메뉴 건너뛰기




Volumn 433, Issue 3, 2011, Pages 423-433

The multiple facets of the Golgi reassembly stacking proteins

Author keywords

cis Golgi membrane protein of 130 kDa (GM130); Functional organization; Golgi reassembly stacking protein (GRASP); Golgi ribbon; Golgi stack; Mitotic checkpoint; Mitotic phosphorylation PDZ; Trans oligomerization; Unconventional secretion

Indexed keywords

MEMBRANE PROTEIN; PROTEIN GRASP 55; PROTEIN GRASP 65; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 78751529769     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20101540     Document Type: Review
Times cited : (80)

References (88)
  • 1
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system
    • Rabouille, C., Misteli, T., Watson, R. and Warren, G. (1995) Reassembly of Golgi stacks from mitotic Golgi fragments in a cell-free system. J. Cell Biol. 129, 605-618
    • (1995) J. Cell Biol. , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 2
    • 0002471181 scopus 로고    scopus 로고
    • Three-dimensional structure of the Golgi apparatus in mammalian cells
    • (Berger, E. G. and Roth, J., eds), Birkhauser Verlag, Basel
    • Rambourg, A. and Clermont, Y. (1997) Three-dimensional structure of the Golgi apparatus in mammalian cells. In The Golgi Apparatus (Berger, E. G. and Roth, J., eds), pp. 37-61, Birkhauser Verlag, Basel
    • (1997) The Golgi Apparatus , pp. 37-61
    • Rambourg, A.1    Clermont, Y.2
  • 3
  • 4
    • 0042672956 scopus 로고    scopus 로고
    • A novel role for dp115 in the organization of tER sites in Drosophila
    • DOI 10.1083/jcb.200301136
    • Kondylis, V. and Rabouille, C. (2003) A novel role for dp115 in the organization of tER sites in Drosophila. J. Cell Biol. 162, 185-198 (Pubitemid 36928833)
    • (2003) Journal of Cell Biology , vol.162 , Issue.2 , pp. 185-198
    • Kondylis, V.1    Rabouille, C.2
  • 5
    • 70450223327 scopus 로고    scopus 로고
    • The Golgi apparatus: Lessons from Drosophila
    • Kondylis, V. and Rabouille, C. (2009) The Golgi apparatus: lessons from Drosophila. FEBS Lett. 583, 3827-3838
    • (2009) FEBS Lett. , vol.583 , pp. 3827-3838
    • Kondylis, V.1    Rabouille, C.2
  • 6
    • 77955260357 scopus 로고    scopus 로고
    • The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway
    • Levi, S. K., Bhattacharyya, D., Strack, R. L., Austin, II, J. R. and Glick, B. S. (2010) The yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway. Traffic 11, 1168-1179
    • (2010) Traffic , vol.11 , pp. 1168-1179
    • Levi, S.K.1    Bhattacharyya, D.2    Strack, R.L.3    Austin II, J.R.4    Glick, B.S.5
  • 7
    • 0027055402 scopus 로고
    • Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures
    • Cluett, E. B. and Brown, W. J. (1992) Adhesion of Golgi cisternae by proteinaceous interactions: intercisternal bridges as putative adhesive structures. J. Cell Sci. 103, 773-784
    • (1992) J. Cell Sci. , vol.103 , pp. 773-784
    • Cluett, E.B.1    Brown, W.J.2
  • 10
    • 0027183419 scopus 로고
    • Membrane partitioning during cell division
    • Warren, G. (1993) Membrane partitioning during cell division. Annu. Rev. Biochem. 62, 323-348
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 323-348
    • Warren, G.1
  • 11
    • 0037926843 scopus 로고    scopus 로고
    • Golgi apparatus partitioning during cell division
    • Rabouille, C. and Jokitalo, E. (2003) Golgi apparatus partitioning during cell division. Mol. Membr. Biol. 20, 117-127
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 117-127
    • Rabouille, C.1    Jokitalo, E.2
  • 12
    • 0028327124 scopus 로고
    • COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system
    • Misteli, T. and Warren, G. (1994) COP-coated vesicles are involved in the mitotic fragmentation of Golgi stacks in a cell-free system. J. Cell Biol. 125, 269-282 (Pubitemid 24135942)
    • (1994) Journal of Cell Biology , vol.125 , Issue.2 , pp. 269-282
    • Misteli, T.1    Warren, G.2
  • 13
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • DOI 10.1016/S0092-8674(00)80407-9
    • Barr, F. A., Puype, M., Vandekerckhove, J. and Warren, G. (1997) GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91, 253-262 (Pubitemid 27456392)
    • (1997) Cell , vol.91 , Issue.2 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 14
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter, J., Watson, R., Giannakou, M. E., Clarke, M., Warren, G. and Barr, F. A. (1999) GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18, 4949-4960
    • (1999) EMBO J. , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 15
    • 0037439823 scopus 로고    scopus 로고
    • An integrated physical and gene map of the 3.5-Mb chromosome 3p21.3 (AP20) region implicated in major human epithelial malignancies
    • Protopopov, A., Kashuba, V., Zabarovska, V. I., Muravenko, O. V., Lerman, M. I., Klein, G. and Zabarovsky, E. R. (2003) An integrated physical and gene map of the 3.5-Mb chromosome 3p21.3 (AP20) region implicated in major human epithelial malignancies. Cancer Res. 63, 404-412
    • (2003) Cancer Res. , vol.63 , pp. 404-412
    • Protopopov, A.1    Kashuba, V.2    Zabarovska, V.I.3    Muravenko, O.V.4    Lerman, M.I.5    Klein, G.6    Zabarovsky, E.R.7
  • 16
    • 0033549551 scopus 로고    scopus 로고
    • A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system
    • Shorter, J. and Warren, G. (1999) A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J. Cell Biol. 146, 57-70
    • (1999) J. Cell Biol. , vol.146 , pp. 57-70
    • Shorter, J.1    Warren, G.2
  • 17
    • 34547604776 scopus 로고    scopus 로고
    • The Golgi-Associated Protein GRASP Is Required for Unconventional Protein Secretion during Development
    • DOI 10.1016/j.cell.2007.06.029, PII S0092867407008264
    • Kinseth, M. A., Anjard, C., Fuller, D., Guizzunti, G., Loomis, W. F. and Malhotra, V. (2007) The Golgi-associated protein GRASP is required for unconventional protein secretion during development. Cell 130, 524-534 (Pubitemid 47198303)
    • (2007) Cell , vol.130 , Issue.3 , pp. 524-534
    • Kinseth, M.A.1    Anjard, C.2    Fuller, D.3    Guizzunti, G.4    Loomis, W.F.5    Malhotra, V.6
  • 19
    • 48049090703 scopus 로고    scopus 로고
    • Plasmodium falciparumpossesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism
    • Struck, N. S., Herrmann, S., Langer, C., Krueger, A., Foth, B. J., Engelberg, K., Cabrera, A. L., Haase, S., Treeck, M., Marti, M. et al. (2008) Plasmodium falciparumpossesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism. J. Cell Sci. 121, 2123-2129
    • (2008) J. Cell Sci. , vol.121 , pp. 2123-2129
    • Struck, N.S.1    Herrmann, S.2    Langer, C.3    Krueger, A.4    Foth, B.J.5    Engelberg, K.6    Cabrera, A.L.7    Haase, S.8    Treeck, M.9    Marti, M.10
  • 20
    • 24344453350 scopus 로고    scopus 로고
    • dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells
    • Kondylis, V., Spoorendonk, K. M. and Rabouille, C. (2005) dGRASP localization and function in the early exocytic pathway in Drosophila S2 cells. Mol. Biol. Cell 16, 4061-4072
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4061-4072
    • Kondylis, V.1    Spoorendonk, K.M.2    Rabouille, C.3
  • 21
    • 59849096584 scopus 로고    scopus 로고
    • Ultrastructural study of Golgi duplication in Trypanosoma brucei
    • Yelinek, J. T., He, C. Y. and Warren, G. (2009) Ultrastructural study of Golgi duplication in Trypanosoma brucei. Traffic 10, 300-306
    • (2009) Traffic , vol.10 , pp. 300-306
    • Yelinek, J.T.1    He, C.Y.2    Warren, G.3
  • 23
    • 33846590554 scopus 로고    scopus 로고
    • The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic
    • DOI 10.1083/jcb.200607151
    • Behnia, R., Barr, F. A., Flanagan, J. J., Barlowe, C. and Munro, S. (2007) The yeast orthologue of GRASP65 forms a complex with a coiled-coil protein that contributes to ER to Golgi traffic. J. Cell Biol. 176, 255-261 (Pubitemid 46184876)
    • (2007) Journal of Cell Biology , vol.176 , Issue.3 , pp. 255-261
    • Behnia, R.1    Barr, F.A.2    Flanagan, J.J.3    Barlowe, C.4    Munro, S.5
  • 26
    • 14244259922 scopus 로고    scopus 로고
    • Mapping the functional domains of the Golgi stacking factor GRASP65
    • Wang, Y., Satoh, A. and Warren, G. (2005) Mapping the functional domains of the Golgi stacking factor GRASP65. J. Biol. Chem. 280, 4921-4928
    • (2005) J. Biol. Chem. , vol.280 , pp. 4921-4928
    • Wang, Y.1    Satoh, A.2    Warren, G.3
  • 27
    • 70349335825 scopus 로고    scopus 로고
    • Golgins and GRASPs: Holding the Golgi together
    • Ramirez, I. B. and Lowe, M. (2009) Golgins and GRASPs: holding the Golgi together. Semin. Cell Dev. Biol. 20, 770-779
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 770-779
    • Ramirez, I.B.1    Lowe, M.2
  • 28
    • 0032526720 scopus 로고    scopus 로고
    • Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae
    • DOI 10.1093/emboj/17.12.3258
    • Barr, F. A., Nakamura, N. and Warren, G. (1998) Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J. 17, 3258-3268 (Pubitemid 28279500)
    • (1998) EMBO Journal , vol.17 , Issue.12 , pp. 3258-3268
    • Barr, F.A.1    Nakamura, N.2    Warren, G.3
  • 29
    • 21844468961 scopus 로고    scopus 로고
    • The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division
    • Sutterlin, C., Polishchuk, R., Pecot, M. and Malhotra, V. (2005) The Golgi-associated protein GRASP65 regulates spindle dynamics and is essential for cell division. Mol. Biol. Cell 16, 3211-3222
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3211-3222
    • Sutterlin, C.1    Polishchuk, R.2    Pecot, M.3    Malhotra, V.4
  • 30
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • Puthenveedu, M. A., Bachert, C., Puri, S., Lanni, F. and Linstedt, A. D. (2006) GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat. Cell Biol. 8, 238-248
    • (2006) Nat. Cell Biol. , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 31
    • 76149083892 scopus 로고    scopus 로고
    • GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
    • Xiang, Y. and Wang, Y. (2010) GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking. J. Cell Biol. 188, 237-251
    • (2010) J. Cell Biol. , vol.188 , pp. 237-251
    • Xiang, Y.1    Wang, Y.2
  • 32
    • 0035842903 scopus 로고    scopus 로고
    • A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
    • Short, B., Preisinger, C., Korner, R., Kopajtich, R., Byron, O. and Barr, F. A. (2001) A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic. J. Cell Biol. 155, 877-883
    • (2001) J. Cell Biol. , vol.155 , pp. 877-883
    • Short, B.1    Preisinger, C.2    Korner, R.3    Kopajtich, R.4    Byron, O.5    Barr, F.A.6
  • 33
    • 0037926394 scopus 로고    scopus 로고
    • A direct role for GRASP65 as a mitotically regulated Golgi stacking factor
    • DOI 10.1093/emboj/cdg317
    • Wang, Y., Seemann, J., Pypaert, M., Shorter, J. and Warren, G. (2003) A direct role for GRASP65 as a mitotically regulated Golgi stacking factor. EMBO J. 22, 3279-3290 (Pubitemid 36834858)
    • (2003) EMBO Journal , vol.22 , Issue.13 , pp. 3279-3290
    • Wang, Y.1    Seemann, J.2    Pypaert, M.3    Shorter, J.4    Warren, G.5
  • 34
    • 67650475442 scopus 로고    scopus 로고
    • Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network
    • Sengupta, D., Truschel, S., Bachert, C. and Linstedt, A. D. (2009) Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network. J. Cell Biol. 186, 41-55
    • (2009) J. Cell Biol. , vol.186 , pp. 41-55
    • Sengupta, D.1    Truschel, S.2    Bachert, C.3    Linstedt, A.D.4
  • 35
    • 77952417354 scopus 로고    scopus 로고
    • Dual anchoring of the GRASP membrane tether promotes trans pairing
    • Bachert, C. and Linstedt, A. D. (2010) Dual anchoring of the GRASP membrane tether promotes trans pairing. J. Biol. Chem. 285, 16294-16301
    • (2010) J. Biol. Chem. , vol.285 , pp. 16294-16301
    • Bachert, C.1    Linstedt, A.D.2
  • 36
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • Kay, B. K., Williamson, M. P. and Sudol, M. (2000) The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains. FASEB J. 14, 231-241
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 37
    • 45749158566 scopus 로고    scopus 로고
    • Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport
    • DOI 10.1371/journal.pone.0001647
    • Wang, Y., Wei, J. H., Bisel, B., Tang, D. and Seemann, J. (2008) Golgi cisternal unstacking stimulates COPI vesicle budding and protein transport. PLoS One 3, e1647 (Pubitemid 351865460)
    • (2008) PLoS ONE , vol.3 , Issue.2
    • Wang, Y.1    Wei, J.-H.2    Bisel, B.3    Tang, D.4    Seemann, J.5
  • 39
    • 51349095514 scopus 로고    scopus 로고
    • GRASP55 regulates Golgi ribbon formation
    • Feinstein, T. N. and Linstedt, A. D. (2008) GRASP55 regulates Golgi ribbon formation. Mol. Biol. Cell 19, 2696-2707
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2696-2707
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 40
    • 38849095347 scopus 로고    scopus 로고
    • DGRASP-Mediated Noncanonical Integrin Secretion Is Required for Drosophila Epithelial Remodeling
    • DOI 10.1016/j.devcel.2007.12.006, PII S1534580707004832
    • Schotman, H., Karhinen, L. and Rabouille, C. (2008) dGRASP-mediated noncanonical integrin secretion is required for Drosophila epithelial remodeling. Dev. Cell 14, 171-182 (Pubitemid 351189181)
    • (2008) Developmental Cell , vol.14 , Issue.2 , pp. 171-182
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3
  • 41
    • 0035842897 scopus 로고    scopus 로고
    • Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus
    • DOI 10.1083/jcb.200108102
    • Barr, F. A., Preisinger, C., Kopajtich, R. and Korner, R. (2001) Golgi matrix proteins interact with p24 cargo receptors and aid their efficient retention in the Golgi apparatus. J. Cell Biol. 155, 885-891 (Pubitemid 34286240)
    • (2001) Journal of Cell Biology , vol.155 , Issue.6 , pp. 885-891
    • Barr, F.A.1    Preisinger, C.2    Kopajtich, R.3    Korner, R.4
  • 42
    • 77953470242 scopus 로고    scopus 로고
    • The role of GRASP65 in Golgi cisternal stacking and cell cycle progression
    • Tang, D., Yuan, H. and Wang, Y. (2010) The role of GRASP65 in Golgi cisternal stacking and cell cycle progression. Traffic 11, 827-842
    • (2010) Traffic , vol.11 , pp. 827-842
    • Tang, D.1    Yuan, H.2    Wang, Y.3
  • 43
    • 78650062474 scopus 로고    scopus 로고
    • Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligand
    • doi:10. 1074/jbc.M110.189449
    • Sengupta, D. and Linstedt, A. D. (2010) Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligand. J. Biol. Chem. doi:10. 1074/jbc.M110.189449
    • (2010) J. Biol. Chem.
    • Sengupta, D.1    Linstedt, A.D.2
  • 44
    • 0033740931 scopus 로고    scopus 로고
    • Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2
    • Lin, C. Y., Madsen, M. L., Yarm, F. R., Jang, Y. J., Liu, X. and Erikson, R. L. (2000) Peripheral Golgi protein GRASP65 is a target of mitotic polo-like kinase (Plk) and Cdc2. Proc. Natl. Acad. Sci. U.S.A. 97, 12589-12594
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12589-12594
    • Lin, C.Y.1    Madsen, M.L.2    Yarm, F.R.3    Jang, Y.J.4    Liu, X.5    Erikson, R.L.6
  • 45
    • 15444380728 scopus 로고    scopus 로고
    • Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling
    • Preisinger, C., Korner, R., Wind, M., Lehmann, W. D., Kopajtich, R. and Barr, F. A. (2005) Plk1 docking to GRASP65 phosphorylated by Cdk1 suggests a mechanism for Golgi checkpoint signalling. EMBO J. 24, 753-765
    • (2005) EMBO J. , vol.24 , pp. 753-765
    • Preisinger, C.1    Korner, R.2    Wind, M.3    Lehmann, W.D.4    Kopajtich, R.5    Barr, F.A.6
  • 48
    • 0035167603 scopus 로고    scopus 로고
    • Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2
    • Jesch, S. A., Lewis, T. S., Ahn, N. G. and Linstedt, A. D. (2001) Mitotic phosphorylation of Golgi reassembly stacking protein 55 by mitogen-activated protein kinase ERK2. Mol. Biol. Cell 12, 1811-1817
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1811-1817
    • Jesch, S.A.1    Lewis, T.S.2    Ahn, N.G.3    Linstedt, A.D.4
  • 49
    • 33644878839 scopus 로고    scopus 로고
    • ERK1c regulates Golgi fragmentation during mitosis
    • Shaul, Y. D. and Seger, R. (2006) ERK1c regulates Golgi fragmentation during mitosis. J. Cell Biol. 172, 885-897
    • (2006) J. Cell Biol. , vol.172 , pp. 885-897
    • Shaul, Y.D.1    Seger, R.2
  • 51
    • 37249078584 scopus 로고    scopus 로고
    • 2/M checkpoint
    • Rabouille, C. and Kondylis, V. (2007) Golgi ribbon unlinking: an organelle-based G2/M checkpoint. Cell Cycle 6, 2723-2729 (Pubitemid 350277161)
    • (2007) Cell Cycle , vol.6 , Issue.22 , pp. 2723-2729
    • Rabouille, C.1    Kondylis, V.2
  • 53
    • 0037013167 scopus 로고    scopus 로고
    • Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells
    • DOI 10.1016/S0092-8674(02)00720-1
    • Sutterlin, C., Hsu, P., Mallabiabarrena, A. and Malhotra, V. (2002) Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells. Cell 109, 359-369 (Pubitemid 34606878)
    • (2002) Cell , vol.109 , Issue.3 , pp. 359-369
    • Sutterlin, C.1    Hsu, P.2    Mallabiabarrena, A.3    Malhotra, V.4
  • 54
    • 33846813500 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase kinase 1-dependent Golgi unlinking occurs in G2 phase and promotes the G2/M cell cycle transition
    • Feinstein, T. N. and Linstedt, A. D. (2007) Mitogen-activated protein kinase kinase 1-dependent Golgi unlinking occurs in G2 phase and promotes the G2/M cell cycle transition. Mol. Biol. Cell 18, 594-604
    • (2007) Mol. Biol. Cell , vol.18 , pp. 594-604
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 56
    • 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
  • 58
    • 0026760941 scopus 로고
    • Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex
    • Corthesy-Theulaz, I., Pauloin, A. and Pfeffer, S. R. (1992) Cytoplasmic dynein participates in the centrosomal localization of the Golgi complex. J. Cell Biol. 118, 1333-1345
    • (1992) J. Cell Biol. , vol.118 , pp. 1333-1345
    • Corthesy-Theulaz, I.1    Pauloin, A.2    Pfeffer, S.R.3
  • 59
    • 0029972823 scopus 로고    scopus 로고
    • Golgi dispersal during microtubule disruption: Regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites
    • Cole, N. B., Sciaky, N., Marotta, A., Song, J. and Lippincott-Schwartz, J. (1996) Golgi dispersal during microtubule disruption: regeneration of Golgi stacks at peripheral endoplasmic reticulum exit sites. Mol. Biol. Cell 7, 631-650
    • (1996) Mol. Biol. Cell , vol.7 , pp. 631-650
    • Cole, N.B.1    Sciaky, N.2    Marotta, A.3    Song, J.4    Lippincott-Schwartz, J.5
  • 60
    • 69949178740 scopus 로고    scopus 로고
    • Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells
    • Miller, P. M., Folkmann, A. W., Maia, A. R., Efimova, N., Efimov, A. and Kaverina, I. (2009) Golgi-derived CLASP-dependent microtubules control Golgi organization and polarized trafficking in motile cells. Nat. Cell Biol. 11, 1069-1080
    • (2009) Nat. Cell Biol. , vol.11 , pp. 1069-1080
    • Miller, P.M.1    Folkmann, A.W.2    Maia, A.R.3    Efimova, N.4    Efimov, A.5    Kaverina, I.6
  • 61
    • 77949375577 scopus 로고    scopus 로고
    • The Golgi and the centrosome: Building a functional partnership
    • Sutterlin, C. and Colanzi, A. (2010) The Golgi and the centrosome: building a functional partnership. J. Cell Biol. 188, 621-628
    • (2010) J. Cell Biol. , vol.188 , pp. 621-628
    • Sutterlin, C.1    Colanzi, A.2
  • 62
    • 77951273067 scopus 로고    scopus 로고
    • Spindle-dependent partitioning of the Golgi ribbon
    • Wei, J. H. and Seemann, J. (2009) Spindle-dependent partitioning of the Golgi ribbon. Commun. Integr. Biol. 2, 406-407
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 406-407
    • Wei, J.H.1    Seemann, J.2
  • 63
    • 39449124362 scopus 로고    scopus 로고
    • The Golgi protein GM130 regulates centrosome morphology and function
    • Kodani, A. and Sutterlin, C. (2008) The Golgi protein GM130 regulates centrosome morphology and function. Mol. Biol. Cell 19, 745-753
    • (2008) Mol. Biol. Cell , vol.19 , pp. 745-753
    • Kodani, A.1    Sutterlin, C.2
  • 65
    • 0042266400 scopus 로고    scopus 로고
    • Death from within: Apoptosis and the secretory pathway
    • Maag, R. S., Hicks, S. W. and Machamer, C E. (2003) Death from within: apoptosis and the secretory pathway. Curr. Opin. Cell Biol. 15, 456-461
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 456-461
    • Maag, R.S.1    Hicks, S.W.2    Machamer, C.E.3
  • 66
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner, M. O. (2000) The biochemistry of apoptosis. Nature 407, 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 68
    • 0037175389 scopus 로고    scopus 로고
    • A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis
    • Chiu, R., Novikov, L., Mukherjee, S. and Shields, D. (2002) A caspase cleavage fragment of p115 induces fragmentation of the Golgi apparatus and apoptosis. J. Cell Biol. 159, 637-648
    • (2002) J. Cell Biol. , vol.159 , pp. 637-648
    • Chiu, R.1    Novikov, L.2    Mukherjee, S.3    Shields, D.4
  • 69
    • 1842426969 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis
    • DOI 10.1242/jcs.00950
    • Lowe, M., Lane, J. D., Woodman, P. G. and Allan, V. J. (2004) Caspase-mediated cleavage of syntaxin 5 and giantin accompanies inhibition of secretory traffic during apoptosis. J. Cell Sci. 117, 1139-1150 (Pubitemid 38456095)
    • (2004) Journal of Cell Science , vol.117 , Issue.7 , pp. 1139-1150
    • Lowe, M.1    Lane, J.D.2    Woodman, P.G.3    Allan, V.J.4
  • 71
    • 0037017405 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis
    • DOI 10.1083/jcb.200110007
    • Lane, J. D., Lucocq, J., Pryde, J., Barr, F. A., Woodman, P. G., Allan, V. J. and Lowe, M. (2002) Caspase-mediated cleavage of the stacking protein GRASP65 is required for Golgi fragmentation during apoptosis. J. Cell Biol. 156, 495-509 (Pubitemid 34839897)
    • (2002) Journal of Cell Biology , vol.156 , Issue.3 , pp. 495-509
    • Lane, J.D.1    Lucocq, J.2    Pryde, J.3    Barr, F.A.4    Woodman, P.G.5    Allan, V.J.6    Lowe, M.7
  • 73
    • 0035976142 scopus 로고    scopus 로고
    • Signaling pathways regulating Golgi structure and function
    • pe38
    • Preisinger, C. and Barr, F. A. (2001) Signaling pathways regulating Golgi structure and function. Sci. STKE 106, pe38
    • (2001) Sci. STKE , vol.106
    • Preisinger, C.1    Barr, F.A.2
  • 74
    • 65249115901 scopus 로고    scopus 로고
    • A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing
    • Yadav, S., Puri, S. and Linstedt, A. D. (2009) A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing. Mol. Biol. Cell 20, 1728-1736
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1728-1736
    • Yadav, S.1    Puri, S.2    Linstedt, A.D.3
  • 76
    • 67949124784 scopus 로고    scopus 로고
    • On vesicle formation and tethering in the ER-Golgi shuttle
    • Spang, A. (2009) On vesicle formation and tethering in the ER-Golgi shuttle. Curr. Opin. Cell Biol. 21, 531-536
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 531-536
    • Spang, A.1
  • 79
    • 77149155386 scopus 로고    scopus 로고
    • Unconventional secretion of Acb1 is mediated by autophagosomes
    • Duran, J. M., Anjard, C., Stefan, C., Loomis, W. F. and Malhotra, V. (2010) Unconventional secretion of Acb1 is mediated by autophagosomes. J. Cell Biol. 188, 527-536
    • (2010) J. Cell Biol. , vol.188 , pp. 527-536
    • Duran, J.M.1    Anjard, C.2    Stefan, C.3    Loomis, W.F.4    Malhotra, V.5
  • 80
    • 77149152566 scopus 로고    scopus 로고
    • Unconventional secretion of Pichia pastorisAcb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation
    • Manjithaya, R., Anjard, C., Loomis, W. F. and Subramani, S. (2010) Unconventional secretion of Pichia pastorisAcb1 is dependent on GRASP protein, peroxisomal functions, and autophagosome formation. J. Cell Biol. 188, 537-546
    • (2010) J. Cell Biol. , vol.188 , pp. 537-546
    • Manjithaya, R.1    Anjard, C.2    Loomis, W.F.3    Subramani, S.4
  • 81
    • 0034423410 scopus 로고    scopus 로고
    • Transmembrane transforming growth factor-α tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55
    • Kuo, A., Zhong, C., Lane, W. S. and Derynck, R. (2000) Transmembrane transforming growth factor-α tethers to the PDZ domain-containing, Golgi membrane-associated protein p59/GRASP55. EMBO J. 19, 6427-6439
    • (2000) EMBO J. , vol.19 , pp. 6427-6439
    • Kuo, A.1    Zhong, C.2    Lane, W.S.3    Derynck, R.4
  • 82
    • 58849089529 scopus 로고    scopus 로고
    • Mechanisms of regulated unconventional protein secretion
    • Nickel, W. and Rabouille, C. (2009) Mechanisms of regulated unconventional protein secretion. Nat Rev Mol Cell Biol. 10, 148-155
    • (2009) Nat Rev Mol Cell Biol. , vol.10 , pp. 148-155
    • Nickel, W.1    Rabouille, C.2
  • 83
    • 77956791062 scopus 로고    scopus 로고
    • Unconventional secretion of AcbA in Dictyostelium discoideumthrough a vesicular intermediate
    • Cabral, M., Anjard, C., Malhotra, V., Loomis, W. F. and Kuspa, A. (2010) Unconventional secretion of AcbA in Dictyostelium discoideumthrough a vesicular intermediate. Eukaryot. Cell 9, 1009-1017
    • (2010) Eukaryot. Cell , vol.9 , pp. 1009-1017
    • Cabral, M.1    Anjard, C.2    Malhotra, V.3    Loomis, W.F.4    Kuspa, A.5
  • 84
    • 34547579825 scopus 로고    scopus 로고
    • GRASPing unconventional secretion
    • Levi, S. K. and Glick, B. S. (2007) GRASPing unconventional secretion. Cell 130, 407-409
    • (2007) Cell , vol.130 , pp. 407-409
    • Levi, S.K.1    Glick, B.S.2
  • 85
    • 78751496610 scopus 로고    scopus 로고
    • Golgi bypass: Skirting around the heart of classical secretion
    • (Warren, G. and Rothman, J., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Grieve, A. G. and Rabouille, C. (2010) Golgi bypass: skirting around the heart of classical secretion. In The Golgi Book: Cold Spring Harbor Perspectives in Biology (Warren, G. and Rothman, J., eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (2010) The Golgi Book: Cold Spring Harbor Perspectives in Biology
    • Grieve, A.G.1    Rabouille, C.2
  • 86
    • 77957329900 scopus 로고    scopus 로고
    • Pathways of unconventional protein secretion
    • Nickel, W. (2010) Pathways of unconventional protein secretion. Curr. Opin. Biotechnol. 21, 621-626
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 621-626
    • Nickel, W.1
  • 87
    • 35848942606 scopus 로고    scopus 로고
    • Transcriptional modulation of genes encoding structural characteristics of differentiating enterocytes during development of a polarized epithelium in vitro
    • Halbleib, J. M., Saaf, AM., Brown, P. O. and Nelson, W. J. (2007) Transcriptional modulation of genes encoding structural characteristics of differentiating enterocytes during development of a polarized epithelium in vitro. Mol. Biol. Cell 18, 4261-4278
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4261-4278
    • Halbleib, J.M.1    Saaf, A.M.2    Brown, P.O.3    Nelson, W.J.4
  • 88
    • 69549138483 scopus 로고    scopus 로고
    • Integrins mediate their unconventional, mechanical-stress-induced secretion via RhoA and PINCH in Drosophila
    • Schotman, H., Karhinen, L. and Rabouille, C. (2009) Integrins mediate their unconventional, mechanical-stress-induced secretion via RhoA and PINCH in Drosophila. J. Cell Sci. 122, 2662-2672
    • (2009) J. Cell Sci. , vol.122 , pp. 2662-2672
    • Schotman, H.1    Karhinen, L.2    Rabouille, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.