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Volumn 112, Issue 6, 1999, Pages 785-795

Opposing motor activities of dynein and kinesin determine retention and transport of MHC class II-containing compartments

Author keywords

Antigen presentation; Dynamitin; Dynein; Kinesin; MHC class II; MIIC; Vesicular transport

Indexed keywords

DYNEIN ADENOSINE TRIPHOSPHATASE; KINESIN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; PROTEIN KINASE INHIBITOR; STAUROSPORINE;

EID: 0032900957     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (82)

References (84)
  • 1
    • 0032525027 scopus 로고    scopus 로고
    • Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments
    • Anderson, H. A. and Roche, P. A. (1998). Phosphorylation regulates the delivery of MHC class II invariant chain complexes to antigen processing compartments. J. Immunol. 160, 4850-4858.
    • (1998) J. Immunol. , vol.160 , pp. 4850-4858
    • Anderson, H.A.1    Roche, P.A.2
  • 2
    • 0027730175 scopus 로고
    • Cytoplasmic dynein-dependent vesicular transport from early to late endosomes
    • Aniento, F., Emans, N., Griffiths, G. and Gruenberg, J. (1993). Cytoplasmic dynein-dependent vesicular transport from early to late endosomes. J. Cell Biol. 123, 1373-1387.
    • (1993) J. Cell Biol. , vol.123 , pp. 1373-1387
    • Aniento, F.1    Emans, N.2    Griffiths, G.3    Gruenberg, J.4
  • 3
    • 0028676010 scopus 로고
    • In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides
    • Avva, R. R. and Cresswell, P. (1994). In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides. Immunity, 1, 763-774.
    • (1994) Immunity , vol.1 , pp. 763-774
    • Avva, R.R.1    Cresswell, P.2
  • 5
    • 0011720253 scopus 로고
    • Role for intracellular proteases in the processing and transport of class II HLA antigens
    • Blum, J. S. and Cresswell, P. (1988). Role for intracellular proteases in the processing and transport of class II HLA antigens. Proc. Natl. Acad. Sci. USA 85, 3975-3979.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3975-3979
    • Blum, J.S.1    Cresswell, P.2
  • 6
    • 0030727535 scopus 로고    scopus 로고
    • Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution
    • Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997). Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol. 139, 469-484.
    • (1997) J. Cell Biol. , vol.139 , pp. 469-484
    • Burkhardt, J.K.1    Echeverri, C.J.2    Nilsson, T.3    Vallee, R.B.4
  • 7
    • 0030858138 scopus 로고    scopus 로고
    • Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells
    • Cella, M., Engering, A., Pinet, V., Pieters, J. and Lanzavecchia, A. (1997). Inflammatory stimuli induce accumulation of MHC class II complexes on dendritic cells. Nature 388, 782-787.
    • (1997) Nature , vol.388 , pp. 782-787
    • Cella, M.1    Engering, A.2    Pinet, V.3    Pieters, J.4    Lanzavecchia, A.5
  • 8
    • 0028313992 scopus 로고
    • Assembly, transport, and function of MHC class II molecules
    • Cresswell, P. (1994). Assembly, transport, and function of MHC class II molecules. Anna. Rev. Immunol. 12, 259-293.
    • (1994) Anna. Rev. Immunol. , vol.12 , pp. 259-293
    • Cresswell, P.1
  • 9
    • 0030028779 scopus 로고    scopus 로고
    • Invariant chain structure and MHC class II function
    • Cresswell, P. (1996). Invariant chain structure and MHC class II function. Cell 84, 505-507.
    • (1996) Cell , vol.84 , pp. 505-507
    • Cresswell, P.1
  • 10
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing, J., Roth, W., Saftig, P., Peters, C., Ploegh, H. L. and Villadangos, J. A. (1998). Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc. Natl. Acad. Sci. USA 95, 4516-4521.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3    Peters, C.4    Ploegh, H.L.5    Villadangos, J.A.6
  • 11
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • Echeverri, C. J., Paschal, B. M., Vaughan, K. T. and Vallee, R. B. (1998). Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J. Cell Biol. 132, 617-633.
    • (1998) J. Cell Biol. , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 12
    • 0031587788 scopus 로고    scopus 로고
    • Dynactin phosphorylation is modulated in response to cellular effectors
    • Farshori, P. and Holzbaur, E. L. (1997). Dynactin phosphorylation is modulated in response to cellular effectors. Biochem. Biophys. Res. Commun. 232, 810-816.
    • (1997) Biochem. Biophys. Res. Commun. , vol.232 , pp. 810-816
    • Farshori, P.1    Holzbaur, E.L.2
  • 15
    • 0031444202 scopus 로고    scopus 로고
    • An extending microtubule-binding structure within the dynein binding domain
    • Gee, M. A., Heuser, J. E. and Vallee, R. B. (1998). An extending microtubule-binding structure within the dynein binding domain. Nature 390, 636-639.
    • (1998) Nature , vol.390 , pp. 636-639
    • Gee, M.A.1    Heuser, J.E.2    Vallee, R.B.3
  • 16
    • 0028823585 scopus 로고
    • The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3
    • Ghosh, P., Amaya, M., Mellins, E. and Wiley, D. C. (1995). The structure of an intermediate in class II MHC maturation: CLIP bound to HLA-DR3. Nature 378, 457-462.
    • (1995) Nature , vol.378 , pp. 457-462
    • Ghosh, P.1    Amaya, M.2    Mellins, E.3    Wiley, D.C.4
  • 20
    • 0027957063 scopus 로고
    • Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules
    • Hagiwara, H., Yorifuji, H., Sato-Yoshitake, R. and Hirokawa, N. (1994). Competition between motor molecules (kinesin and cytoplasmic dynein) and fibrous microtubule-associated proteins in binding to microtubules. J. Biol. Chem. 269, 3581-3589.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3581-3589
    • Hagiwara, H.1    Yorifuji, H.2    Sato-Yoshitake, R.3    Hirokawa, N.4
  • 21
    • 0024351343 scopus 로고
    • Lysed chromatophores: A model system for the study of bidirectional organelle transport
    • Haimo, L. T. and Rozdzial, M. M. (1989). Lysed chromatophores: a model system for the study of bidirectional organelle transport. Methods Cell Biol. 31, 3-24.
    • (1989) Methods Cell Biol. , vol.31 , pp. 3-24
    • Haimo, L.T.1    Rozdzial, M.M.2
  • 22
    • 0027491245 scopus 로고
    • Regulation of vesicle transport in CV-1 cells and extracts
    • Hamm-Alvarez, S. F., Kim, P. Y. and Sheetz, M. P. (1993). Regulation of vesicle transport in CV-1 cells and extracts. J. Cell Sci. 106, 955-966.
    • (1993) J. Cell Sci. , vol.106 , pp. 955-966
    • Hamm-Alvarez, S.F.1    Kim, P.Y.2    Sheetz, M.P.3
  • 23
    • 0030087710 scopus 로고    scopus 로고
    • Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer
    • Heim, R. and Tsien, R. Y. (1996). Engineering green fluorescent protein for improved brightness, longer wavelengths and fluorescence resonance energy transfer. Curr. Biol. 6, 178-182.
    • (1996) Curr. Biol. , vol.6 , pp. 178-182
    • Heim, R.1    Tsien, R.Y.2
  • 24
    • 0032559260 scopus 로고    scopus 로고
    • Kinesin and dynein superfamily proteins and the mechanism of organelle transport
    • Hirokawa, N. (1998). Kinesin and dynein superfamily proteins and the mechanism of organelle transport. Science 279, 519-526.
    • (1998) Science , vol.279 , pp. 519-526
    • Hirokawa, N.1
  • 25
    • 0022360053 scopus 로고
    • Purification and characterization of a cation-dependent mannose 6-phosphale receptor from murine P388DI macrophages and bovine liver
    • Hoflack, B. and Kornfeld, S. (1985). Purification and characterization of a cation-dependent mannose 6-phosphale receptor from murine P388DI macrophages and bovine liver. J. Biol. Chem. 260, 12008-12014.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12008-12014
    • Hoflack, B.1    Kornfeld, S.2
  • 26
    • 0025045429 scopus 로고
    • Radial extension of macrophage tubular lysosomes supported by kinesin
    • Hollenbeck, P. J. and Swanson, J. A. (1990). Radial extension of macrophage tubular lysosomes supported by kinesin. Nature 346, 864-866.
    • (1990) Nature , vol.346 , pp. 864-866
    • Hollenbeck, P.J.1    Swanson, J.A.2
  • 27
    • 0027263661 scopus 로고
    • Phosphorylation of neuronal kinesin heavy and light chains in vivo
    • Hollenbeck, P. J. (1993). Phosphorylation of neuronal kinesin heavy and light chains in vivo. J. Neurochem. 60, 2265-2275.
    • (1993) J. Neurochem. , vol.60 , pp. 2265-2275
    • Hollenbeck, P.J.1
  • 28
    • 0028170819 scopus 로고
    • DYNEINS: Molecular structure and cellular function
    • Holzbaur, E. L. and Vallee, R. B. (1994). DYNEINS: molecular structure and cellular function. Annu. Rev. Cell Biol. 10, 339-372.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 339-372
    • Holzbaur, E.L.1    Vallee, R.B.2
  • 29
    • 0021922406 scopus 로고
    • A teflon culture dish for high-magnification microscopy and measurements in single cells
    • Ince, C., van Dissel, J. T. and Diesselhoff, M. M. (1985). A teflon culture dish for high-magnification microscopy and measurements in single cells. Pflugers Arch. 403, 240-244.
    • (1985) Pflugers Arch. , vol.403 , pp. 240-244
    • Ince, C.1    Van Dissel, J.T.2    Diesselhoff, M.M.3
  • 30
    • 0032509943 scopus 로고    scopus 로고
    • Antigen processing: HLA-DO - A hitchhiking inhibitor of HLA-DM
    • Jensen, P. E. (1998). Antigen processing: HLA-DO - a hitchhiking inhibitor of HLA-DM. Curr. Biol. 8, R128-31.
    • (1998) Curr. Biol. , vol.8
    • Jensen, P.E.1
  • 31
    • 0028618339 scopus 로고
    • Reconstitution of an operational MHC class II compartment in nonantigen-presenting cells
    • Karlsson, L., Peleraux, A., Lindstedt, R., Liljedahl, M. and Peterson, P. A. (1994). Reconstitution of an operational MHC class II compartment in nonantigen-presenting cells. Science 266, 1569-1573.
    • (1994) Science , vol.266 , pp. 1569-1573
    • Karlsson, L.1    Peleraux, A.2    Lindstedt, R.3    Liljedahl, M.4    Peterson, P.A.5
  • 33
    • 0031406170 scopus 로고    scopus 로고
    • Interleukin-10 down-regulates MHC class II ab peptide complexes at the plasma membrane of monocyte by affecting arrival and recycling
    • Koppelman, B., Neefjes, J., de Vries, J. E. and de Waal Malefyt, R. (1997). Interleukin-10 down-regulates MHC class II ab peptide complexes at the plasma membrane of monocyte by affecting arrival and recycling. Immunity 7, 861-871.
    • (1997) Immunity , vol.7 , pp. 861-871
    • Koppelman, B.1    Neefjes, J.2    De Vries, J.E.3    De Waal Malefyt, R.4
  • 35
    • 0028933382 scopus 로고
    • Kinectin, an essential anchor for kinesin-driven vesicle motility
    • Kumar, J., Yu, H. and Sheetz, M. P. (1995). Kinectin, an essential anchor for kinesin-driven vesicle motility. Science 267, 1834-1837.
    • (1995) Science , vol.267 , pp. 1834-1837
    • Kumar, J.1    Yu, H.2    Sheetz, M.P.3
  • 36
    • 0028939893 scopus 로고
    • Phosphorylation of kinesin in vivo correlates with organelle association and neurite outgrowth
    • Lee, K. D. and Hollenbeck, P. J. (1995). Phosphorylation of kinesin in vivo correlates with organelle association and neurite outgrowth. J. Biol. Chem. 270, 5600-5605.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5600-5605
    • Lee, K.D.1    Hollenbeck, P.J.2
  • 38
    • 0028139160 scopus 로고
    • Cytoplasmic dynein undergoes intracellular redistribution concomitant with phosphorylation of the heavy chain in response to serum starvation and okadaic acid
    • Lin, S. X., Ferro, K. L. and Collins, C. A. (1994). Cytoplasmic dynein undergoes intracellular redistribution concomitant with phosphorylation of the heavy chain in response to serum starvation and okadaic acid. J. Cell Biol. 127, 1009-1019.
    • (1994) J. Cell Biol. , vol.127 , pp. 1009-1019
    • Lin, S.X.1    Ferro, K.L.2    Collins, C.A.3
  • 39
    • 0029738637 scopus 로고    scopus 로고
    • Comparison of the intracellular distribution of cytoplasmic dynein and kinesin in cultured cells: Motor protein location does not reliably predict function
    • Lin, S. X., Pfister, K. K. and Collins, C. A. (1996). Comparison of the intracellular distribution of cytoplasmic dynein and kinesin in cultured cells: motor protein location does not reliably predict function. Cell Motil. Cytoskel. 34, 299-312.
    • (1996) Cell Motil. Cytoskel. , vol.34 , pp. 299-312
    • Lin, S.X.1    Pfister, K.K.2    Collins, C.A.3
  • 40
    • 0030884680 scopus 로고    scopus 로고
    • Phosphotransferases associated with the regulation of kinesin motor activity
    • Lindesmith, L., McIlvain Jr., J. M., Argon, Y. and Sheetz, M. P. (1997). Phosphotransferases associated with the regulation of kinesin motor activity. J.Biol.Chem. 272, 22929-22933.
    • (1997) J.biol.chem. , vol.272 , pp. 22929-22933
    • Lindesmith, L.1    McIlvain J.M., Jr.2    Argon, Y.3    Sheetz, M.P.4
  • 41
    • 0029103105 scopus 로고
    • Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex
    • Lippincott-Schwartz, J. and Cole, N. B. (1995). Roles for microtubules and kinesin in membrane traffic between the endoplasmic reticulum and the Golgi complex. Biochem. Soc. Trans. 23, 544-548.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 544-548
    • Lippincott-Schwartz, J.1    Cole, N.B.2
  • 42
    • 0027533201 scopus 로고
    • Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2
    • Lopez, L. A. and Sheetz, M. P. (1993). Steric inhibition of cytoplasmic dynein and kinesin motility by MAP2. Cell Motil. Cytoskel. 24, 1-16.
    • (1993) Cell Motil. Cytoskel. , vol.24 , pp. 1-16
    • Lopez, L.A.1    Sheetz, M.P.2
  • 43
    • 0028853165 scopus 로고
    • Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells
    • Morton, P. A., Zacheis, M. L., Giacoletto, K. S., Manning, J. A. and Schwartz, B. D. (1995). Delivery of nascent MHC class II-invariant chain complexes to lysosomal compartments and proteolysis of invariant chain by cysteine proteases precedes peptide binding in B-lymphoblastoid cells. J. Immunol. 154, 137-150.
    • (1995) J. Immunol. , vol.154 , pp. 137-150
    • Morton, P.A.1    Zacheis, M.L.2    Giacoletto, K.S.3    Manning, J.A.4    Schwartz, B.D.5
  • 44
    • 0028871742 scopus 로고
    • Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport
    • Nakata, T. and Hirokawa, N. (1995). Point mutation of adenosine triphosphate-binding motif generated rigor kinesin that selectively blocks anterograde lysosome membrane transport. J. Cell Biol. 131, 1039-1053.
    • (1995) J. Cell Biol. , vol.131 , pp. 1039-1053
    • Nakata, T.1    Hirokawa, N.2
  • 45
    • 0026632855 scopus 로고
    • Cloning and expression of a human kinesin heavy chain gene: Interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells
    • Navone, F., Niclas, J., Hom-Booher, N., Sparks, L., Bernstein, H. D., McCaffrey, G. and Vale, R. D. (1992). Cloning and expression of a human kinesin heavy chain gene: interaction of the COOH-terminal domain with cytoplasmic microtubules in transfected CV-1 cells. J. Cell Biol. 117, 1263-1275.
    • (1992) J. Cell Biol. , vol.117 , pp. 1263-1275
    • Navone, F.1    Niclas, J.2    Hom-Booher, N.3    Sparks, L.4    Bernstein, H.5    McCaffrey, G.6    Vale, R.D.7
  • 46
    • 0026583941 scopus 로고
    • Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistance alpha-beta heterodimers in endosomes
    • Neefjes, J. J. and Ploegh, H. L. (1992). Inhibition of endosomal proteolytic activity by leupeptin blocks surface expression of MHC class II molecules and their conversion to SDS resistance alpha-beta heterodimers in endosomes. EMBO J. 11, 411-416.
    • (1992) EMBO J. , vol.11 , pp. 411-416
    • Neefjes, J.J.1    Ploegh, H.L.2
  • 47
    • 0024589213 scopus 로고
    • Time course of intracellular associations, processing, and cleavages of Ii forms and class II major histocompatibility complex molecules
    • Nguyen, Q. V. and Humphreys, R. E. (1989). Time course of intracellular associations, processing, and cleavages of Ii forms and class II major histocompatibility complex molecules. J. Biol. Chem. 264, 1631-1637.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1631-1637
    • Nguyen, Q.V.1    Humphreys, R.E.2
  • 49
    • 0029013998 scopus 로고
    • Interaction of the microtubule cytoskeleton with endocytic vesicles and cytoplasmic dynein in cultured rat hepatocytes
    • Oda, H., Stockert, R. J., Collins, C, Wang, H., Novikoff, P. M., Satir, P. and Wolkoff, A. W. (1995). Interaction of the microtubule cytoskeleton with endocytic vesicles and cytoplasmic dynein in cultured rat hepatocytes. J. Biol. Chem. 270, 15242-15249.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15242-15249
    • Oda, H.1    Stockert, R.J.2    Collins, C.3    Wang, H.4    Novikoff, P.M.5    Satir, P.6    Wolkoff, A.W.7
  • 50
    • 0023608935 scopus 로고
    • MAP IC is a microtubule-aclivated ATPase which translocates microtubules in vitro and has dynein-like properties
    • Paschal, B. M., Shpetner, H. S. and Vallee, R. B. (1987). MAP IC is a microtubule-aclivated ATPase which translocates microtubules in vitro and has dynein-like properties. J. Cell Biol. 105, 1273-1282.
    • (1987) J. Cell Biol. , vol.105 , pp. 1273-1282
    • Paschal, B.M.1    Shpetner, H.S.2    Vallee, R.B.3
  • 51
    • 0027435586 scopus 로고
    • Chediak-Higashi syndrome is not due to a defect in microtubule-based lysosomal mobility
    • Perou, C. M. and Kaplan, J. (1993). Chediak-Higashi syndrome is not due to a defect in microtubule-based lysosomal mobility. J. Cell Sci. 106, 99-107.
    • (1993) J. Cell Sci. , vol.106 , pp. 99-107
    • Perou, C.M.1    Kaplan, J.2
  • 52
    • 0026034448 scopus 로고
    • Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments
    • Peters, P. J., Neefjes, J. J., Oorschot, V, Ploegh, H. L. and Geuze, H. J. (1991). Segregation of MHC class II molecules from MHC class I molecules in the Golgi complex for transport to lysosomal compartments. Nature 349, 669-676.
    • (1991) Nature , vol.349 , pp. 669-676
    • Peters, P.J.1    Neefjes, J.J.2    Oorschot, V.3    Ploegh, H.L.4    Geuze, H.J.5
  • 53
    • 0029923571 scopus 로고    scopus 로고
    • HLA-DM is localized to conventional and unconventional MHC class II-containing endocytic compartments
    • Pierre, P., Denzin, L. K., Hammond, C., Drake, J. R., Amigorena, S., Cresswell, P. and Mellman, I. (1996). HLA-DM is localized to conventional and unconventional MHC class II-containing endocytic compartments. Immunity 4, 229-239.
    • (1996) Immunity , vol.4 , pp. 229-239
    • Pierre, P.1    Denzin, L.K.2    Hammond, C.3    Drake, J.R.4    Amigorena, S.5    Cresswell, P.6    Mellman, I.7
  • 55
    • 0032568806 scopus 로고    scopus 로고
    • Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre, P. and Mellman, I. (1998). Developmental regulation of invariant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 93, 1135-1145.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 56
    • 0025824732 scopus 로고
    • Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain
    • Pieters, J., Horstmann, H., Bakke, O., Griffiths, G. and Lipp, J. (1991). Intracellular transport and localization of major histocompatibility complex class II molecules and associated invariant chain. J. Cell Biol. 115, 1213-1223.
    • (1991) J. Cell Biol. , vol.115 , pp. 1213-1223
    • Pieters, J.1    Horstmann, H.2    Bakke, O.3    Griffiths, G.4    Lipp, J.5
  • 57
    • 0030889062 scopus 로고    scopus 로고
    • Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells
    • Prescott, A. R., Lucocq, J. M., James, J., Lister, J. M. and Ponnambalam, S. (1997). Distinct compartmentalization of TGN46 and beta 1,4-galactosyltransferase in HeLa cells. Eur. J. Cell Biol. 72, 238-246.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 238-246
    • Prescott, A.R.1    Lucocq, J.M.2    James, J.3    Lister, J.M.4    Ponnambalam, S.5
  • 58
    • 0021326933 scopus 로고
    • A human Ia cytoplasmic determinant located on multiple forms of invariant chain (gamma, gamma 2, gamma 3)
    • Quaranta, V., Majdic, O., Stingl, G., Liszka, K., Honigsmann, H. and Knapp, W. (1984). A human Ia cytoplasmic determinant located on multiple forms of invariant chain (gamma, gamma 2, gamma 3). J. Immunol. 132, 1900-1905.
    • (1984) J. Immunol. , vol.132 , pp. 1900-1905
    • Quaranta, V.1    Majdic, O.2    Stingl, G.3    Liszka, K.4    Honigsmann, H.5    Knapp, W.6
  • 59
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Reise, R. J., Wolf, P. R., Bromme, D., Natkin, L. R., Villadangos, J. A., Ploegh, H. L. and Chapman, H. A. (1996). Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 4, 357-366.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Reise, R.J.1    Wolf, P.R.2    Bromme, D.3    Natkin, L.R.4    Villadangos, J.A.5    Ploegh, H.L.6    Chapman, H.A.7
  • 60
    • 0029979452 scopus 로고    scopus 로고
    • Trafficking of major histocompatibility complex class II molecules through intracellular compartments containing HLA-DM
    • Robbins, N. F., Hammond, C., Denzin, L. K., Pan, M. and Cresswell, P. (1996). Trafficking of major histocompatibility complex class II molecules through intracellular compartments containing HLA-DM. Hum. Immunol. 45, 13-23.
    • (1996) Hum. Immunol. , vol.45 , pp. 13-23
    • Robbins, N.F.1    Hammond, C.2    Denzin, L.K.3    Pan, M.4    Cresswell, P.5
  • 61
    • 0030008358 scopus 로고    scopus 로고
    • Host cell invasion by trypanosomes requires lysosomes and microtubule/kinesin-mediated transport
    • Rodriguez, A., Samoff, K., Rioult, M. G., Chung, A. and Andrews, N. W. (1996). Host cell invasion by trypanosomes requires lysosomes and microtubule/kinesin-mediated transport. J. Cell Biol. 134, 349-362.
    • (1996) J. Cell Biol. , vol.134 , pp. 349-362
    • Rodriguez, A.1    Samoff, K.2    Rioult, M.G.3    Chung, A.4    Andrews, N.W.5
  • 62
    • 0030933293 scopus 로고    scopus 로고
    • Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro
    • Rogers, S. L., Tint, I. S., Fanapour, P. C. and Gelfand, V. I. (1997). Regulated bidirectional motility of melanophore pigment granules along microtubules in vitro. Proc. Natl. Acad. Sci. USA 94, 3720-3725.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3720-3725
    • Rogers, S.L.1    Tint, I.S.2    Fanapour, P.C.3    Gelfand, V.I.4
  • 63
    • 0028289244 scopus 로고
    • Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α
    • Sallusto, F. and Lanzavecchia, A. (1994). Efficient presentation of soluble antigen by cultured human dendritic cells is maintained by granulocyte/macrophage colony-stimulating factor plus interleukin 4 and downregulated by tumor necrosis factor α. J. Exp. Med. 179, 1109-1118.
    • (1994) J. Exp. Med. , vol.179 , pp. 1109-1118
    • Sallusto, F.1    Lanzavecchia, A.2
  • 65
    • 0030447498 scopus 로고    scopus 로고
    • Microtubule-associated proteins regulate microtubule function as the track for intracellular membrane organelle transports
    • Sato-Harada, R., Okabe, S., Umeyama, T., Kanai, Y. and Hirokawa, N. (1996). Microtubule-associated proteins regulate microtubule function as the track for intracellular membrane organelle transports. Cell Struct. Funct. 21, 283-295.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 283-295
    • Sato-Harada, R.1    Okabe, S.2    Umeyama, T.3    Kanai, Y.4    Hirokawa, N.5
  • 66
    • 0030744142 scopus 로고    scopus 로고
    • Kinesin hydrolyses one ATP per 8-nm step
    • Schnitzer, M. J. and Block, S. M. (1997). Kinesin hydrolyses one ATP per 8-nm step. Nature 388, 386-390.
    • (1997) Nature , vol.388 , pp. 386-390
    • Schnitzer, M.J.1    Block, S.M.2
  • 67
    • 0024604298 scopus 로고
    • Cytoplasmic dynein is a minus end-directed motor for membranous organelles
    • Schroer, T. A., Steuer, E. R. and Sheetz, M. P. (1989). Cytoplasmic dynein is a minus end-directed motor for membranous organelles. Cell 56, 937-946.
    • (1989) Cell , vol.56 , pp. 937-946
    • Schroer, T.A.1    Steuer, E.R.2    Sheetz, M.P.3
  • 68
    • 0024469867 scopus 로고
    • The invariant chain is a phosphorylated subunit of class II molecules
    • Spiro, R. C. and Quaranta, V. (1989). The invariant chain is a phosphorylated subunit of class II molecules. J. Immunol. 143, 2589-2594.
    • (1989) J. Immunol. , vol.143 , pp. 2589-2594
    • Spiro, R.C.1    Quaranta, V.2
  • 69
    • 0026786344 scopus 로고
    • Radial movement of lysosomes along microtubules in permeabilized macrophages
    • Swanson, J. A., Locke, A., Ansel, P. and Hollenbeck, P. J. (1992). Radial movement of lysosomes along microtubules in permeabilized macrophages. J. Cell Sci. 103, 201-209.
    • (1992) J. Cell Sci. , vol.103 , pp. 201-209
    • Swanson, J.A.1    Locke, A.2    Ansel, P.3    Hollenbeck, P.J.4
  • 70
    • 0026775359 scopus 로고
    • Kinectin, a major kinesin-binding protein on ER
    • Toyoshima, I., Yu, H., Steuer, E. R. and Sheetz, M. P. (1992). Kinectin, a major kinesin-binding protein on ER. J. Cell Biol. 118, 1121-1131.
    • (1992) J. Cell Biol. , vol.118 , pp. 1121-1131
    • Toyoshima, I.1    Yu, H.2    Steuer, E.R.3    Sheetz, M.P.4
  • 72
    • 0027070849 scopus 로고
    • Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins
    • Vale, R. D., Malik, F. and Brown, D. (1992). Directional instability of microtubule transport in the presence of kinesin and dynein, two opposite polarity motor proteins. J. Cell Biol. 119, 1589-1596.
    • (1992) J. Cell Biol. , vol.119 , pp. 1589-1596
    • Vale, R.D.1    Malik, F.2    Brown, D.3
  • 74
    • 0029932027 scopus 로고    scopus 로고
    • Targeting of motor proteins
    • Vallee, R. B. and Sheetz, M. P. (1996). Targeting of motor proteins. Science 271, 1539-1544.
    • (1996) Science , vol.271 , pp. 1539-1544
    • Vallee, R.B.1    Sheetz, M.P.2
  • 76
    • 0029563632 scopus 로고
    • Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued
    • Vaughan, K. T. and Vallee, R. B. (1995). Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued. J. Cell Biol. 131, 1507-1516.
    • (1995) J. Cell Biol. , vol.131 , pp. 1507-1516
    • Vaughan, K.T.1    Vallee, R.B.2
  • 77
    • 0021801145 scopus 로고
    • Biochemical characterization and cellular localization of a formalin-resistant melanoma-associated antigen reacting with monoclonal antibody NKI/C-3
    • Vennegoor, C., Calafat, J., Hageman, P., van Buitenen, F., Janssen, H., Kolk, A. and Rumke, P. (1985). Biochemical characterization and cellular localization of a formalin-resistant melanoma-associated antigen reacting with monoclonal antibody NKI/C-3. Int. J Cancer 35, 287-295.
    • (1985) Int. J Cancer , vol.35 , pp. 287-295
    • Vennegoor, C.1    Calafat, J.2    Hageman, P.3    Van Buitenen, F.4    Janssen, H.5    Kolk, A.6    Rumke, P.7
  • 78
    • 0028986631 scopus 로고
    • The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1)
    • Waterman-Storer, C. M., Karki, S. and Holzbaur, E. L. (1995). The p150Glued component of the dynactin complex binds to both microtubules and the actin-related protein centractin (Arp-1). Proc. Natl. Acad. Sci. USA 92, 1634-1638.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1634-1638
    • Waterman-Storer, C.M.1    Karki, S.2    Holzbaur, E.L.3
  • 79
    • 0030937833 scopus 로고    scopus 로고
    • Capture and processing of exogenous antigens for presentation on MHC molecules
    • Watts, C. (1997). Capture and processing of exogenous antigens for presentation on MHC molecules. Annu. Rev. Immunol. 15, 821-850.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 821-850
    • Watts, C.1
  • 81
    • 0029615496 scopus 로고    scopus 로고
    • How MHC class II molecules acquire peptide cargo: Biosynthesis and trafficking through the endocytic pathway
    • Wolf, P. R. and Ploegh, H. L. (1996). How MHC class II molecules acquire peptide cargo: biosynthesis and trafficking through the endocytic pathway. Ann. Rev. Cell Dev. Biol. 11, 267-306.
    • (1996) Ann. Rev. Cell Dev. Biol. , vol.11 , pp. 267-306
    • Wolf, P.R.1    Ploegh, H.L.2
  • 83
    • 0029015040 scopus 로고
    • Characterization of kinectin, a kinesin-binding protein: Primary sequence and N-terminal topogenic signal analysis
    • Yu, H., Nicchitta, C. V., Kumar, J., Becker, M., Toyoshima, I. and Sheetz, M. P. (1995). Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis. Mol. Biol. Cell 6, 171-183.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 171-183
    • Yu, H.1    Nicchitta, C.V.2    Kumar, J.3    Becker, M.4    Toyoshima, I.5    Sheetz, M.P.6
  • 84
    • 0027094238 scopus 로고
    • A block in degradation of MHC class II-associated invariant chain correlates with a reduction in transport from endosome carrier vesicles to the prelysosome compartment
    • Zachgo, S., Dobberstein, B. and Griffiths, G. (1992). A block in degradation of MHC class II-associated invariant chain correlates with a reduction in transport from endosome carrier vesicles to the prelysosome compartment. J. Cell Sci. 103, 811-822.
    • (1992) J. Cell Sci. , vol.103 , pp. 811-822
    • Zachgo, S.1    Dobberstein, B.2    Griffiths, G.3


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