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Volumn 121, Issue 20, 2008, Pages 3413-3421

Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport

Author keywords

CENPF; GLUT4; Rab11a; SNAP 25; Syntaxin 4; VAMP2

Indexed keywords

CENTROMERE PROTEIN F; GLUCOSE TRANSPORTER 4; NUCLEAR PROTEIN; SNARE PROTEIN; SYNTAXIN 4; UNCLASSIFIED DRUG;

EID: 56349135047     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.032847     Document Type: Article
Times cited : (20)

References (80)
  • 1
    • 31944441121 scopus 로고    scopus 로고
    • SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells
    • Aikawa, Y., Xia, X. and Martin, T. F. (2006). SNAP25, but not syntaxin 1A, recycles via an ARF6-regulated pathway in neuroendocrine cells. Mol. Biol. Cell 17, 711-722.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 711-722
    • Aikawa, Y.1    Xia, X.2    Martin, T.F.3
  • 3
    • 0347052864 scopus 로고    scopus 로고
    • LEK1 is a potential inhibitor of pocket protein-mediated cellular processes
    • Ashe, M., Pabon-Pena, L., Dees, E., Price, K. L. and Bader, D. (2004). LEK1 is a potential inhibitor of pocket protein-mediated cellular processes. J. Biol Chem. 279, 664-676.
    • (2004) J. Biol Chem , vol.279 , pp. 664-676
    • Ashe, M.1    Pabon-Pena, L.2    Dees, E.3    Price, K.L.4    Bader, D.5
  • 4
    • 29144521278 scopus 로고    scopus 로고
    • Promiscuous interaction of SNAP-25 with all plasma membrane syntaxins in a neuroendocrine cell
    • Bajohrs, M., Darios, F., Peak-Chew, S. Y. and Davletov, B. (2005). Promiscuous interaction of SNAP-25 with all plasma membrane syntaxins in a neuroendocrine cell. Biochem. J. 392, 283-289.
    • (2005) Biochem. J , vol.392 , pp. 283-289
    • Bajohrs, M.1    Darios, F.2    Peak-Chew, S.Y.3    Davletov, B.4
  • 5
    • 0037145811 scopus 로고    scopus 로고
    • Endogenous plasma membrane t-SNARE syntaxin 4 is present m rab11 positive endosomal membranes and associates with cortical actin cytoskeleton
    • Band, A. M., Ali, H., Vartiainen, M. K., Welti, S., Lappalainen, P., Olkkonen, V. M. and Kuismanen, E. (2002). Endogenous plasma membrane t-SNARE syntaxin 4 is present m rab11 positive endosomal membranes and associates with cortical actin cytoskeleton. FEBS Lett. 531, 513-519.
    • (2002) FEBS Lett , vol.531 , pp. 513-519
    • Band, A.M.1    Ali, H.2    Vartiainen, M.K.3    Welti, S.4    Lappalainen, P.5    Olkkonen, V.M.6    Kuismanen, E.7
  • 6
    • 0027997974 scopus 로고
    • Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains
    • Banfield, D. K., Lewis, M. J., Rabouille, C., Warren, G. and Pelham, H. R. (1994). Localization of Sed5, a putative vesicle targeting molecule, to the cis-Golgi network involves both its transmembrane and cytoplasmic domains. J. Cell Biol. 127, 357-371.
    • (1994) J. Cell Biol , vol.127 , pp. 357-371
    • Banfield, D.K.1    Lewis, M.J.2    Rabouille, C.3    Warren, G.4    Pelham, H.R.5
  • 7
    • 0035916323 scopus 로고    scopus 로고
    • Chromosome movement: Dynein-out at the kinetochore
    • Banks, J. D. and Heald, R. (2001). Chromosome movement: dynein-out at the kinetochore. Curr. Biol. 11, R128-R131.
    • (2001) Curr. Biol , vol.11
    • Banks, J.D.1    Heald, R.2
  • 8
    • 0036270751 scopus 로고    scopus 로고
    • Regulated transport of the glucose transporter GLUT4
    • Bryant, N. J., Govers, R. and James, D. E. (2002). Regulated transport of the glucose transporter GLUT4. Nat. Rev. Mol. Cell. Biol. 3, 267-277.
    • (2002) Nat. Rev. Mol. Cell. Biol , vol.3 , pp. 267-277
    • Bryant, N.J.1    Govers, R.2    James, D.E.3
  • 9
    • 0026780311 scopus 로고
    • Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes
    • Cain, C. C., Trimble, W. S. and Lienhard, G. E. (1992). Members of the VAMP family of synaptic vesicle proteins are components of glucose transporter-containing vesicles from rat adipocytes. J. Biol. Chem. 267, 11681-11684.
    • (1992) J. Biol. Chem , vol.267 , pp. 11681-11684
    • Cain, C.C.1    Trimble, W.S.2    Lienhard, G.E.3
  • 10
    • 33749015997 scopus 로고    scopus 로고
    • Microtubule motors at the intersection of trafficking and transport
    • Caviston, J. P. and Holzbaur, E. L. (2006). Microtubule motors at the intersection of trafficking and transport. Trends Cell Biol. 16, 530-537.
    • (2006) Trends Cell Biol , vol.16 , pp. 530-537
    • Caviston, J.P.1    Holzbaur, E.L.2
  • 12
    • 0031467820 scopus 로고    scopus 로고
    • Mitosin (a new proliferation marker) correlates with clinical outcome in node-negative breast cancer
    • Clark, G. M., Allred, D. C., Hilsenbeck, S. G., Chamness, G. C., Osborne, C. K., Jones, D. and Lee, W. H. (1997). Mitosin (a new proliferation marker) correlates with clinical outcome in node-negative breast cancer. Cancer Res. 57, 5505-5508.
    • (1997) Cancer Res , vol.57 , pp. 5505-5508
    • Clark, G.M.1    Allred, D.C.2    Hilsenbeck, S.G.3    Chamness, G.C.4    Osborne, C.K.5    Jones, D.6    Lee, W.H.7
  • 13
    • 0037459109 scopus 로고    scopus 로고
    • Centromeres and kinetochores: From epigenetics to mitotic checkpoint signaling
    • Cleveland, D. W., Mao, Y. and Sullivan, K. F.(2003). Centromeres and kinetochores: from epigenetics to mitotic checkpoint signaling. Cell 112, 407-421.
    • (2003) Cell , vol.112 , pp. 407-421
    • Cleveland, D.W.1    Mao, Y.2    Sullivan, K.F.3
  • 14
    • 0033774834 scopus 로고    scopus 로고
    • Characterization of CMF1 in avian skeletal muscle
    • Dees, E., Pabon-Pena, L M., Goodwin, R. L. and Bader, D. (2000). Characterization of CMF1 in avian skeletal muscle. Dev. Dyn. 219, 169-181.
    • (2000) Dev. Dyn , vol.219 , pp. 169-181
    • Dees, E.1    Pabon-Pena, L.M.2    Goodwin, R.L.3    Bader, D.4
  • 16
    • 33750466222 scopus 로고    scopus 로고
    • Microtubule: A common target for parkin and Parkinson's disease toxins
    • Feng, J. (2006). Microtubule: a common target for parkin and Parkinson's disease toxins. Neuroscientist 12, 469-476.
    • (2006) Neuroscientist , vol.12 , pp. 469-476
    • Feng, J.1
  • 17
    • 33745256260 scopus 로고    scopus 로고
    • CENP-F is a novel microtubule-binding protein that is essential for kinetochore attachments and affects the duration of the mitotic checkpoint delay
    • Feng, J., Huang, H. and Yen, T. J. (2006). CENP-F is a novel microtubule-binding protein that is essential for kinetochore attachments and affects the duration of the mitotic checkpoint delay. Chromosoma 115, 320-329.
    • (2006) Chromosoma , vol.115 , pp. 320-329
    • Feng, J.1    Huang, H.2    Yen, T.J.3
  • 18
    • 5144222593 scopus 로고    scopus 로고
    • Mitotic spindle regulation by Nde1 controls cerebral cortical size
    • Feng, Y. and Walsh, C. A. (2004). Mitotic spindle regulation by Nde1 controls cerebral cortical size. Neuron 44, 279-293.
    • (2004) Neuron , vol.44 , pp. 279-293
    • Feng, Y.1    Walsh, C.A.2
  • 19
    • 0034517593 scopus 로고    scopus 로고
    • LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome
    • Feng, Y., Olson, E. C., Stukenberg, P. T., Flanagan, L. A., Kirschner, M. W. and Walsh, C. A. (2000). LIS1 regulates CNS lamination by interacting with mNudE, a central component of the centrosome. Neuron 28, 665-679.
    • (2000) Neuron , vol.28 , pp. 665-679
    • Feng, Y.1    Olson, E.C.2    Stukenberg, P.T.3    Flanagan, L.A.4    Kirschner, M.W.5    Walsh, C.A.6
  • 20
    • 0033696020 scopus 로고    scopus 로고
    • Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells
    • Foster, L. J. and Klip, A. (2000). Mechanism and regulation of GLUT-4 vesicle fusion in muscle and fat cells. Am. J. Physiol. Cell Physiol. 279, C877-C890.
    • (2000) Am. J. Physiol. Cell Physiol , vol.279
    • Foster, L.J.1    Klip, A.2
  • 21
    • 33749385706 scopus 로고    scopus 로고
    • Primordial germ cell deficiency in the connexin 43 knockout mouse arises from apoptosis associated with abnormal p53 activation
    • Francis, R. J. and Lo, C. W. (2006). Primordial germ cell deficiency in the connexin 43 knockout mouse arises from apoptosis associated with abnormal p53 activation, Development 133, 3451-3460,
    • (2006) Development , vol.133 , pp. 3451-3460
    • Francis, R.J.1    Lo, C.W.2
  • 22
    • 0021997899 scopus 로고
    • Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes
    • Frost, S. C. and Lane, M. D. (1985). Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes. J. Biol. Chem. 260, 2646-2652.
    • (1985) J. Biol. Chem , vol.260 , pp. 2646-2652
    • Frost, S.C.1    Lane, M.D.2
  • 23
    • 0030460756 scopus 로고    scopus 로고
    • The role of dynein in microtubule-based motility
    • Gibbons, I. R. (1996). The role of dynein in microtubule-based motility. Cell Struct. Funct. 21, 331-342.
    • (1996) Cell Struct. Funct , vol.21 , pp. 331-342
    • Gibbons, I.R.1
  • 24
    • 0040737599 scopus 로고    scopus 로고
    • The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family
    • Goodwin, R. L., Pabon-Pena, L. M., Foster, G. C. and Bader, D. (1999). The cloning and analysis of LEK1 identifies variations in the LEK/centromere protein F/mitosin gene family. J. Biol. Chem. 274, 18597-18604.
    • (1999) J. Biol. Chem , vol.274 , pp. 18597-18604
    • Goodwin, R.L.1    Pabon-Pena, L.M.2    Foster, G.C.3    Bader, D.4
  • 25
    • 0033117833 scopus 로고    scopus 로고
    • Microtubule-based motor function in mitosis
    • Heald, R. and Walczak, C. E. (1999). Microtubule-based motor function in mitosis. Curr. Opin. Struct. Biol. 9, 268-274.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 268-274
    • Heald, R.1    Walczak, C.E.2
  • 26
    • 34248149386 scopus 로고    scopus 로고
    • Regulating cytoskeleton-based vesicle motility
    • Hehnly, H. and Stamnes, M. (2007). Regulating cytoskeleton-based vesicle motility. FEBS Lett. 581, 2112-2118.
    • (2007) FEBS Lett , vol.581 , pp. 2112-2118
    • Hehnly, H.1    Stamnes, M.2
  • 27
    • 0036714596 scopus 로고    scopus 로고
    • Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis
    • Hussein, D. and Taylor, S. S. (2002). Farnesylation of Cenp-F is required for G2/M progression and degradation after mitosis. J. Cell Sci. 115, 3403-3414.
    • (2002) J. Cell Sci , vol.115 , pp. 3403-3414
    • Hussein, D.1    Taylor, S.S.2
  • 28
    • 27844435600 scopus 로고    scopus 로고
    • Minireview: Recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners
    • Ishiki, M. and Klip, A. (2005). Minireview: recent developments in the regulation of glucose transporter-4 traffic: new signals, locations, and partners. Endocrinology 146, 5071-5078.
    • (2005) Endocrinology , vol.146 , pp. 5071-5078
    • Ishiki, M.1    Klip, A.2
  • 29
    • 23344431984 scopus 로고    scopus 로고
    • Insulin regulates the membrane arrival, fusion, and C-terminal unmasking of glucose transporter-4 via distinct phosphoinositides
    • Ishiki, M., Randhawa, V. K., Poon, V., Jebailey, L. and Klip, A. (2005). Insulin regulates the membrane arrival, fusion, and C-terminal unmasking of glucose transporter-4 via distinct phosphoinositides. J. Biol. Chem. 280, 28792-28802.
    • (2005) J. Biol. Chem , vol.280 , pp. 28792-28802
    • Ishiki, M.1    Randhawa, V.K.2    Poon, V.3    Jebailey, L.4    Klip, A.5
  • 30
    • 0029817806 scopus 로고    scopus 로고
    • Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2
    • Jagadish, M. N., Fernandez, C. S, Hewish, D. R., Macaulay, S. L, Gough, K. H., Grusovin, J., Verkuylen, A., Cosgrove, L., Alafaci, A., Frenkel, M. J. and Ward, C. W. (1996). Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2. Biochem. J. 317, 945-954.
    • (1996) Biochem. J , vol.317 , pp. 945-954
    • Jagadish, M.N.1    Fernandez, C.S.2    Hewish, D.R.3    Macaulay, S.L.4    Gough, K.H.5    Grusovin, J.6    Verkuylen, A.7    Cosgrove, L.8    Alafaci, A.9    Frenkel, M.J.10    Ward, C.W.11
  • 31
    • 0032836484 scopus 로고    scopus 로고
    • Membrane fusion and exocytosis
    • Jahn, R. and Sudhof, T. C. (1999). Membrane fusion and exocytosis. Annu. Rev. Biochem. 68, 863-911.
    • (1999) Annu. Rev. Biochem , vol.68 , pp. 863-911
    • Jahn, R.1    Sudhof, T.C.2
  • 32
    • 0034677749 scopus 로고    scopus 로고
    • Role of SNAP23 m insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2
    • Kawanishi, M., Tamori, Y., Okazawa, H., Araki, S., Shinoda, H. and Kasuga, M. (2000). Role of SNAP23 m insulin-induced translocation of GLUT4 in 3T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2. J. Biol. Chem. 275, 8240-8247.
    • (2000) J. Biol. Chem , vol.275 , pp. 8240-8247
    • Kawanishi, M.1    Tamori, Y.2    Okazawa, H.3    Araki, S.4    Shinoda, H.5    Kasuga, M.6
  • 33
    • 34748911230 scopus 로고    scopus 로고
    • Secretion of apolipoprotein E from macrophages occurs via a protein kinase A and calcium-dependent pathway along the microtubule network
    • Kockx, M., Guo, D. L, Huby, T., Lesnik, P., Kay, J., Sabaretnam, T., Jary, E., Hill, M., Gaus, K, Chapman, J. et al. (2007). Secretion of apolipoprotein E from macrophages occurs via a protein kinase A and calcium-dependent pathway along the microtubule network. Circ. Res. 101, 607-616.
    • (2007) Circ. Res , vol.101 , pp. 607-616
    • Kockx, M.1    Guo, D.L.2    Huby, T.3    Lesnik, P.4    Kay, J.5    Sabaretnam, T.6    Jary, E.7    Hill, M.8    Gaus, K.9    Chapman, J.10
  • 34
    • 26444562309 scopus 로고    scopus 로고
    • Kondratova, A. A, Neznanov, N., Kondratov, R. V. and Gudkov, A. V. (2005). Poliovirus protein 3A binds and inactivates LIS1, causing block of membrane protein trafficking and deregulation of cell division. Cell Cycle 4, 1403-1410.
    • Kondratova, A. A, Neznanov, N., Kondratov, R. V. and Gudkov, A. V. (2005). Poliovirus protein 3A binds and inactivates LIS1, causing block of membrane protein trafficking and deregulation of cell division. Cell Cycle 4, 1403-1410.
  • 36
    • 0036677449 scopus 로고    scopus 로고
    • Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells
    • Lauf, U., Giepmans, B. N., Lopez, P, Braconnot, S., Chen, S. C. and Falk, M. M. (2002). Dynamic trafficking and delivery of connexons to the plasma membrane and accretion to gap junctions in living cells. Proc. Natl. Acad. Sci. USA 99, 10446-10451.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10446-10451
    • Lauf, U.1    Giepmans, B.N.2    Lopez, P.3    Braconnot, S.4    Chen, S.C.5    Falk, M.M.6
  • 37
    • 1242285142 scopus 로고    scopus 로고
    • Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein
    • Liang, Y., Yu, W., Li, Y., Yang, Z., Yan, X., Huang, Q. and Zhu, X. (2004). Nudel functions in membrane traffic mainly through association with Lis1 and cytoplasmic dynein. J. Cell Biol. 164, 557-566.
    • (2004) J. Cell Biol , vol.164 , pp. 557-566
    • Liang, Y.1    Yu, W.2    Li, Y.3    Yang, Z.4    Yan, X.5    Huang, Q.6    Zhu, X.7
  • 38
    • 0029096822 scopus 로고
    • CENP-F is a protein of the nuclear matrix that assembles unto kinetochores at late G2 and is rapidly degraded after mitosis
    • Liao, H., Winkfein, R. J., Mack, G., Rattner, J. B. and Yen, T. J. (1995). CENP-F is a protein of the nuclear matrix that assembles unto kinetochores at late G2 and is rapidly degraded after mitosis. J. Cell Biol. 130, 507-518.
    • (1995) J. Cell Biol , vol.130 , pp. 507-518
    • Liao, H.1    Winkfein, R.J.2    Mack, G.3    Rattner, J.B.4    Yen, T.J.5
  • 39
    • 33645356427 scopus 로고    scopus 로고
    • Mitosin/CENP-F in mitosis, transcriptional control, and differentiation
    • Ma, L., Zhao, X. and Zhu, X. (2006). Mitosin/CENP-F in mitosis, transcriptional control, and differentiation. J. Biomed. Sci. 13, 205-213.
    • (2006) J. Biomed. Sci , vol.13 , pp. 205-213
    • Ma, L.1    Zhao, X.2    Zhu, X.3
  • 41
    • 0031891004 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes
    • Martin, L. B., Shewan, A., Millar, C. A., Gould, G. W. and James, D. E. (1998). Vesicle-associated membrane protein 2 plays a specific role in the insulin-dependent trafficking of the facilitative glucose transporter GLUT4 in 3T3-L1 adipocytes. J. Biol. Chem. 273, 1444-1452.
    • (1998) J. Biol. Chem , vol.273 , pp. 1444-1452
    • Martin, L.B.1    Shewan, A.2    Millar, C.A.3    Gould, G.W.4    James, D.E.5
  • 42
    • 0029741442 scopus 로고    scopus 로고
    • The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells
    • Martin, S., Tellam, J., Livingstone, C., Slot, J. W., Gould, G. W. and James, D. E. (1996). The glucose transporter (GLUT-4) and vesicle-associated membrane protein-2 (VAMP-2) are segregated from recycling endosomes in insulin-sensitive cells. J Cell Biol. 134, 625-635.
    • (1996) J Cell Biol , vol.134 , pp. 625-635
    • Martin, S.1    Tellam, J.2    Livingstone, C.3    Slot, J.W.4    Gould, G.W.5    James, D.E.6
  • 43
    • 0027265710 scopus 로고
    • Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein
    • McMahon, H. T., Ushkaryov, Y. A., Edelmann, L., Link, E., Binz, T., Niemann, H., Jahn, R. and Sudhof, T. C. (1993). Cellubrevin is a ubiquitous tetanus-toxin substrate homologous to a putative synaptic vesicle fusion protein. Nature 364, 346-349.
    • (1993) Nature , vol.364 , pp. 346-349
    • McMahon, H.T.1    Ushkaryov, Y.A.2    Edelmann, L.3    Link, E.4    Binz, T.5    Niemann, H.6    Jahn, R.7    Sudhof, T.C.8
  • 44
    • 33745890228 scopus 로고    scopus 로고
    • TrkB binds and tyrosine-phosphorylates Tiam1, leading to activation of Rac1 mad induction of changes in cellular morphology
    • Miyamato, Y., Yamauchi, J., Tanoue, A., Wu, C. and Mobley, W. C. (2006). TrkB binds and tyrosine-phosphorylates Tiam1, leading to activation of Rac1 mad induction of changes in cellular morphology. Proc. Natl. Acad. Sci. USA 103, 10444-10449.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10444-10449
    • Miyamato, Y.1    Yamauchi, J.2    Tanoue, A.3    Wu, C.4    Mobley, W.C.5
  • 45
    • 0028105461 scopus 로고
    • Functions of the Golgi complex in cell division: Formation of cell-matrix contacts and cell-cell communication channels in the terminal phase of cytokinesis
    • Moskalewski, S, Popowicz, P. and Thyberg, J. (1994). Functions of the Golgi complex in cell division: formation of cell-matrix contacts and cell-cell communication channels in the terminal phase of cytokinesis. J. Submicrosc. Cytol. Pathol. 26, 9-20.
    • (1994) J. Submicrosc. Cytol. Pathol , vol.26 , pp. 9-20
    • Moskalewski, S.1    Popowicz, P.2    Thyberg, J.3
  • 46
    • 0040949721 scopus 로고    scopus 로고
    • Analysis of CMF1 reveals a bone morphogenetic protein-independent component of the cardiomyogenic pathway
    • Pabon-Pena, L. M., Goodwin, R. L., Cise, L. J. and Bader, D. (2000). Analysis of CMF1 reveals a bone morphogenetic protein-independent component of the cardiomyogenic pathway. J. Biol. Chem. 275, 21453-21459.
    • (2000) J. Biol. Chem , vol.275 , pp. 21453-21459
    • Pabon-Pena, L.M.1    Goodwin, R.L.2    Cise, L.J.3    Bader, D.4
  • 47
    • 0033613830 scopus 로고    scopus 로고
    • Molecular basis of insulin-stimulated GLUT4 vesicle trafficking. Location! Location! Location!
    • Pessin, J. E., Thurmond, D. C., Elmendorf, J. S., Coker, K. J. and Okada, S. (1999). Molecular basis of insulin-stimulated GLUT4 vesicle trafficking. Location! Location! Location! J. Biol. Chem. 274, 2593-2596.
    • (1999) J. Biol. Chem , vol.274 , pp. 2593-2596
    • Pessin, J.E.1    Thurmond, D.C.2    Elmendorf, J.S.3    Coker, K.J.4    Okada, S.5
  • 49
    • 33745608087 scopus 로고    scopus 로고
    • CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25
    • Pooley, R. D., Reddy, S., Soukoulis, V., Roland, J. T., Goldenring, J. R. and Bader, D. M. (2006). CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25. Mol. Biol. Cell 17, 3176-3186.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3176-3186
    • Pooley, R.D.1    Reddy, S.2    Soukoulis, V.3    Roland, J.T.4    Goldenring, J.R.5    Bader, D.M.6
  • 50
    • 0345237979 scopus 로고    scopus 로고
    • Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations
    • Quinones, B., Riento, K., Olkkonen, V. M., Hardy, S. and Bennett, M. K. (1999). Syntaxin 2 splice variants exhibit differential expression patterns, biochemical properties and subcellular localizations. J. Cell Sci. 112, 4291-4304.
    • (1999) J. Cell Sci , vol.112 , pp. 4291-4304
    • Quinones, B.1    Riento, K.2    Olkkonen, V.M.3    Hardy, S.4    Bennett, M.K.5
  • 51
    • 0027436345 scopus 로고
    • CENP-F is a.ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization
    • Rattner, J. B., Rao, A., Fritzler, M. J., Valencia, D. W. and Yen, T. J. (1993). CENP-F is a.ca 400 kDa kinetochore protein that exhibits a cell-cycle dependent localization. Cell Motil. Cytoskeleton 26, 214-226.
    • (1993) Cell Motil. Cytoskeleton , vol.26 , pp. 214-226
    • Rattner, J.B.1    Rao, A.2    Fritzler, M.J.3    Valencia, D.W.4    Yen, T.J.5
  • 52
    • 0032146974 scopus 로고    scopus 로고
    • The vertebrate cell kinetochore and its roles during mitosis
    • Rieder, C. L. and Salmon, E. D. (1998). The vertebrate cell kinetochore and its roles during mitosis. Trends Cell Biol. 8, 310-318.
    • (1998) Trends Cell Biol , vol.8 , pp. 310-318
    • Rieder, C.L.1    Salmon, E.D.2
  • 53
    • 0032775945 scopus 로고    scopus 로고
    • Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: Prevention by rbSEC1
    • Rowe, J., Corradi, N., Malosio, M. L., Taverna, E., Halban, P., Meldolesi, J. and Rosa, P. (1999). Blockade of membrane transport and disassembly of the Golgi complex by expression of syntaxin 1A in neurosecretion-incompetent cells: prevention by rbSEC1. J. Cell Sci. 112 (Pt 12), 1865-1877.
    • (1999) J. Cell Sci , vol.112 , Issue.PART 12 , pp. 1865-1877
    • Rowe, J.1    Corradi, N.2    Malosio, M.L.3    Taverna, E.4    Halban, P.5    Meldolesi, J.6    Rosa, P.7
  • 56
    • 0037672688 scopus 로고    scopus 로고
    • Trafficking of signaling modules by kinesin motors
    • Schnapp, B. J. (2003). Trafficking of signaling modules by kinesin motors. J. Cell Sci. 116, 2125-2135.
    • (2003) J. Cell Sci , vol.116 , pp. 2125-2135
    • Schnapp, B.J.1
  • 57
    • 0034618565 scopus 로고    scopus 로고
    • Microtubule motors in mitosis
    • Sharp, D. J., Rogers, G. C. and Scholey, J. M. (2000). Microtubule motors in mitosis. Nature 407, 41-47.
    • (2000) Nature , vol.407 , pp. 41-47
    • Sharp, D.J.1    Rogers, G.C.2    Scholey, J.M.3
  • 59
    • 33845315084 scopus 로고    scopus 로고
    • Powering membrane traffic in endocytosis and recycling
    • Soldati, T. and Schliwa, M. (2006). Powering membrane traffic in endocytosis and recycling. Nat. Rev. Mol. Cell. Biol. 7, 897-908.
    • (2006) Nat. Rev. Mol. Cell. Biol , vol.7 , pp. 897-908
    • Soldati, T.1    Schliwa, M.2
  • 61
    • 20844434818 scopus 로고    scopus 로고
    • Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway
    • Soukoulis, V., Reddy, S., Pooley, R. D, Feng, Y., Walsh, C. A. and Bader, D. M. (2005). Cytoplasmic LEK1 is a regulator of microtubule function through its interaction with the LIS1 pathway. Proc. Natl. Acad. Sci. USA 102, 8549-8554.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 8549-8554
    • Soukoulis, V.1    Reddy, S.2    Pooley, R.D.3    Feng, Y.4    Walsh, C.A.5    Bader, D.M.6
  • 62
    • 0036854497 scopus 로고    scopus 로고
    • Trafficking of green fluorescent protein-tagged SNARE proteins in HSY cells
    • Takuma, T., Arakawa, T., Okayama, M., Mizoguchi, I., Tanimura, A. and Tajima, Y. (2002). Trafficking of green fluorescent protein-tagged SNARE proteins in HSY cells. J. Biochem. 132, 729-735.
    • (2002) J. Biochem , vol.132 , pp. 729-735
    • Takuma, T.1    Arakawa, T.2    Okayama, M.3    Mizoguchi, I.4    Tanimura, A.5    Tajima, Y.6
  • 63
    • 0029778167 scopus 로고    scopus 로고
    • Visualization of slow axonal transport in vivo
    • Terada, S., Nakata, T., Peterson, A. C. and Hirokawa, N. (1996). Visualization of slow axonal transport in vivo. Science 273, 784-788.
    • (1996) Science , vol.273 , pp. 784-788
    • Terada, S.1    Nakata, T.2    Peterson, A.C.3    Hirokawa, N.4
  • 64
    • 0032509214 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated GLUT4 translocation by Mune18c in 3T3L1 adipocytas
    • Thurmond, D. C., Ceresa, B. P., Okada, S., Elmendorf, J. S., Coker, K. and Pessin, J. E. (1998). Regulation of insulin-stimulated GLUT4 translocation by Mune18c in 3T3L1 adipocytas. J. Biol. Chem. 273, 33876-33883.
    • (1998) J. Biol. Chem , vol.273 , pp. 33876-33883
    • Thurmond, D.C.1    Ceresa, B.P.2    Okada, S.3    Elmendorf, J.S.4    Coker, K.5    Pessin, J.E.6
  • 65
    • 0036710325 scopus 로고    scopus 로고
    • C2C12 myocytes lack an insulin-responsive vesicular compartment despite dexamethasone-induced GLUT4 expression
    • Tortorella, L. L. and Pilch, P. F. (2002). C2C12 myocytes lack an insulin-responsive vesicular compartment despite dexamethasone-induced GLUT4 expression. Am. J. Physiol. Endocrinol. Metab. 283, E514-E524.
    • (2002) Am. J. Physiol. Endocrinol. Metab , vol.283
    • Tortorella, L.L.1    Pilch, P.F.2
  • 66
    • 33646409613 scopus 로고    scopus 로고
    • Morphogenesis of the endoplasmic reticulum: Beyond active membrane expansion
    • Vedrenne, C. and Hauri, H. P. (2006). Morphogenesis of the endoplasmic reticulum: beyond active membrane expansion. Traffic 7, 639-646.
    • (2006) Traffic , vol.7 , pp. 639-646
    • Vedrenne, C.1    Hauri, H.P.2
  • 67
    • 34250833558 scopus 로고    scopus 로고
    • Cenp-F links kinetochores to Ndell/Ndel/Lisl/dynein microtubule motor complexes
    • Vergnolle, M. A. and Taylor, S. S. (2007). Cenp-F links kinetochores to Ndell/Ndel/Lisl/dynein microtubule motor complexes. Curr Biol. 17, 1173-1179.
    • (2007) Curr Biol , vol.17 , pp. 1173-1179
    • Vergnolle, M.A.1    Taylor, S.S.2
  • 68
    • 0030055490 scopus 로고    scopus 로고
    • Syntaxin 4 in 3T3-L1 adipocytes: Regulation by insulin and participation in insulin-dependent glucose transport
    • Volchuk, A., Wang, Q., Ewart, H. S., Liu, Z., He, L., Bennett, M. K. and Klip, A. (1996). Syntaxin 4 in 3T3-L1 adipocytes: regulation by insulin and participation in insulin-dependent glucose transport. Mol. Biol. Cell 7, 1075-1082.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1075-1082
    • Volchuk, A.1    Wang, Q.2    Ewart, H.S.3    Liu, Z.4    He, L.5    Bennett, M.K.6    Klip, A.7
  • 69
    • 0035425203 scopus 로고    scopus 로고
    • Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting
    • Washbourne, P., Cansino, V., Mathews, J. R., Graham, M., Burgoyne, R. D. and Wilson, M. C. (2001). Cysteine residues of SNAP-25 are required for SNARE disassembly and exocytosis, but not for membrane targeting. Biochem. J. 357, 625-634.
    • (2001) Biochem. J , vol.357 , pp. 625-634
    • Washbourne, P.1    Cansino, V.2    Mathews, J.R.3    Graham, M.4    Burgoyne, R.D.5    Wilson, M.C.6
  • 70
    • 0034805876 scopus 로고    scopus 로고
    • Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5
    • Watson, R. T. and Pessin, J. E. (2001). Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5. Am. J. Physiol., Cell Physiol. 281, C215-C223.
    • (2001) Am. J. Physiol., Cell Physiol , vol.281
    • Watson, R.T.1    Pessin, J.E.2
  • 71
    • 8444245596 scopus 로고    scopus 로고
    • Connexins and cell signaling in development and disease
    • Wei, C. J., Xu, X. and Lo, C. W. (2004). Connexins and cell signaling in development and disease. Annu. Rev. Cell Dev. Biol. 20, 811-838.
    • (2004) Annu. Rev. Cell Dev. Biol , vol.20 , pp. 811-838
    • Wei, C.J.1    Xu, X.2    Lo, C.W.3
  • 72
    • 0034638828 scopus 로고    scopus 로고
    • Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network
    • Wilcke, M., Johannes, L., Galli, T, Mayau, V., Goud, B. and Salamero, J. (2000). Rab11 regulates the compartmentalization of early endosomes required for efficient transport from early endosomes to the trans-golgi network. J. Cell Biol. 151, 1207-1220.
    • (2000) J. Cell Biol , vol.151 , pp. 1207-1220
    • Wilcke, M.1    Johannes, L.2    Galli, T.3    Mayau, V.4    Goud, B.5    Salamero, J.6
  • 74
    • 0032782945 scopus 로고    scopus 로고
    • Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration
    • Xiang, X., Zuo, W., Efimov, V. P. and Morris, N. R. (1999). Isolation of a new set of Aspergillus nidulans mutants defective in nuclear migration. Curr. Genet. 35, 626-630.
    • (1999) Curr. Genet , vol.35 , pp. 626-630
    • Xiang, X.1    Zuo, W.2    Efimov, V.P.3    Morris, N.R.4
  • 75
    • 18144374884 scopus 로고    scopus 로고
    • Silencing mitosin induces misaligned chromosomes, premature chromosome decondensation before anaphase onset, and mitotic cell death
    • Yang, Z., Guo, J., Chen, Q., Ding, C., Do, J. and Zhu, X. (2005). Silencing mitosin induces misaligned chromosomes, premature chromosome decondensation before anaphase onset, and mitotic cell death. Mol. Cell. Biol. 25, 4062-4074.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 4062-4074
    • Yang, Z.1    Guo, J.2    Chen, Q.3    Ding, C.4    Do, J.5    Zhu, X.6
  • 76
    • 34548490482 scopus 로고    scopus 로고
    • H-Ras does not need COP I- or COP II-dependent vesicular transport to reach the plasma membrane
    • Zheng, H., McKay, J. and Buss, J. E. (2007). H-Ras does not need COP I- or COP II-dependent vesicular transport to reach the plasma membrane. J. Biol. Chem. 282, 25760-25768.
    • (2007) J. Biol. Chem , vol.282 , pp. 25760-25768
    • Zheng, H.1    McKay, J.2    Buss, J.E.3
  • 77
    • 17144390551 scopus 로고    scopus 로고
    • Mitosin/CENP-F as a negative regulator of activating transcription factor-4
    • Zhou, X., Wang, R., Fan, L, Li, Y., Ma, L., Yang, Z., Yu, W., Jing, N. and Zhu, X. (2005). Mitosin/CENP-F as a negative regulator of activating transcription factor-4. J. Biol. Chem. 280, 13973-13977.
    • (2005) J. Biol. Chem , vol.280 , pp. 13973-13977
    • Zhou, X.1    Wang, R.2    Fan, L.3    Li, Y.4    Ma, L.5    Yang, Z.6    Yu, W.7    Jing, N.8    Zhu, X.9
  • 78
    • 0029101199 scopus 로고
    • The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization
    • Zhu, X., Chang, K. H., He, D., Muncini, M. A., Brinkley, W. R. and Lee, W. H. (1995a). The C terminus of mitosin is essential for its nuclear localization, centromere/kinetochore targeting, and dimerization. J. Biol. Chem. 270, 19545-19550.
    • (1995) J. Biol. Chem , vol.270 , pp. 19545-19550
    • Zhu, X.1    Chang, K.H.2    He, D.3    Muncini, M.A.4    Brinkley, W.R.5    Lee, W.H.6
  • 79
    • 0029098787 scopus 로고
    • Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression
    • Zhu, X., Mancini, M. A., Chang, K. H., Liu, C. Y., Chen, C. F., Shan, B., Jones, D., Yung-Feng, T. L. and Lee, W. H. (1995b). Characterization of a novel 350-kilodalton nuclear phosphoprotein that is specifically involved in mitotic-phase progression. Mol. Cell. Biol. 15, 5017-5029.
    • (1995) Mol. Cell. Biol , vol.15 , pp. 5017-5029
    • Zhu, X.1    Mancini, M.A.2    Chang, K.H.3    Liu, C.Y.4    Chen, C.F.5    Shan, B.6    Jones, D.7    Yung-Feng, T.L.8    Lee, W.H.9
  • 80
    • 0030752107 scopus 로고    scopus 로고
    • Carboxyl terminus of mitosin is sufficient to confer spindle pole localization
    • Zhu, X., Ding, L. and Pei, G. (1997). Carboxyl terminus of mitosin is sufficient to confer spindle pole localization. J. Cell Biochem. 66, 441-449.
    • (1997) J. Cell Biochem , vol.66 , pp. 441-449
    • Zhu, X.1    Ding, L.2    Pei, G.3


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