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Volumn 15, Issue 2, 2004, Pages 481-496

The EF-Hand Ca2+-binding Protein p22 Plays a Role in Microtubule and Endoplasmic Reticulum Organization and Dynamics with Distinct Ca2+-binding Requirements

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; MUTANT PROTEIN; PROTEIN P22; CALCIUM BINDING PROTEIN P22, RAT; LIPOPROTEIN; RECOMBINANT PROTEIN;

EID: 0742288064     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-07-0500     Document Type: Article
Times cited : (41)

References (83)
  • 2
    • 0033552616 scopus 로고    scopus 로고
    • ER to Golgi transport: Requirement for p115 at a pre-Golgi VTC stage
    • Alvarez, C., Fujita, H., Hubbard, A., and Sztul, E. (1999). ER to Golgi transport: requirement for p115 at a pre-Golgi VTC stage. J. Cell Biol. 147, 1205-1222.
    • (1999) J. Cell Biol. , vol.147 , pp. 1205-1222
    • Alvarez, C.1    Fujita, H.2    Hubbard, A.3    Sztul, E.4
  • 4
    • 0035009245 scopus 로고    scopus 로고
    • Endocytic traffic in polarized epithelial cells: Role of the actin and microtubule cytoskeleton
    • Apodaca, G. (2001). Endocytic traffic in polarized epithelial cells: role of the actin and microtubule cytoskeleton. Traffic 2, 149-159.
    • (2001) Traffic , vol.2 , pp. 149-159
    • Apodaca, G.1
  • 5
    • 0036304655 scopus 로고    scopus 로고
    • Polarized calcium and calmodulin signaling in secretory epithelia
    • Ashby, M.C., and Tepikin, A.V. (2002). Polarized calcium and calmodulin signaling in secretory epithelia. Physiol. Rev. 82, 701-34.
    • (2002) Physiol. Rev. , vol.82 , pp. 701-734
    • Ashby, M.C.1    Tepikin, A.V.2
  • 6
    • 0028796834 scopus 로고
    • Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes
    • Barroso, M., Nelson, D.S., and Sztul, E. (1995). Transcytosis-associated protein (TAP)/p115 is a general fusion factor required for binding of vesicles to acceptor membranes. Proc. Natl. Acad. Sci. USA 92, 527-531.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 527-531
    • Barroso, M.1    Nelson, D.S.2    Sztul, E.3
  • 8
    • 0030467529 scopus 로고    scopus 로고
    • Molecular mechanisms in synaptic vesicle recycling
    • Bauerfeind, R., Galli, T., and De Camilli, P. (1996). Molecular mechanisms in synaptic vesicle recycling. J. Neurocytol. 25, 701-715.
    • (1996) J. Neurocytol. , vol.25 , pp. 701-715
    • Bauerfeind, R.1    Galli, T.2    De Camilli, P.3
  • 9
    • 0035038577 scopus 로고    scopus 로고
    • Endoplasmic reticulum of animal cells and its organization into structural and functional domains
    • Baumann, O., and Walz, B. (2001). Endoplasmic reticulum of animal cells and its organization into structural and functional domains. Int. Rev. Cytol. 205, 149-214.
    • (2001) Int. Rev. Cytol. , vol.205 , pp. 149-214
    • Baumann, O.1    Walz, B.2
  • 10
    • 0035156560 scopus 로고    scopus 로고
    • The neuronal calcium sensor family of Ca2+-binding proteins
    • Burgoyne, R.D., and Weiss, J.L. (2001). The neuronal calcium sensor family of Ca2+-binding proteins. Biochem. J. 353, 1-12.
    • (2001) Biochem. J. , vol.353 , pp. 1-12
    • Burgoyne, R.D.1    Weiss, J.L.2
  • 11
    • 0034826896 scopus 로고    scopus 로고
    • Regulation of microtubule-associated proteins
    • Cassimeris, L., and Spittle, C. (2001). Regulation of microtubule-associated proteins. Int. Rev. Cytol. 210, 163-226.
    • (2001) Int. Rev. Cytol. , vol.210 , pp. 163-226
    • Cassimeris, L.1    Spittle, C.2
  • 13
    • 0037144587 scopus 로고    scopus 로고
    • Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell
    • Chen, J.L., Ahluwalia, J.P., and Stamnes, M. (2002). Selective effects of calcium chelators on anterograde and retrograde protein transport in the cell. J. Biol. Chem. 277, 35682-35687.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35682-35687
    • Chen, J.L.1    Ahluwalia, J.P.2    Stamnes, M.3
  • 14
    • 0034610998 scopus 로고    scopus 로고
    • In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction
    • Dreier, L., and Rapoport, T.A. (2000). In vitro formation of the endoplasmic reticulum occurs independently of microtubules by a controlled fusion reaction. J. Cell Biol. 148, 883-898.
    • (2000) J. Cell Biol. , vol.148 , pp. 883-898
    • Dreier, L.1    Rapoport, T.A.2
  • 16
    • 0031664962 scopus 로고    scopus 로고
    • In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes
    • Fullerton, A.T., Bau, M.Y., Conrad, P.A., and Bloom, G.S. (1998). In vitro reconstitution of microtubule plus end-directed, GTPgammaS-sensitive motility of Golgi membranes. Mol. Biol. Cell 9, 2699-2714.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2699-2714
    • Fullerton, A.T.1    Bau, M.Y.2    Conrad, P.A.3    Bloom, G.S.4
  • 17
    • 0025612221 scopus 로고
    • Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral plasma membranes: Energy dependence and involvement of GTP-binding proteins
    • Gravotta, D., Adesnik, M., and Sabatini, D.D. (1990). Transport of influenza HA from the trans-Golgi network to the apical surface of MDCK cells permeabilized in their basolateral plasma membranes: energy dependence and involvement of GTP-binding proteins. J. Cell Biol. 111, 2893-2908.
    • (1990) J. Cell Biol. , vol.111 , pp. 2893-2908
    • Gravotta, D.1    Adesnik, M.2    Sabatini, D.D.3
  • 18
    • 0036468368 scopus 로고    scopus 로고
    • Rabs grab motors: Defining the connections between Rab GTPases and motor proteins
    • Hammer, J.A., 3rd, and Wu, X.S. (2002). Rabs grab motors: defining the connections between Rab GTPases and motor proteins. Curr. Opin. Cell Biol. 14, 69-75.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 69-75
    • Hammer III, J.A.1    Wu, X.S.2
  • 19
    • 0017840798 scopus 로고
    • Structure of cortical microtubule arrays in plant cells
    • Hardham, A.R., and Gunning, B.E. (1978). Structure of cortical microtubule arrays in plant cells. J. Cell Biol. 77, 14-34.
    • (1978) J. Cell Biol. , vol.77 , pp. 14-34
    • Hardham, A.R.1    Gunning, B.E.2
  • 20
    • 0029936185 scopus 로고    scopus 로고
    • Tubulin domains for the interaction of microtubule associated protein DMAP-85 from Drosophila melanogaster
    • Henriquez, J.P., Cambiazo, V., and Maccioni, R.B. (1996). Tubulin domains for the interaction of microtubule associated protein DMAP-85 from Drosophila melanogaster. Mol. Cell. Biochem. 158, 149-159.
    • (1996) Mol. Cell. Biochem. , vol.158 , pp. 149-159
    • Henriquez, J.P.1    Cambiazo, V.2    Maccioni, R.B.3
  • 22
    • 0037452096 scopus 로고    scopus 로고
    • Dynamics and mechanics of the microtubule plus end
    • Howard, J., and Hyman, A.A. (2003). Dynamics and mechanics of the microtubule plus end. Nature 422, 753-758.
    • (2003) Nature , vol.422 , pp. 753-758
    • Howard, J.1    Hyman, A.A.2
  • 23
    • 0030032040 scopus 로고    scopus 로고
    • Calcium binding and conformational response in EF-hand proteins
    • Ikura, M. (1996). Calcium binding and conformational response in EF-hand proteins. Trends Biochem. Sci. 21, 14-17.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 14-17
    • Ikura, M.1
  • 24
    • 0028791675 scopus 로고
    • The Brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores
    • Ivessa, N.E., De Lemos-Chiarandini, C., Gravotta, D., Sabatini, D.D., and Kreibich, G. (1995). The Brefeldin A-induced retrograde transport from the Golgi apparatus to the endoplasmic reticulum depends on calcium sequestered to intracellular stores. J. Biol. Chem. 270, 25960-7.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25960-25967
    • Ivessa, N.E.1    De Lemos-Chiarandini, C.2    Gravotta, D.3    Sabatini, D.D.4    Kreibich, G.5
  • 25
    • 0036558061 scopus 로고    scopus 로고
    • 2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: Interaction with actin, clathrin, and tubulin
    • 2+-dependent binding partners for the neuronal calcium sensor protein neurocalcin delta: interaction with actin, clathrin, and tubulin. Biochem. J. 1, 599-608.
    • (2002) Biochem. J. , vol.1 , pp. 599-608
    • Ivings, L.1    Pennington, S.R.2    Jenkins, R.3    Weiss, J.L.4    Burgoyne, R.D.5
  • 27
    • 0036171544 scopus 로고    scopus 로고
    • Motor-cargo interactions: The key to transport specificity
    • Karcher, R.L., Deacon, S.W., and Gelfand, V.I. (2002). Motor-cargo interactions: the key to transport specificity. Trends Cell Biol. 12, 21-27.
    • (2002) Trends Cell Biol. , vol.12 , pp. 21-27
    • Karcher, R.L.1    Deacon, S.W.2    Gelfand, V.I.3
  • 29
    • 0036678201 scopus 로고    scopus 로고
    • The microtubule-destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells
    • Kline-Smith, S.L., and Walczak, C.E. (2002). The microtubule-destabilizing kinesin XKCM1 regulates microtubule dynamic instability in cells. Mol. Biol. Cell 13, 2718-2731.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2718-2731
    • Kline-Smith, S.L.1    Walczak, C.E.2
  • 30
    • 0032476663 scopus 로고    scopus 로고
    • A novel direct interaction of endoplasmic reficulum with microtubules
    • Klopfenstein, D.R., Kappeler, F., and Hauri, H.P. (1998). A novel direct interaction of endoplasmic reficulum with microtubules. EMBO J. 17, 6168-6177.
    • (1998) EMBO J. , vol.17 , pp. 6168-6177
    • Klopfenstein, D.R.1    Kappeler, F.2    Hauri, H.P.3
  • 31
    • 0035844877 scopus 로고    scopus 로고
    • Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment
    • Klopfenstein, D.R., Klumperman, J., Lustig, A., Kammerer, R.A., Oorschot, V., and Hauri, H.P. (2001). Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment. J. Cell Biol. 153, 1287-1300.
    • (2001) J. Cell Biol. , vol.153 , pp. 1287-1300
    • Klopfenstein, D.R.1    Klumperman, J.2    Lustig, A.3    Kammerer, R.A.4    Oorschot, V.5    Hauri, H.P.6
  • 32
    • 0005126252 scopus 로고    scopus 로고
    • Mechanisms underlying the neuronal calcium sensor-1-evoked enhancement of exocytosis in PC12 cells
    • Koizumi, S., et al. (2002). Mechanisms underlying the neuronal calcium sensor-1-evoked enhancement of exocytosis in PC12 cells. J. Biol. Chem. 277, 30315-30324.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30315-30324
    • Koizumi, S.1
  • 34
    • 0033052099 scopus 로고    scopus 로고
    • Microtubule-based ER motility in Xenopus laevis: Activation of membrane-associated kinesin during development
    • Lane, J.D., and Allan, V.J. (1999). Microtubule-based ER motility in Xenopus laevis: activation of membrane-associated kinesin during development. Mol. Biol. Cell 10, 1909-1922.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1909-1922
    • Lane, J.D.1    Allan, V.J.2
  • 35
    • 0024456323 scopus 로고
    • Construction of the endoplasmic reticulum
    • Lee, C., Ferguson, M., and Chen, L.B. (1989). Construction of the endoplasmic reticulum. J. Cell Biol. 109, 2045-55.
    • (1989) J. Cell Biol. , vol.109 , pp. 2045-2055
    • Lee, C.1    Ferguson, M.2    Chen, L.B.3
  • 36
    • 0030598896 scopus 로고    scopus 로고
    • The neuronal EF-hand Ca(2+)-binding protein VILIP: Interaction with cell membrane and actin-based cytoskeleton
    • Lenz, S.E., Braunewell, K.H., Weise, C., Nedlina-Chittka, A., and Gundelfinger, E.D. (1996). The neuronal EF-hand Ca(2+)-binding protein VILIP: interaction with cell membrane and actin-based cytoskeleton. Biochem. Biophys. Res. Commun. 225, 1078-1083.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 1078-1083
    • Lenz, S.E.1    Braunewell, K.H.2    Weise, C.3    Nedlina-Chittka, A.4    Gundelfinger, E.D.5
  • 37
    • 0038709397 scopus 로고    scopus 로고
    • The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization
    • Ligon, L.A., Shelly, S.S., Tokito, M., and Holzbaur, E.L. (2003). The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization. Mol. Biol. Cell 14, 1405-1417.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1405-1417
    • Ligon, L.A.1    Shelly, S.S.2    Tokito, M.3    Holzbaur, E.L.4
  • 38
    • 0029981094 scopus 로고    scopus 로고
    • A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange
    • Lin, X., and Barber, D.L. (1996). A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange. Proc. Natl. Acad. Sci. USA 93, 12631-12636.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12631-12636
    • Lin, X.1    Barber, D.L.2
  • 39
    • 0033579413 scopus 로고    scopus 로고
    • Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein
    • Lin, X., Sikkink, R.A., Rusnak, F., and Barber, D.L. (1999). Inhibition of calcineurin phosphatase activity by a calcineurin B homologous protein. J. Biol. Chem. 274, 36125-36131.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36125-36131
    • Lin, X.1    Sikkink, R.A.2    Rusnak, F.3    Barber, D.L.4
  • 40
    • 0030921043 scopus 로고    scopus 로고
    • Sequence and overexpression of GPP130/GIMPc: Evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein
    • Linstedt, A.D., Mehta, A., Suhan, J., Reggio, H., and Hauri, H.P. (1997). Sequence and overexpression of GPP130/GIMPc: evidence for saturable pH-sensitive targeting of a type II early Golgi membrane protein. Mol. Biol. Cell 8, 1073-1087.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1073-1087
    • Linstedt, A.D.1    Mehta, A.2    Suhan, J.3    Reggio, H.4    Hauri, H.P.5
  • 41
    • 0035956989 scopus 로고    scopus 로고
    • Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography
    • Marsh, B.J., Mastronarde, D.N., Buttle, K.F., Howell, K.E., and McIntosh, J.R. (2001). Organellar relationships in the Golgi region of the pancreatic beta cell line, HIT-T15, visualized by high resolution electron tomography. Proc. Natl. Acad. Sci. USA 98, 2399-2406.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2399-2406
    • Marsh, B.J.1    Mastronarde, D.N.2    Buttle, K.F.3    Howell, K.E.4    McIntosh, J.R.5
  • 44
    • 0037199929 scopus 로고    scopus 로고
    • Rab4 function in membrane recycling from early endosomes depends on a membrane to cytoplasm cycle
    • Mohrmann, K., Gerez, L., Oorschot, V., Klumperman, J., and van der Sluijs, P. (2002). Rab4 function in membrane recycling from early endosomes depends on a membrane to cytoplasm cycle. J. Biol. Chem. 277, 32029-32035.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32029-32035
    • Mohrmann, K.1    Gerez, L.2    Oorschot, V.3    Klumperman, J.4    Van Der Sluijs, P.5
  • 45
    • 0037178876 scopus 로고    scopus 로고
    • NCS-1 inhibits insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes through a phosphatidylinositol 4-kinase-dependent pathway
    • Mora, S., Durham, P.L., Smith, J.R., Russo, A.F., Jeromin, A., and Pessin, J.E. (2002). NCS-1 inhibits insulin-stimulated GLUT4 translocation in 3T3L1 adipocytes through a phosphatidylinositol 4-kinase-dependent pathway. J. Biol. Chem. 277, 27494-27500.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27494-27500
    • Mora, S.1    Durham, P.L.2    Smith, J.R.3    Russo, A.F.4    Jeromin, A.5    Pessin, J.E.6
  • 47
    • 0032547807 scopus 로고    scopus 로고
    • The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function
    • Nelson, D.S., Alvarez, C., Gao, Y.S., Garcia-Mata, R., Fialkowski, E., and Sztul, E. (1998). The membrane transport factor TAP/p115 cycles between the Golgi and earlier secretory compartments and contains distinct domains required for its localization and function. J. Cell Biol. 143, 319-331.
    • (1998) J. Cell Biol. , vol.143 , pp. 319-331
    • Nelson, D.S.1    Alvarez, C.2    Gao, Y.S.3    Garcia-Mata, R.4    Fialkowski, E.5    Sztul, E.6
  • 53
    • 0037128212 scopus 로고    scopus 로고
    • CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
    • Perez, F., Pernet-Gallay, K., Nizak, C., Goodson, H.V., Kreis, T.E., and Goud, B. (2002). CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family. J. Cell Biol. 156, 631-642.
    • (2002) J. Cell Biol. , vol.156 , pp. 631-642
    • Perez, F.1    Pernet-Gallay, K.2    Nizak, C.3    Goodson, H.V.4    Kreis, T.E.5    Goud, B.6
  • 54
    • 0036843024 scopus 로고    scopus 로고
    • The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus
    • Pernet-Gallay, K., Antony, C., Johannes, L., Bornens, M., Goud, B., and Rios, R.M. (2002). The overexpression of GMAP-210 blocks anterograde and retrograde transport between the ER and the Golgi apparatus. Traffic 3, 822-832.
    • (2002) Traffic , vol.3 , pp. 822-832
    • Pernet-Gallay, K.1    Antony, C.2    Johannes, L.3    Bornens, M.4    Goud, B.5    Rios, R.M.6
  • 55
    • 0035252348 scopus 로고    scopus 로고
    • Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion
    • Peters, C., Bayer, M.J., Buhler, S., Andersen, J. S. Mann, M., and Mayer, A. (2001). Trans-complex formation by proteolipid channels in the terminal phase of membrane fusion. Nature 409, 581-588.
    • (2001) Nature , vol.409 , pp. 581-588
    • Peters, C.1    Bayer, M.J.2    Buhler, S.3    Andersen, J.S.4    Mann, M.5    Mayer, A.6
  • 57
    • 0028283041 scopus 로고
    • Molecular characterization of two functional domains of CLIP-170 in vivo
    • Pierre, P., Pepperkok, R., and Kreis, T.E. (1994). Molecular characterization of two functional domains of CLIP-170 in vivo. J. Cell Sci. 107, 1909-1920.
    • (1994) J. Cell Sci. , vol.107 , pp. 1909-1920
    • Pierre, P.1    Pepperkok, R.2    Kreis, T.E.3
  • 58
    • 0032530396 scopus 로고    scopus 로고
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum
    • 2+ store, with functional properties distinct from those of the endoplasmic reticulum. EMBO J. 17, 5298-5308.
    • (1998) EMBO J. , vol.17 , pp. 5298-5308
    • Pinton, P.1    Pozzan, T.2    Rizzuto, R.3
  • 59
    • 0034703092 scopus 로고    scopus 로고
    • Regulation of intra-Golgi membrane transport by calcium
    • Porat, A., and Elazar, Z. (2000). Regulation of intra-Golgi membrane transport by calcium. J. Biol. Chem. 275, 29233-29237.
    • (2000) J. Biol. Chem. , vol.275 , pp. 29233-29237
    • Porat, A.1    Elazar, Z.2
  • 60
    • 0034729167 scopus 로고    scopus 로고
    • 2+ in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles
    • 2+ in late endosome-lysosome heterotypic fusion and in the reformation of lysosomes from hybrid organelles. J. Cell Biol. 149, 1053-1062.
    • (2000) J. Cell Biol. , vol.149 , pp. 1053-1062
    • Pryor, P.R.1    Mullock, B.M.2    Bright, N.A.3    Gray, S.R.4    Luzio, J.P.5
  • 61
    • 0031661650 scopus 로고    scopus 로고
    • Cytoskeleton and mitochondrial morphology and function
    • Rappaport, L., Oliviero, P., and Samuel, J.L. (1998). Cytoskeleton and mitochondrial morphology and function. Mol. Cell Biochem. 184, 101-105.
    • (1998) Mol. Cell Biochem. , vol.184 , pp. 101-105
    • Rappaport, L.1    Oliviero, P.2    Samuel, J.L.3
  • 62
    • 0031610283 scopus 로고    scopus 로고
    • Magnetic bead assay for characterization of microtubule-membrane interactions
    • Scheel, J., and Kreis, T.E. (1998). Magnetic bead assay for characterization of microtubule-membrane interactions. Methods Enzymol. 298, 381-389.
    • (1998) Methods Enzymol. , vol.298 , pp. 381-389
    • Scheel, J.1    Kreis, T.E.2
  • 63
    • 0034799402 scopus 로고    scopus 로고
    • The structure of calnexin, an ER chaperone involved in quality control of protein folding
    • Schrag, J.D., Bergeron, J.J., Li, Y., Borisova, S., Hahn, M., Thomas, D.Y., and Cygler, M. (2001). The structure of calnexin, an ER chaperone involved in quality control of protein folding. Mol. Cell 8, 633-644.
    • (2001) Mol. Cell , vol.8 , pp. 633-644
    • Schrag, J.D.1    Bergeron, J.J.2    Li, Y.3    Borisova, S.4    Hahn, M.5    Thomas, D.Y.6    Cygler, M.7
  • 64
    • 0033525888 scopus 로고    scopus 로고
    • Identification of a domain in guanylyl cyclase-activating protein 1 that interacts with a complex of guanylyl cyclase and tubulin in photoreceptors
    • Schrem, A., Lange, C., Beyermann, M., and Koch, K.W. (1999). Identification of a domain in guanylyl cyclase-activating protein 1 that interacts with a complex of guanylyl cyclase and tubulin in photoreceptors. J. Biol. Chem. 274, 6244-6249.
    • (1999) J. Biol. Chem. , vol.274 , pp. 6244-6249
    • Schrem, A.1    Lange, C.2    Beyermann, M.3    Koch, K.W.4
  • 65
    • 0035906940 scopus 로고    scopus 로고
    • Microtubule "plus-end-tracking proteins": The end is just the beginning
    • Schuyler, S.C., and Pellman, D. (2001). Microtubule " plus-end-tracking proteins": The end is just the beginning. Cell 105, 421-424.
    • (2001) Cell , vol.105 , pp. 421-424
    • Schuyler, S.C.1    Pellman, D.2
  • 66
    • 0033525930 scopus 로고    scopus 로고
    • The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions
    • Sheff, D.R., Daro, E.A., Hull, M., and Mellman, I. (1999). The receptor recycling pathway contains two distinct populations of early endosomes with different sorting functions. J. Cell Biol. 145, 123-139.
    • (1999) J. Cell Biol. , vol.145 , pp. 123-139
    • Sheff, D.R.1    Daro, E.A.2    Hull, M.3    Mellman, I.4
  • 67
    • 0036758614 scopus 로고    scopus 로고
    • Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different membrane compartments in living hippocampal neurons
    • Spilker, C., Dresbach, T., and Braunewell, K.H. (2002a). Reversible translocation and activity-dependent localization of the calcium-myristoyl switch protein VILIP-1 to different membrane compartments in living hippocampal neurons. J. Neurosci. 22, 7331-7339.
    • (2002) J. Neurosci. , vol.22 , pp. 7331-7339
    • Spilker, C.1    Dresbach, T.2    Braunewell, K.H.3
  • 68
    • 0037020687 scopus 로고    scopus 로고
    • Evidence for different functional properties of the neuronal calcium sensor proteins VILIP-1 and VILIP-3, from subcellular localization to cellular function
    • Spilker, C., Gundelfinger, E.D., and Braunewell, K.H. (2002b). Evidence for different functional properties of the neuronal calcium sensor proteins VILIP-1 and VILIP-3, from subcellular localization to cellular function. Biochim. Biophys. Acta 1600, 118-127.
    • (2002) Biochim. Biophys. Acta , vol.1600 , pp. 118-127
    • Spilker, C.1    Gundelfinger, E.D.2    Braunewell, K.H.3
  • 69
    • 0031552376 scopus 로고    scopus 로고
    • Calcium- and myristoyl-dependent subcellular localization of the neuronal calcium-binding protein VILIP in transfected PC12 cells
    • Spilker, C., Gundelfinger, E.D., and Braunewell, K.H. (1997). Calcium- and myristoyl-dependent subcellular localization of the neuronal calcium-binding protein VILIP in transfected PC12 cells. Neurosci. Lett. 225, 126-128.
    • (1997) Neurosci. Lett. , vol.225 , pp. 126-128
    • Spilker, C.1    Gundelfinger, E.D.2    Braunewell, K.H.3
  • 70
    • 0033981121 scopus 로고    scopus 로고
    • The neuronal EF-hand calcium-binding protein visinin-like protein-3 is expressed in cerebellar Purkinje cells and shows a calcium-dependent membrane association
    • Spilker, C., Richter, K., Smalla, K.H., Manahan-Vaughan, D., Gundelfinger, E.D., and Braunewell, K.H. (2000). The neuronal EF-hand calcium-binding protein visinin-like protein-3 is expressed in cerebellar Purkinje cells and shows a calcium-dependent membrane association. Neuroscience 96, 121-9.
    • (2000) Neuroscience , vol.96 , pp. 121-129
    • Spilker, C.1    Richter, K.2    Smalla, K.H.3    Manahan-Vaughan, D.4    Gundelfinger, E.D.5    Braunewell, K.H.6
  • 71
    • 0035568345 scopus 로고    scopus 로고
    • Calcium, protease activation, and cytoskeleton remodeling underlie growth cone formation and neuronal regeneration
    • Spira, M.E., Oren, R., Dormann, A., Ilouz, N., and Lev, S. (2001). Calcium, protease activation, and cytoskeleton remodeling underlie growth cone formation and neuronal regeneration. Cell. Mol. Neurobiol. 21, 591-604.
    • (2001) Cell. Mol. Neurobiol. , vol.21 , pp. 591-604
    • Spira, M.E.1    Oren, R.2    Dormann, A.3    Ilouz, N.4    Lev, S.5
  • 72
    • 0029135419 scopus 로고
    • Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state
    • Tanaka, T., Ames, J.B., Harvey, T.S., Stryer, L., and Ikura, M. (1995). Sequestration of the membrane-targeting myristoyl group of recoverin in the calcium-free state. Nature 376, 444-447.
    • (1995) Nature , vol.376 , pp. 444-447
    • Tanaka, T.1    Ames, J.B.2    Harvey, T.S.3    Stryer, L.4    Ikura, M.5
  • 73
    • 0034103149 scopus 로고    scopus 로고
    • Dynamics of the endoplasmic reticulum and Golgi apparatus during early sea urchin development
    • Terasaki, M. (2000). Dynamics of the endoplasmic reticulum and Golgi apparatus during early sea urchin development. Mol. Biol. Cell 11, 897-914.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 897-914
    • Terasaki, M.1
  • 74
    • 0027987340 scopus 로고
    • Interactions among endoplasmic reticulum, microtubules, and retrograde movements of the cell surface
    • Terasaki, M., and Reese, T.S. (1994). Interactions among endoplasmic reticulum, microtubules, and retrograde movements of the cell surface. Cell Motil. Cytoskeleton 29, 291-300.
    • (1994) Cell Motil. Cytoskeleton , vol.29 , pp. 291-300
    • Terasaki, M.1    Reese, T.S.2
  • 75
    • 0023025842 scopus 로고
    • Microtubules and the endoplasmic reticulum are highly interdependent structures
    • Terasaki, M., Chen, L.B., and Fujiwara, K. (1986). Microtubules and the endoplasmic reticulum are highly interdependent structures. J. Cell Biol. 103, 1557-68.
    • (1986) J. Cell Biol. , vol.103 , pp. 1557-1568
    • Terasaki, M.1    Chen, L.B.2    Fujiwara, K.3
  • 76
    • 0033080404 scopus 로고    scopus 로고
    • Role of microtubules in the organization of the Golgi complex
    • Thyberg, J., and Moskalewski, S. (1999). Role of microtubules in the organization of the Golgi complex. Exp. Cell Res. 246, 263-279.
    • (1999) Exp. Cell Res. , vol.246 , pp. 263-279
    • Thyberg, J.1    Moskalewski, S.2
  • 77
    • 0032830852 scopus 로고    scopus 로고
    • 2+-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner
    • 2+-binding protein p22 associates with microtubules in an N-myristoylation-dependent manner. Mol. Biol. Cell 10, 3473-3488.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3473-3488
    • Timm, S.1    Titus, B.2    Bernd, K.3    Barroso, M.4
  • 78
    • 0037049466 scopus 로고    scopus 로고
    • VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo
    • Uchiyama, K., et al. (2002). VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo. J. Cell Biol. 159, 855-866.
    • (2002) J. Cell Biol. , vol.159 , pp. 855-866
    • Uchiyama, K.1
  • 80
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz, G.K., Rolls, M.M., and Rapoport, T.A. (2002). Structural organization of the endoplasmic reticulum. EMBO Rep. 3, 944-950.
    • (2002) EMBO Rep. , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 81
    • 0035809910 scopus 로고    scopus 로고
    • The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins
    • Walenta, J.H., Didier, A.J., Liu, X., and Kramer, H. (2001). The Golgi-associated hook3 protein is a member of a novel family of microtubule-binding proteins. J. Cell Biol. 152, 923-934.
    • (2001) J. Cell Biol. , vol.152 , pp. 923-934
    • Walenta, J.H.1    Didier, A.J.2    Liu, X.3    Kramer, H.4
  • 82
    • 0032474825 scopus 로고    scopus 로고
    • ER membrane tubules are distributed by microtubules in living cells using three distinct mechanisms
    • Waterman-Storer, C.M., and Salmon, E.D. (1998). ER membrane tubules are distributed by microtubules in living cells using three distinct mechanisms. Curr. Biol. 14, 798-806.
    • (1998) Curr. Biol. , vol.14 , pp. 798-806
    • Waterman-Storer, C.M.1    Salmon, E.D.2
  • 83
    • 0026468238 scopus 로고
    • Calcium-myristoyl protein switch
    • Zozulya, S., and Stryer, L. (1992). Calcium-myristoyl protein switch. Proc. Natl. Acad. Sci. USA 89, 11569-11573.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11569-11573
    • Zozulya, S.1    Stryer, L.2


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