메뉴 건너뛰기




Volumn 43, Issue C, 1996, Pages 15-25

Chapter 2 Once There, Making the Descision To Stay or Leave

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0343882362     PISSN: 00702161     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0070-2161(08)60382-2     Document Type: Article
Times cited : (3)

References (40)
  • 1
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet.
    • Anderson R. Caveolae: Where incoming and outgoing messengers meet. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 10909-10913
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 10909-10913
    • Anderson, R.1
  • 2
    • 0029905387 scopus 로고    scopus 로고
    • The spectrin-based membrane skeleton as a membrane protein sorting machine.
    • Beck K.A., and Nelson W.J. The spectrin-based membrane skeleton as a membrane protein sorting machine. Am. J. Physiol. (Cell). 270 (1996) C1263-C1270
    • (1996) Am. J. Physiol. (Cell). , vol.270
    • Beck, K.A.1    Nelson, W.J.2
  • 3
    • 0027993053 scopus 로고
    • Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex.
    • Beck K.A., Malhotra V., and Nelson W.J. Golgi spectrin: Identification of an erythroid beta-spectrin homolog associated with the Golgi complex. J. Cell Biol. 127 (1994) 707-723
    • (1994) J. Cell Biol. , vol.127 , pp. 707-723
    • Beck, K.A.1    Malhotra, V.2    Nelson, W.J.3
  • 4
    • 0026806912 scopus 로고
    • Ankyrins: Adaptors between diverse plasma membrane proteins and the cytoplasm.
    • Bennett V. Ankyrins: Adaptors between diverse plasma membrane proteins and the cytoplasm. J. Biol. Chem. 267 (1992) 8703-8706
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 5
    • 0027333413 scopus 로고
    • The spectrin-based membrane skeleton and micronscale organization of the plasma membrane.
    • Bennett V., and Gilligan D. The spectrin-based membrane skeleton and micronscale organization of the plasma membrane. Annu. Rev. Cell Biol. 9 (1993) 27-66
    • (1993) Annu. Rev. Cell Biol. , vol.9 , pp. 27-66
    • Bennett, V.1    Gilligan, D.2
  • 6
    • 0028176099 scopus 로고
    • Rapid capping in alpha-spectrin deficient MEL cells from mice afflicted with hereditary hemolytic anemia.
    • Dahl S.C., Greib R.W., Fox M.T., Edidin M., and Branton D. Rapid capping in alpha-spectrin deficient MEL cells from mice afflicted with hereditary hemolytic anemia. J. Cell Biol. 125 (1994) 1057-1066
    • (1994) J. Cell Biol. , vol.125 , pp. 1057-1066
    • Dahl, S.C.1    Greib, R.W.2    Fox, M.T.3    Edidin, M.4    Branton, D.5
  • 7
    • 0025115664 scopus 로고
    • +-ATPase interact with distinct sites on ankyrin in in vitro assays.
    • +-ATPase interact with distinct sites on ankyrin in in vitro assays. J. Biol. Chem. 265 (1990) 17252-17256
    • (1990) J. Biol. Chem. , vol.265 , pp. 17252-17256
    • Davis, J.1    Bennett, V.2
  • 8
    • 0028262115 scopus 로고
    • Ankyrin binds to two distinct cytoplasmic domains of Na, K-ATPase α subunit.
    • Devarajan P., Scaramuzzino D.A., and Morrow J.S. Ankyrin binds to two distinct cytoplasmic domains of Na, K-ATPase α subunit. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 2965-2969
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 2965-2969
    • Devarajan, P.1    Scaramuzzino, D.A.2    Morrow, J.S.3
  • 9
    • 0022411389 scopus 로고
    • Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney.
    • Drenckhahn D., Schulter K., Allen D., and Bennett V. Colocalization of band 3 with ankyrin and spectrin at the basal membrane of intercalated cells in the rat kidney. Science 230 (1985) 1287-1289
    • (1985) Science , vol.230 , pp. 1287-1289
    • Drenckhahn, D.1    Schulter, K.2    Allen, D.3    Bennett, V.4
  • 10
    • 0022975133 scopus 로고
    • The trans Golgi network: Sorting at the exit site of the Golgi complex.
    • Griffiths G., and Simons K. The trans Golgi network: Sorting at the exit site of the Golgi complex. Science 234 (1986) 438-443
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 11
    • 0026085673 scopus 로고
    • Apical polarity of Na, K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submem-brane cytoskeleton.
    • Gundersen D., Orlowski J., and Rodriguez-Boulan E. Apical polarity of Na, K-ATPase in retinal pigment epithelium is linked to a reversal of the ankyrin-fodrin submem-brane cytoskeleton. J. Cell Biol. 112 (1991) 863-872
    • (1991) J. Cell Biol. , vol.112 , pp. 863-872
    • Gundersen, D.1    Orlowski, J.2    Rodriguez-Boulan, E.3
  • 12
    • 0026322157 scopus 로고
    • Mechanism for regulating cell surface distribution of Na/K-ATPase in polarized epithelial cells.
    • Hammerton R.W., Krzeminski K.A., Mays R.W., Wollner D.A., and Nelson W.J. Mechanism for regulating cell surface distribution of Na/K-ATPase in polarized epithelial cells. Science 254 (1991) 847-850
    • (1991) Science , vol.254 , pp. 847-850
    • Hammerton, R.W.1    Krzeminski, K.A.2    Mays, R.W.3    Wollner, D.A.4    Nelson, W.J.5
  • 13
    • 0028305138 scopus 로고
    • Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex formation.
    • Hinck L., Nathke I.S., Papkoff J., and Nelson W.J. Dynamics of cadherin/catenin complex formation: Novel protein interactions and pathways of complex formation. J. Cell Biol. 125 (1994) 1327-1340
    • (1994) J. Cell Biol. , vol.125 , pp. 1327-1340
    • Hinck, L.1    Nathke, I.S.2    Papkoff, J.3    Nelson, W.J.4
  • 14
    • 0024344616 scopus 로고
    • ++-dependent association with sites of cell-cell contact.
    • ++-dependent association with sites of cell-cell contact. J. Cell Biol. 109 (1989) 557-569
    • (1989) J. Cell Biol. , vol.109 , pp. 557-569
    • Kaiser, H.W.1    O'Keefe, E.2    Bennett, V.3
  • 15
    • 0025345414 scopus 로고
    • Clathrin and associated assembly and disassembly proteins.
    • Keen J.H. Clathrin and associated assembly and disassembly proteins. Annu. Rev. Biochem. 59 (1990) 415-438
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 415-438
    • Keen, J.H.1
  • 16
    • 0024745305 scopus 로고
    • 2+-dependent cell adhesion molecule.
    • 2+-dependent cell adhesion molecule. Bioessays 11 (1989) 88-91
    • (1989) Bioessays , vol.11 , pp. 88-91
    • Kemler, R.1    Ozawa, M.2
  • 17
    • 0025231649 scopus 로고
    • An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves.
    • Kordeli E., Davis J., Trapp B., and Bennett V. An isoform of ankyrin is localized at nodes of Ranvier in myelinated axons of central and peripheral nerves. J. Cell Biol. 110 (1990) 1341-1352
    • (1990) J. Cell Biol. , vol.110 , pp. 1341-1352
    • Kordeli, E.1    Davis, J.2    Trapp, B.3    Bennett, V.4
  • 18
    • 0028068272 scopus 로고
    • Coat proteins in intracellular membrane transport.
    • Kreis T., and Pepperkok R. Coat proteins in intracellular membrane transport. Curr. Opin. Cell Biol. 6 (1994) 533-537
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 533-537
    • Kreis, T.1    Pepperkok, R.2
  • 19
    • 0020585554 scopus 로고
    • Erythrocyte and brain forms of spectrin in cerebellum: Distinct membrane-cytoskeletal domains in neurons.
    • Lazarides E., and Nelson W. Erythrocyte and brain forms of spectrin in cerebellum: Distinct membrane-cytoskeletal domains in neurons. Science 220 (1983) 1295-1296
    • (1983) Science , vol.220 , pp. 1295-1296
    • Lazarides, E.1    Nelson, W.2
  • 20
    • 0027756154 scopus 로고
    • Cell shape and interaction defects in α-spectrin mutants of Drosophila melanogaster.
    • Lee J.K., Coyne R.S., Dubreuil R.R., Goldstein L.S.B., and Branton D. Cell shape and interaction defects in α-spectrin mutants of Drosophila melanogaster. J. Cell Biol. 123 (1993) 1797-1809
    • (1993) J. Cell Biol. , vol.123 , pp. 1797-1809
    • Lee, J.K.1    Coyne, R.S.2    Dubreuil, R.R.3    Goldstein, L.S.B.4    Branton, D.5
  • 24
    • 0025325815 scopus 로고
    • Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity.
    • McNeill H., Ozawa M., Kemler R., and Nelson W.J. Novel function of the cell adhesion molecule uvomorulin as an inducer of cell surface polarity. Cell 62 (1990) 309-316
    • (1990) Cell , vol.62 , pp. 309-316
    • McNeill, H.1    Ozawa, M.2    Kemler, R.3    Nelson, W.J.4
  • 26
    • 0028920639 scopus 로고
    • Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes.
    • Narula N., and Stow J. Distinct coated vesicles labeled for p200 bud from trans-Golgi network membranes. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 2874-2878
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 2874-2878
    • Narula, N.1    Stow, J.2
  • 28
    • 0026446341 scopus 로고
    • Regulation of cell surface polarity from bacteria to mammals.
    • Nelson W.J. Regulation of cell surface polarity from bacteria to mammals. Science 258 (1992) 948-955
    • (1992) Science , vol.258 , pp. 948-955
    • Nelson, W.J.1
  • 29
    • 0024554715 scopus 로고
    • +-ATPase, ankyrin, and fodrin in Madin-Darby canine kidney (MDCK) cells: Implications for the biogenesis of epithelial cell polarity.
    • +-ATPase, ankyrin, and fodrin in Madin-Darby canine kidney (MDCK) cells: Implications for the biogenesis of epithelial cell polarity. J. Cell Biol. 108 (1989) 893-902
    • (1989) J. Cell Biol. , vol.108 , pp. 893-902
    • Nelson, W.J.1    Hammerton, R.W.2
  • 30
    • 0023001826 scopus 로고
    • Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby canine kidney epithelial cells.
    • Nelson W.J., and Veshnock P.J. Dynamics of membrane-skeleton (fodrin) organization during development of polarity in Madin-Darby canine kidney epithelial cells. J Cell Biol. 103 (1986) 1751-1766
    • (1986) J Cell Biol. , vol.103 , pp. 1751-1766
    • Nelson, W.J.1    Veshnock, P.J.2
  • 31
    • 0023262074 scopus 로고
    • +-ATPase and implications for the organization of membrane domains in polarized cells.
    • +-ATPase and implications for the organization of membrane domains in polarized cells. Nature (London) 328 (1987) 533-536
    • (1987) Nature (London) , vol.328 , pp. 533-536
    • Nelson, W.J.1    Veshnock, P.J.2
  • 32
    • 0023267654 scopus 로고
    • Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells.
    • Nelson W.J., and Veshnock P.J. Modulation of fodrin (membrane skeleton) stability by cell-cell contact in Madin-Darby canine kidney epithelial cells. J. Cell Biol. 104 (1987) 1527-1537
    • (1987) J. Cell Biol. , vol.104 , pp. 1527-1537
    • Nelson, W.J.1    Veshnock, P.J.2
  • 33
    • 0025125799 scopus 로고
    • Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells.
    • Nelson W.J., Shore E.M., Wang A.Z., and Hammerton R.W. Identification of a membrane-cytoskeletal complex containing the cell adhesion molecule uvomorulin (E-cadherin), ankyrin, and fodrin in Madin-Darby canine kidney epithelial cells. J Cell Biol 110 (1990) 349-357
    • (1990) J Cell Biol , vol.110 , pp. 349-357
    • Nelson, W.J.1    Shore, E.M.2    Wang, A.Z.3    Hammerton, R.W.4
  • 34
  • 35
    • 0023485004 scopus 로고
    • Hereditary elliptocytosis, spherocytosis and related disorders: Consequences of a deficiency or a mutation of membrane skeletal proteins.
    • Palek J. Hereditary elliptocytosis, spherocytosis and related disorders: Consequences of a deficiency or a mutation of membrane skeletal proteins. Blood Rev. 1 (1987) 147-168
    • (1987) Blood Rev. , vol.1 , pp. 147-168
    • Palek, J.1
  • 36
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi.
    • Pfeffer S.R., and Rothman J.E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 56 (1987) 829-852
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 37
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis.
    • Robinson M. The role of clathrin, adaptors and dynamin in endocytosis. Curr. Opin. Cell Biol. 6 (1994) 538-544
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 538-544
    • Robinson, M.1
  • 38
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics.
    • Rothman J.E., and Warren G. Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4 (1994) 220-233
    • (1994) Curr. Biol. , vol.4 , pp. 220-233
    • Rothman, J.E.1    Warren, G.2
  • 39
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes.
    • Sheetz M.P., Schindler M., and Koppel D. Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature (London) 285 (1980) 510-512
    • (1980) Nature (London) , vol.285 , pp. 510-512
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.3
  • 40
    • 0026628312 scopus 로고
    • 100-kD proteins of Golgi-and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties.
    • Wong D.H., and Brodsky F.M. 100-kD proteins of Golgi-and trans-Golgi network-associated coated vesicles have related but distinct membrane binding properties. J. Cell Biol. 117 (1992) 1171-1179
    • (1992) J. Cell Biol. , vol.117 , pp. 1171-1179
    • Wong, D.H.1    Brodsky, F.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.