Biol. 17, 375–412 (1963). · DOI
  4. Cereijido, M., Robbins, E. S., Dolan, W. J., Rotunno, C. A. & Sabatini, D. D. Polarized monolayers formed by epithelial cells on a permeable and translucent support. J. Cell Biol. 77, 853–880 (1978). A landmark paper that characterized the formation of an epithelium in vitro. · DOI
  5. Misfeldt, D. S., Hammamoto, S. T. & Pitelka, D. R. Transepithelial transport in cell culture. Proc. Natl Acad. Sci. USA 73, 1212–1216 (1976). · DOI
  6. Rodriguez-Boulan, E. & Sabatini, D. D. Asymmetric budding of viruses in epithelial monolayers: a model system for study of epithelial polarity. Proc. Natl Acad. Sci. USA 75, 5071–5075 (1978). Showed that enveloped viruses can be used as tools to study the generation and maintenance of epithelial polarity. · DOI
  7. Rodriguez-Boulan, E. & Pendergast, M. Polarized distribution of viral envelope proteins in the plasma membrane of infected epithelial cells. Cell 20, 45–54 (1980). · DOI
  8. Griffiths, G. & Simons, K. The trans Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438–443 (1986). · DOI
  9. Misek, D. E., Bard, E. & Rodriguez-Boulan, E. Biogenesis of epithelial cell polarity: intracellular sorting and vectorial exocytosis of an apical plasma membrane glycoprotein. Cell 39, 537–546 (1984). · DOI
  10. Rindler, M. J., Ivanov, I. E., Plesken, H., Rodriguez-Boulan, E. & Sabatini, D. D. 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). · DOI
  11. Rodriguez-Boulan, E. & Nelson, W. J. Morphogenesis of the polarized epithelial cell phenotype. Science 245, 718–725 (1989). · DOI
  12. Simons, K. & Wandinger-Ness, A. Polarized sorting in epithelia. Cell 62, 207–210 (1990). · DOI
  13. Tuma, P. L. & Hubbard, A. L. Transcytosis: crossing cellular barriers. Physiol. Rev. 83, 871–932 (2003). · DOI · Paper page
  14. Rodriguez-Boulan, E. & Powell, S. K. Polarity of epithelial and neuronal cells. Annu. Rev. Cell Biol. 8, 395–427 (1992). · DOI
  15. Matter, K. & Mellman, I. Mechanisms of cell polarity: sorting and transport in epithelial cells. Curr. Opin. Cell Biol. 6, 545–554 (1994). · DOI
  16. Yeaman, C., Grindstaff, K. K. & Nelson, W. J. New perspectives on mechanisms involved in generating epithelial cell polarity. Physiol. Rev. 79, 73–98 (1999). · DOI
  17. Mostov, K., Su, T. & ter Beest, M. Polarized epithelial membrane traffic: conservation and plasticity. Nature Cell Biol. 5, 287–293 (2003). · DOI
  18. Schock, F. & Perrimon, N. Molecular mechanisms of epithelial morphogenesis. Annu. Rev. Cell Dev. Biol. 18, 463–493 (2002). · DOI
  19. Ang, A. L. et al. Recycling endosomes can serve as intermediates during transport from the Golgi to the plasma membrane of MDCK cells. J. Cell Biol. 167, 531–543 (2004). · DOI
  20. Brown, P. S. et al. Definition of distinct compartments in polarized Madin–Darby canine kidney (MDCK) cells for membrane-volume sorting, polarized sorting and apical recycling. Traffic 1, 124–140 (2000). · DOI
  21. Polishchuk, R., Di Pentima, A. & Lippincott-Schwartz, J. Delivery of raft-associated, GPI-anchored proteins to the apical surface of polarized MDCK cells by a transcytotic pathway. Nature Cell Biol. 6, 297–307 (2004). · DOI · Paper page
  22. Lisanti, M., Sargiacomo, M., Graeve, L., Saltiel, A. & Rodriguez-Boulan, E. Polarized apical distribution of glycosyl phosphatidylinositol anchored proteins in a renal epithelial line. Proc. Natl Acad. Sci. USA 85, 9557–9561 (1988). First indication that a lipid (GPI) contributes to apical targeting. · DOI
  23. Lisanti, M., Caras, I. P., Davitz, M. A. & Rodriguez-Boulan, E. A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells. J. Cell Biol. 109, 2145–2156 (1989). · DOI
  24. Brown, D. A., Crise, B. & Rose, J. K. Mechanism of membrane anchoring affects polarized expression of two proteins in MDCK cells. Science 245, 1499–1501 (1989). · DOI
  25. Scheiffele, P., Peranen, J. & Simons, K. N-glycans as apical sorting signals in epithelial cells. Nature 378, 96–98 (1995). First demonstration of N -glycans as apical sorting signals. · DOI
  26. Yeaman, C. et al. The O-glycosylated stalk domain is required for apical sorting of neurotrophin receptors in polarized MDCK cells. J. Cell Biol. 139, 929–940 (1997). First indication that O -glycans function as an apical targeting mechanism. · DOI
  27. Alfalah, M. et al. O-linked glycans mediate apical sorting of human intestinal sucrase-isomaltase through association with lipid rafts. Curr. Biol. 9, 593–596 (1999). · DOI
  28. Rodriguez-Boulan, E. & Gonzalez, A. Glycans in post-Golgi apical targeting: sorting signals or structural props? Trends Cell Biol. 9, 291–294 (1999). · DOI
  29. Gut, A. et al. Carbohydrate-mediated Golgi to cell surface transport and apical targeting of membrane proteins. EMBO J. 17, 1919–1929 (1998). · DOI
  30. Fiedler, K. & Simons, K. The role of N-glycans in the secretory pathway. Cell 81, 309–312 (1995). · DOI
  31. Marzolo, M. P., Bull, P. & Gonzalez, A. Apical sorting of hepatitis B surface antigen (HBsAg) is independent of N-glycosylation and glycosylphosphatidylinositol-anchored protein segregation. Proc. Natl Acad. Sci. USA 94, 1834–1839 (1997). · DOI
  32. Bravo-Zehnder, M. et al. Apical sorting of a voltage- and Ca2+-activated K+ channel α- subunit in Madin–Darby canine kidney cells is independent of N-glycosylation. Proc. Natl Acad. Sci. USA 97, 13114–13119 (2000). · DOI
  33. Tai, A. W., Chuang, J. Z., Bode, C., Wolfrum, U. & Sung, C. H. Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1. Cell 97, 877–887 (1999). · DOI
  34. Takeda, T., Yamazaki, H. & Farquhar, M. G. Identification of an apical sorting determinant in the cytoplasmic tail of megalin. Am. J. Physiol. Cell Physiol. 284, C1105–C1113 (2003). · DOI
  35. Marzolo, M. P. et al. Differential distribution of low-density lipoprotein-receptor-related protein (LRP) and megalin in polarized epithelial cells is determined by their cytoplasmic domains. Traffic 4, 273–288 (2003). · DOI · Paper page
  36. Altschuler, Y., Hodson, C. & Milgram, S. L. The apical compartment: trafficking pathways, regulators and scaffolding proteins. Curr. Opin. Cell Biol. 15, 423–429 (2003). · DOI
  37. Marmorstein, A. D. et al. Saturation of, and competition for entry into, the apical secretory pathway. Proc. Natl Acad. Sci. USA 97, 3248–3253 (2000). · DOI
  38. Fullekrug, J., Scheiffele, P. & Simons, K. VIP-36 localisation to the early secretory pathway. J. Cell Sci. 112, 2813–2821 (1999). · DOI
  39. van Meer, G. & Simons, K. Lipid polarity and sorting in epithelial cells. J. Cell Biochem. 36, 51–58 (1988). The concept of lipid rafts was proposed. · DOI
  40. Paladino, S. et al. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 167, 699–709 (2004). An exciting observation that throws light on the role of protein oligomerization in promoting apical targeting. · DOI
  41. Benting, J. H., Rietveld, A. G. & Simons, K. N-Glycans mediate the apical sorting of a GPI-anchored, raft-associated protein in Madin–Darby canine kidney cells. J. Cell Biol. 146, 313–320 (1999). · DOI
  42. Sharma, P. et al. Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116, 577–589 (2004). · DOI
  43. Hannan, L. A., Lisanti, M. P., Rodriguez-Boulan, E. & Edidin, M. Correctly sorted molecules of a GPI-anchored protein are clustered and immobile when they arrive at the apical surface of MDCK cells. J. Cell Biol. 120, 353–358 (1993). Initial proposal that a clustering event might be involved in apical targeting of GPI-anchored proteins. · DOI
  44. Mayor, S., Rothenberg, K. G. & Maxfield, F. R. Sequestration of GPI-anchored proteins in caveolae triggered by cross-linking. Science 264, 1948–1951 (1994). · DOI
  45. Verkade, P., Harder, T., Lafont, F. & Simons, K. Induction of caveolae in the apical plasma membrane of Madin–Darby canine kidney cells. J. Cell Biol. 148, 727–739 (2000). · DOI
  46. Lisanti, M. P., Le Bivic, A., Saltiel, A. & Rodriguez-Boulan, E. Preferred apical distribution of glycosyl-phosphatidylinositol (GPI) anchored proteins: a highly conserved feature of the polarized epithelial cell phenotype. J. Memb. Biol. 268, 155–167 (1990). · DOI
  47. 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). · DOI
  48. Scheiffele, P. et al. Caveolin-1 and-2 in the exocytic pathway of MDCK cells. J. Cell Biol. 140, 795–806 (1998). · DOI
  49. Puertollano, R., Martinez-Menarguez, J. A., Batista, A., Ballesta, J. & Alonso, M. A. An intact dilysine-like motif in the carboxyl terminus of MAL is required for normal apical transport of the influenza virus hemagglutinin cargo protein in epithelial Madin–Darby canine kidney cells. Mol. Biol. Cell 12, 1869–1883 (2001). · DOI
  50. Mostov, K. E., Kops, A. B. & Deitcher, D. L. Deletion of the cytoplasmic domain of the polymeric immunoglobulin receptor prevents basolateral localization and endocytosis. Cell 47, 359–364 (1986). The first demonstration that basolateral sorting information exists in the cytoplasmic domain. · DOI
  51. Casanova, J. E., Apodaca, G. & Mostov, K. E. An autonomous signal for basolateral sorting in the cytoplasmic domain of the polymeric immunoglobulin receptor. Cell 66, 65–75 (1991). Identification of one of the first basolateral signals. · DOI
  52. Hunziker, W., Harter, C., Matter, K. & Mellman, I. Basolateral sorting in MDCK cells requires a distinct cytoplasmic domain determinant. Cell 66, 907–920 (1991). Identification of one of the first basolateral signals. · DOI
  53. 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). · DOI · Paper page
  54. Brewer, C. B. & Roth, M. G. A single amino acid change in the cytoplasmic domain alters the polarized delivery of influenza viral hemagglutin. J. Cell Biol. 114, 413–421 (1991) Showed dual importance of tyrosine signals in endocytosis and basolateral targeting. · DOI
  55. Le Bivic, A. et al. 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). · DOI
  56. 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). · DOI · Paper page
  57. Muth, T. R. & Caplan, M. J. Transport protein trafficking in polarized cells. Annu. Rev. Cell Dev. Biol. 19, 333–366 (2003). · DOI
  58. Wehrle-Haller, B. & Imhof, B. A. Stem cell factor presentation to c-Kit. Identification of a basolateral targeting domain. J. Biol. Chem. 276, 12667–12674 (2001). · DOI
  59. Koivisto, U. M., Hubbard, A. L. & Mellman, I. A novel cellular phenotype for familial hypercholesterolemia due to a defect in polarized targeting of LDL receptor. Cell 105, 575–585 (2001). · DOI · Paper page
  60. Nelson, W. J. & Veshnock, P. J. Ankyrin binding to (Na+, K+) ATPase and implications for the organization of membrane domains in polarized cells. Nature 328, 533–536 (1987). Demonstration of an alternative mechanism for basolateral localization: immobilization by the membrane cytoskeleton. · DOI
  61. Pimplikar, S. W., Ikonen, E. & Simons, K. Basolateral protein transport in streptolysin O-permeabilized MDCK cells. J. Cell Biol. 125, 1025–1035 (1994). · DOI
  62. Musch, 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). · DOI
  63. Soza, A. et al. Sorting competition with membrane-permeable peptides in intact epithelial cells revealed discrimination of transmembrane proteins not only at the trans-Golgi network but also at pre-Golgi stages. J. Biol. Chem. 279, 17376–17383 (2004). · DOI
  64. Skibbens, J. E., Roth, M. G. & Matlin, K. S. Differential extractability of influenza virus hemagglutinin during intracellular transport in polarized epithelial cells and non polar fibroblasts. J. Cell Biol. 108, 821–832 (1989). First demonstration that an apical transmembrane protein might be associated with lipid rafts. · DOI
  65. Yoshimori, T., Keller, P., Roth, M. G. & Simons, K. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 133, 247–256 (1996). · DOI
  66. Matter, K., Whitney, J. A., Yamamoto, E. M. & Mellman, I. Common signals control low density lipoprotein receptor sorting in endosomes and in the Golgi complex of MDCK cells. Cell 74, 1053–1064 (1993). Showed common signals that control sorting in endosomes and the Golgi complex. · DOI · Paper page
  67. Aroeti, B. & Mostov, K. E. Polarized sorting of the polymeric immunoglobulin receptor in the exocytic and endocytic pathway is controlled by the same amino acids. EMBO J. 13, 2297–2304 (1994). · DOI · Paper page
  68. Bonifacino, J. S. & Lippincott-Schwartz, J. Coat proteins: shaping membrane transport. Nature Rev. Mol. Cell Biol. 4, 409–414 (2003). · DOI
  69. Folsch, H., Ohno, H., Bonifacino, J. S. & Mellman, I. A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells. Cell 99, 189–198 (1999). Reports the characterization of an epithelial adaptor for basolateral sorting signals. Provides a review of the basolateral signal subfield. · DOI · Paper page
  70. Simmen, T., Honing, S., Icking, A., Tikkanen, R. & Hunziker, W. AP-4 binds basolateral signals and participates in basolateral sorting in epithelial MDCK cells. Nature Cell Biol. 4, 154–159 (2002). · DOI · Paper page
  71. Ohno, H. et al. Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells. FEBS Lett. 4, 215–220 (1999). · DOI · Paper page
  72. Gan, Y., McGraw, T. E. & Rodriguez-Boulan, E. The epithelial-specific adaptor AP1B mediates post-endocytic recycling to the basolateral membrane. Nature Cell Biol. 4, 605–609 (2002). Shows that two different forms of the AP1 adaptor localize to different organelles and that AP1B controls basolateral sorting in endosomes. · DOI
  73. Folsch, 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). · DOI
  74. Futter, C. E., Connolly, C. N., Cutler, D. F. & Hopkins, C. R. Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J. Biol. Chem. 270, 10999–11003 (1995). · DOI
  75. Orzech, E., Cohen, S., Weiss, A. & Aroeti, B. Interactions between the exocytic and endocytic pathways in polarized Madin–Darby canine kidney cells. J. Biol. Chem. 275, 15207–15219 (2000). · DOI
  76. Wang, Y. J. et al. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell 114, 299–310 (2003). · DOI
  77. Nishimura, N., Plutner, H., Hahn, K. & Balch, W. E. The δ subunit of AP-3 is required for efficient transport of VSV-G from the trans-Golgi network to the cell surface. Proc. Natl Acad. Sci. USA 99, 6755–6760 (2002). · DOI
  78. Futter, C. E. et al. In polarized MDCK cells basolateral vesicles arise from clathrin–γ-adaptin-coated domains on endosomal tubules. J. Cell Biol. 141, 611–623 (1998). · DOI
  79. Musch, A. Microtubule organization and function in epithelial cells. Traffic 5, 1–9 (2004). · DOI
  80. Allan, V. J., Thompson, H. M. & McNiven, M. A. Motoring around the Golgi. Nature Cell Biol. 4, E236–E242 (2002). · DOI
  81. Hirschberg, K. et al. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J. Cell Biol. 143, 1485–1503 (1998). · DOI
  82. Toomre, D., Keller, P., White, J., Olivo, J. C. & Simons, K. Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells. J. Cell Sci. 112, 21–33 (1999). · DOI
  83. Kreitzer, G., Marmorstein, A., Okamoto, P., Vallee, R. & Rodriguez-Boulan, E. Kinesin and dynamin are required for post-Golgi transport of a plasma-membrane protein. Nature Cell Biol. 2, 125–127 (2000). · DOI
  84. Keller, P., Toomre, D., Diaz, E., White, J. & Simons, K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nature Cell Biol 3, 140–149 (2001). · DOI · Paper page
  85. Kreitzer, G. et al. Three-dimensional analysis of post-Golgi carrier exocytosis in epithelial cells. Nature Cell Biol. 5, 126–136 (2003). Reports live-cell-imaging studies that show the relocation of exocytosis sites when MDCK cells polarize. Basolateral exocytosis localizes to the junctional area. · DOI · Paper page
  86. Jacob, R. & Naim, H. Y. Apical membrane proteins are transported in distinct vesicular carriers. Curr. Biol. 11, 1444–1450 (2001). · DOI
  87. Noda, Y. et al. KIFC3, a microtubule minus end-directed motor for the apical transport of annexin XIIIb-associated Triton-insoluble membranes. J. Cell Biol. 155, 77–88 (2001). · DOI
  88. Stammes, M. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell Biol. 14, 428–433 (2002). · DOI
  89. Musch, A., Cohen, D., Kreitzer, G. & Rodriguez-Boulan, E. Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J. 20, 2171–2179 (2001). · DOI
  90. Durrbach, A., Raposo, G., Tenza, D., Louvard, D. & Coudrier, E. Truncated brush border myosin I affects membrane traffic in polarized epithelial cells. Traffic 1, 411–424 (2000). · DOI
  91. Sheff, D. R., Kroschewski, R. & Mellman, I. Actin dependence of polarized receptor recycling in Madin–Darby canine kidney cell endosomes. Mol. Biol. Cell 13, 262–275 (2002). · DOI
  92. Hales, C. M., Vaerman, J. P. & Goldenring, J. R. Rab11 family interacting protein 2 associates with Myosin Vb and regulates plasma membrane recycling. J. Biol. Chem. 277, 50415–50421 (2002). · DOI
  93. Musch, A., Cohen, D. & Rodriguez-Boulan, E. Myosin II is involved in the production of constitutive transport vesicles from the trans-Golgi network. J. Cell Biol. 138, 291–306 (1997). · DOI
  94. Orth, J. D. & McNiven, M. A. Dynamin at the actin–membrane interface. Curr. Opin. Cell Biol. 15, 31–39 (2003). · DOI
  95. Galli, T. et al. A novel tetanus neurotoxin-insensitive vesicle-associated membrane protein in SNARE complexes of the apical plasma membrane of epithelial cells. Mol. Biol. Cell 9, 1437–1448 (1998). · DOI
  96. Low, S. H. et al. The SNARE machinery is involved in apical plasma membrane trafficking in MDCK cells. J. Cell Biol. 141, 1503–1513 (1998). · DOI
  97. Low, S. H. et al. Differential localization of syntaxin isoforms in polarized Madin–Darby canine kidney cells. Mol. Biol. Cell 7, 2007–2018 (1996). · DOI
  98. Lafont, F. et al. Raft association of SNAP receptors acting in apical trafficking in Madin–Darby canine kidney cells. Proc. Natl Acad. Sci. USA 96, 3734–3738 (1999). · DOI
  99. Riento, K., Kauppi, M., Keranen, S. & Olkkonen, V. M. Munc18-2, a functional partner of syntaxin 3, controls apical membrane trafficking in epithelial cells. J. Biol. Chem. 275, 13476–13483 (2000). · DOI
  100. Lafont, F., Lecat, S., Verkade, P. & Simons, K. Annexin XIIIb associates with lipid microdomains to function in apical delivery. J. Cell Biol. 142, 1413–1427 (1998). · DOI
  101. Jacob, R. et al. Annexin II is required for apical transport in polarized epithelial cells. J. Biol. Chem. 279, 3680–3684 (2004). · DOI
  102. Thurmond, D. C. & Pessin, J. E. Discrimination of GLUT4 vesicle trafficking from fusion using a temperature-sensitive Munc18c mutant. EMBO J. 19, 3565–3575 (2000). · DOI
  103. Musch, A. et al. Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin–Darby canine kidney cells. Mol. Biol. Cell 13, 158–168 (2002). · DOI
  104. Lipschutz, J. H. & Mostov, K. E. Exocytosis: the many masters of the exocyst. Curr. Biol. 12, R212–R214 (2002). · DOI · Paper page
  105. Grindstaff, K. et al. Sec6/8 complex is recruited to cell–cell contacts and specifies transport vesicle delivery to the basal–lateral membrane in epithelial cells. Cell 93, 731–740 (1998). Reports a key role for exocyst in basolateral targeting. · DOI · Paper page
  106. Yeaman, C., Grindstaff, K., Wright, J. & Nelson, W. Sec 6/8 complexes on trans-Golgi network and plasma membrane regulate late stages of exocytosis in mammalian cells. J. Cell Biol. 155, 593–604 (2001). · DOI
  107. Yeaman, C. et al. Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. Nature Cell Biol. 6, 106–112 (2004). · DOI
  108. Moskalenko, S. et al. The exocyst is a Ral effector complex. Nature Cell Biol. 4, 66–72 (2002). · DOI · Paper page
  109. Ang, A., Fölsch, H., Koivisto, U., Pypaert, M. & Mellman, I. The Rab8 GTPase selectively regulates AP-1B-dependent basolateral transport in polarized Madin–Darby canine kidney cells. J. Cell Biol. 163, 339–350 (2003). · DOI
  110. Huber, L. A. et al. Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J. Cell Biol. 123, 35–45 (1993). · DOI
  111. Louvard, D. Apical membrane aminopeptidase appears at site of cell–cell contact in cultured kidney epithelial cells. Proc. Natl Acad. Sci. USA 77, 4132–4136 (1980). · DOI
  112. Kroschewski, R., Hall, A. & Mellman, I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nature Cell Biol. 1, 8–13 (1999). · DOI
  113. Cohen, D., Musch, A. & Rodriguez-Boulan, E. Selective control of basolateral membrane protein polarity by cdc42. Traffic 2, 556–564 (2001). · DOI
  114. Gonzalez-Mariscal, L., Chavez de Ramirez, B. & Cereijido, M. Tight-junction formation in cultured epithelial cells (MDCK). J. Membr. Biol. 86, 113–125 (1985). · DOI
  115. Ojakian, G. K., Nelson, W. J. & Beck, K. A. Mechanisms for de novo biogenesis of an apical membrane compartment in groups of simple epithelial cells surrounded by extracellular matrix. J. Cell Sci. 110, 2781–2794 (1997). · DOI
  116. Vega Salas, D. E., Salas, P. J. & Rodriguez-Boulan, E. Modulation of the expression of an apical plasma membrane protein of Madin–Darby canine kidney epithelial cells: cell–cell interactions control the appearance of a novel intracellular storage compartment. J. Cell Biol. 104, 1249–1259 (1987). · DOI
  117. Low, S. H. et al. Intracellular redirection of plasma membrane trafficking after loss of epithelial cell polarity. Mol. Biol. Cell 11, 3045–3060 (2000). · DOI
  118. Cohen, D., Brennwald, P., Rodriguez-Boulan, E. & Musch, A. Mammalian PAR-1 determines epithelial lumen polarity by organizing the microtubule cytoskeleton. J. Cell Biol. 164, 717–728 (2004). A kinase for microtubule-associated proteins is a key organizer of microtubules and lumen polarity in epithelial cells. · DOI
  119. Vega-Salas, D. E., Salas, P. J. I. & Rodriguez-Boulan, E. Exocytosis of vacuolar apical compartment (VAC): a cell–cell contact controlled mechanism for the establishment of the apical plasma membrane domain in epithelial cells. J. Cell Biol. 107, 1717–1728 (1988). · DOI
  120. Amerongen, H. M., Mack, J. A., Wilson, J. M. & Neutra, M. R. Membrane domains of intestinal epithelial cells: distribution of Na+,K+ ATPase and the membrane skeleton in adult rat intestine during fetal development and after epithelial isolation. J. Cell Biol. 109, 2129–2138 (1989). · DOI
  121. Benton, R., Palacios, I. M. & Johnston, D. S. Drosophila 14-3-3/PAR5 is an essential mediator of PAR-1 function in axis formation. Dev. Cell 3, 659–671 (2002). · DOI
  122. Suzuki, A. et al. aPKC acts upstream of PAR-1b in both the establishment and maintenance of mammalian epithelial polarity. Curr. Biol. 14, 1425–1435 (2004). · DOI
  123. Benton, R. & St Johnston, D. Drosophila PAR-1 and 14-3-3 inhibit Bazooka/PAR-3 to establish complementary cortical domains in polarized cells. Cell 115, 691–704 (2003). · DOI · Paper page
  124. Hurd, T. W. et al. Phosphorylation-dependent binding of 14-3-3 to the polarity protein Par3 regulates cell polarity in mammalian epithelia. Curr. Biol. 13, 2082–2090 (2003). · DOI
  125. Macara, I. G. Par proteins: partners in polarization. Curr. Biol. 14, R160–R162 (2004). · DOI
  126. Baas, A. et al. Complete polarization of single intestinal cells upon activation of LKB1 by Strad. Cell 116, 457–466 (2004). · DOI
  127. Cohen, D., Rodriguez-Boulan, E. & Musch, A. Par-1 promotes a hepatic mode of apical protein trafficking in MDCK cells. Proc. Natl Acad. Sci. USA 101, 13792–13797 (2004). · DOI
  128. Sargiacomo, M., Lisanti, M., Graeve, L., Le Bivic, A. & Rodriguez-Boulan, E. Integral and peripheral protein compositions of the apical and basolateral membrane domains in MDCK cells. J. Memb. Biol. 107, 277–286 (1989). · DOI
  129. Le Bivic, A., Real, F. X. & Rodriguez-Boulan, E. Vectorial targeting of apical and basolateral plasma membrane proteins in a human adenocarcinoma epithelial cell line. Proc. Natl Acad. Sci. USA 86, 9313–9317 (1989). · DOI
  130. Gravotta, D., Adesnik, M. & Sabatini, D. D. Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral membranes: energy dependence and involvement of GTP-binding proteins. J. Cell Biol. 111, 2893–2908 (1990). · DOI
  131. Pimplikar, S. W. & Simons, K. Activators of protein kinase A stimulate apical but not basolateral transport in epithelial Madin–Darby canine kidney cells. J. Biol. Chem. 269, 19054–19059 (1994). · DOI
  132. Simons, K. & Virta, H. Perforated MDCK cells support intracellular transport. EMBO J. 6, 2241–2247 (1987). · DOI
  133. Marmorstein, A. D. et al. Apical polarity of N-CAM and EMMPRIN in retinal pigment epithelium resulting from suppression of basolateral signal recognition. J. Cell Biol. 142, 697–710 (1998). · DOI
  134. Roush, D. L., Gottardi, C. J., Naim, H. Y., Roth, M. G. & Caplan, M. J. 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). · DOI
  135. Casanova, J. E., Mishumi, Y., Ikehara, Y., Hubbard, A. L. & Mostov, K. E. Direct apical sorting of rat liver dipeptidylpeptidase IV expressed in Madin–Darby kidney cells. J. Biol. Chem. 266, 24428–24432 (1991). · DOI
  136. Bonilha, V. L., Marmorstein, A. D., Cohen-Gould, L. & Rodriguez-Boulan, E. Apical sorting of hemagglutinin by transcytosis in retinal pigment epithelium. J. Cell Sci. 110, 1717–1727 (1997). · DOI
  137. Zurzolo, C., Le Bivic, A., Quaroni, A., Nitsch, L. & Rodriguez-Boulan, E. Modulation of transcytotic and direct targeting pathways in a polarized thyroid cell line. EMBO J. 11, 2337–2344 (1992). · DOI
  138. Bartles, J. R., Feracci, H. M., Stieger, B. & Hubbard, A. L. 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). Identifies transcytosis as a primary mode of delivery of apical proteins in liver cells. · DOI
  139. Kipp, H. & Arias, I. M. Newly synthesized canalicular ABC transporters are directly targeted from the Golgi to the hepatocyte apical domain in rat liver. J. Biol. Chem. 275, 15917–15925 (2000). · DOI
  140. Brown, D. A. & Rose, J. K. Sorting of GPI-anchored proteins to glycolipid enriched membrane subdomains during transport to the apical cell surface. Cell 68, 533–544 (1992). Showed that GPI-anchored proteins become lipid-raft-associated as they move into the Golgi complex. · DOI · Paper page
  141. Shvartsman, D. E., Kotler, M., Tall, R. D., Roth, M. G. & Henis, Y. I. Differently anchored influenza hemagglutinin mutants display distinct interaction dynamics with mutual rafts. J. Cell Biol. 163, 879–888 (2003). Reports the biophysical characterization of different types of lipid rafts and their possible role in apical targeting. · DOI
  142. Zurzolo, C., van't Hof, W., van Meer, G. & Rodriguez-Boulan, E. VIP21/caveolin, glycosphingolipid clusters and the sorting of glycosylphosphatidylinositol anchored proteins in epithelial cells. EMBO J. 13, 42–53 (1994). · DOI
  143. Mays, R. W. et al. Hierarchy of mechanisms involved in generating Na/K-ATPase polarity in MDCK epithelial cells. J. Cell Biol. 130, 1105–1115 (1995). · DOI
  144. Keller, P. & Simons, K. Cholesterol is required for surface transport of influenza virus hemagglutinin. J. Cell Biol. 140, 1357–1367 (1998). · DOI
  145. van Meer, G., Stelzer, E. H., Wijnaendts-van-Resandt, R. W. & Simons, K. Sorting of sphingolipids in epithelial (Madin–Darby canine kidney) cells. J. Cell Biol. 105, 1623–1635 (1987). · DOI
  146. van Helvoort, A. et al. MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine. Cell 87, 507–517 (1996). · DOI
  147. Nabi, I. R., Le Bivic, A., Fambrough, D. & Rodriguez-Boulan, E. An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes. J. Cell Biol. 115, 1573–1584 (1991). · DOI
  148. Harter, C. & Mellman, I. Transport of the lysosomal membrane glycoprotein lgp120 (lgp-A) to lysosomes does not require appearance on the plasma membrane. J. Cell Biol. 117, 311–325 (1992). · DOI
  149. Apodaca, G., Katz, L. A. & Mostov, K. E. Receptor-mediated transcytosis of IgA in MDCK cells is via apical recycling endosomes. J. Cell Biol. 125, 67–86 (1994). · DOI
  150. Bruns, J., Ellis, M., Jeromin, A. & Weisz, O. A. Multiple roles for phosphatidylinositol 4-kinase in biosynthetic transport in polarized MDCK cells. J. Biol. Chem. 277, 2012–2018 (2002). · DOI
  151. Verges, M. et al. The mammalian retromer regulates transcytosis of the polymeric immunoglobulin receptor. Nature Cell Biol. 6, 763–769 (2004). · DOI
  152. Carreno, S., Engqvist-Goldstein, A. E., Zhang, C. X., McDonald, K. L. & Drubin, D. G. Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network. J. Cell Biol. 165, 781–788 (2004). · DOI · Paper page
  153. Casanova, J. E. et al. Association of Rab25 and Rab11a with the apical recycling system of polarized Madin–Darby canine kidney cells. Mol. Biol. Cell 10, 47–61 (1999). · DOI
  154. Yeaman, C., Grindstaff, K. K. & Nelson, W. J. Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells. J. Cell Sci. 117, 559–570 (2004). · DOI
  155. Bacallao, R. et al. The subcellular organization of Madin–Darby canine kidney cells during the formation of a polarized epithelium. J. Cell Biol. 109, 2817–2832 (1989). · DOI · Paper page

Cited by

Sorted by citations

Metadata

Authors
Rodriguez-Boulan, E., Kreitzer, G., & Müsch, A.
Venue
Nature Reviews Molecular Cell Biology
Publisher
Springer Science and Business Media LLC
Published
2005-03
Volume
6
Issue
3
Pages
233-247
ISSN
  • 1471-0072
  • 1471-0080
DOI
10.1038/nrm1593
Cited by
574
References
4
Language
en
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review