메뉴 건너뛰기




Volumn 46, Issue 1, 2018, Pages 43-50

At the ends of their tethers! How coiled-coil proteins capture vesicles at the golgi

Author keywords

[No Author keywords available]

Indexed keywords

COILED COIL PROTEIN; LIPID; MEMBRANE PROTEIN; SECRETORY PROTEIN; UNCLASSIFIED DRUG;

EID: 85043375557     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20170188     Document Type: Review
Times cited : (12)

References (73)
  • 1
    • 84890246880 scopus 로고    scopus 로고
    • A Nobel Prize for membrane traffic: Vesicles find their journey’s end
    • Mellman, I. and Emr, S.D. (2013) A Nobel Prize for membrane traffic: vesicles find their journey’s end. J. Cell Biol. 203, 559–561 https://doi.org/10.1083/jcb.201310134
    • (2013) J. Cell Biol. , vol.203 , pp. 559-561
    • Mellman, I.1    Emr, S.D.2
  • 2
    • 84890883320 scopus 로고    scopus 로고
    • Vesicular transport earns a Nobel
    • Bonifacino, J.S. (2014) Vesicular transport earns a Nobel. Trends Cell Biol. 24, 3–5 https://doi.org/10.1016/j.tcb.2013.11.001
    • (2014) Trends Cell Biol , vol.24 , pp. 3-5
    • Bonifacino, J.S.1
  • 3
    • 2942755631 scopus 로고    scopus 로고
    • Organelle identity and the organization of membrane traffic
    • Munro, S. (2004) Organelle identity and the organization of membrane traffic. Nat. Cell Biol. 6, 469–472 https://doi.org/10.1038/ncb0604-469
    • (2004) Nat. Cell Biol. , vol.6 , pp. 469-472
    • Munro, S.1
  • 4
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia, R. and Munro, S. (2005) Organelle identity and the signposts for membrane traffic. Nature 438, 597–604 https://doi.org/10.1038/nature04397
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 5
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • PMID:12077354
    • Whyte, J.R.C. and Munro, S. (2002) Vesicle tethering complexes in membrane traffic. J. Cell. Sci. 115, 2627–2637 PMID:12077354
    • (2002) J. Cell. Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.C.1    Munro, S.2
  • 6
    • 78049368534 scopus 로고    scopus 로고
    • Tethering factors as organizers of intracellular vesicular traffic
    • Yu, I.-M. and Hughson, F.M. (2010) Tethering factors as organizers of intracellular vesicular traffic. Annu. Rev. Cell Dev. Biol. 26, 137–156 https://doi.org/10.1146/annurev.cellbio.042308.113327
    • (2010) Annu. Rev. Cell Dev. Biol. , vol.26 , pp. 137-156
    • Yu, I.-M.1    Hughson, F.M.2
  • 7
    • 0032581654 scopus 로고    scopus 로고
    • EEA1 links PI(3)K function to Rab5 regulation of endosome fusion
    • Simonsen, A., Lippé, R., Christoforidis, S., Gaullier, J.-M., Brech, A., Callaghan, J. et al. (1998) EEA1 links PI(3)K function to Rab5 regulation of endosome fusion. Nature 394, 494–498 https://doi.org/10.1038/28879
    • (1998) Nature , vol.394 , pp. 494-498
    • Simonsen, A.1    Lippé, R.2    Christoforidis, S.3    Gaullier, J.-M.4    Brech, A.5    Callaghan, J.6
  • 8
    • 0033580299 scopus 로고    scopus 로고
    • The Rab5 effector EEA1 is a core component of endosome docking
    • Christoforidis, S., McBride, H.M., Burgoyne, R.D. and Zerial, M. (1999) The Rab5 effector EEA1 is a core component of endosome docking. Nature 397, 621–625 https://doi.org/10.1038/17618
    • (1999) Nature , vol.397 , pp. 621-625
    • Christoforidis, S.1    McBride, H.M.2    Burgoyne, R.D.3    Zerial, M.4
  • 9
    • 84955320566 scopus 로고    scopus 로고
    • TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export
    • Santos, A.J.M., Raote, I., Scarpa, M., Brouwers, N. and Malhotra, V. (2015) TANGO1 recruits ERGIC membranes to the endoplasmic reticulum for procollagen export. eLife 4, e10982 https://doi.org/10.7554/eLife.10982
    • (2015) eLife , vol.4 , pp. e10982
    • Santos, A.J.M.1    Raote, I.2    Scarpa, M.3    Brouwers, N.4    Malhotra, V.5
  • 10
    • 17044430726 scopus 로고    scopus 로고
    • Multi-component protein complexes and Golgi membrane trafficking
    • Oka, T. (2005) Multi-component protein complexes and Golgi membrane trafficking. J. Biochem. 137, 109–114 https://doi.org/10.1093/jb/mvi024
    • (2005) J. Biochem. , vol.137 , pp. 109-114
    • Oka, T.1
  • 11
    • 78149306025 scopus 로고    scopus 로고
    • Multisubunit tethering complexes and their role in membrane fusion
    • Bröcker, C., Engelbrecht-Vandré, S. and Ungermann, C. (2010) Multisubunit tethering complexes and their role in membrane fusion. Curr. Biol. 20, R943–R952 https://doi.org/10.1016/j.cub.2010.09.015
    • (2010) Curr. Biol. , vol.20 , pp. R943-R952
    • Bröcker, C.1    Engelbrecht-Vandré, S.2    Ungermann, C.3
  • 12
    • 85043368012 scopus 로고    scopus 로고
    • The golgin family of coiled-coil tethering proteins
    • Witkos, T.M. and Lowe, M. (2016) The golgin family of coiled-coil tethering proteins. Front. Cell Dev. Biol. 3, 86 https://doi.org/10.3389/fcell.2015. 00086
    • (2016) Front. Cell Dev. Biol. , vol.3 , pp. 86
    • Witkos, T.M.1    Lowe, M.2
  • 13
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short, B., Haas, A. and Barr, F.A. (2005) Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta, Mol. Cell Res. 1744, 383–395 https://doi.org/10.1016/j.bbamcr.2005.02.001
    • (2005) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 14
    • 70450223107 scopus 로고    scopus 로고
    • Role of vesicle tethering factors in the ER-Golgi membrane traffic
    • Sztul, E. and Lupashin, V. (2009) Role of vesicle tethering factors in the ER-Golgi membrane traffic. FEBS Lett. 583, 3770–3783 https://doi.org/10.1016/j.febslet.2009.10.083
    • (2009) FEBS Lett , vol.583 , pp. 3770-3783
    • Sztul, E.1    Lupashin, V.2
  • 15
    • 80455144527 scopus 로고    scopus 로고
    • Architecture of the mammalian Golgi
    • Klumperman, J. (2011) Architecture of the mammalian Golgi. Cold Spring Harb. Perspect. Biol. 3, a005181 https://doi.org/10.1101/cshperspect. a005181
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a005181
    • Klumperman, J.1
  • 16
    • 84862492324 scopus 로고    scopus 로고
    • Models for Golgi traffic: A critical assessment
    • Glick, B.S. and Luini, A. (2011) Models for Golgi traffic: a critical assessment. Cold Spring Harb. Perspect. Biol. 3, a005215 https://doi.org/10.1101/cshperspect.a005215
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a005215
    • Glick, B.S.1    Luini, A.2
  • 17
    • 0027198921 scopus 로고
    • Molecular characterization of two human autoantigens: Unique cDNAs encoding 95- And 160-kD proteins of a putative family in the Golgi complex
    • Fritzler, M.J., Hamel, J.C., Ochs, R.L. and Chan, E.K. (1993) Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex. J. Exp. Med. 178, 49–62 https://doi.org/10.1084/jem.178.1.49
    • (1993) J. Exp. Med. , vol.178 , pp. 49-62
    • Fritzler, M.J.1    Hamel, J.C.2    Ochs, R.L.3    Chan, E.K.4
  • 18
    • 84860311872 scopus 로고    scopus 로고
    • The golgin coiled-coil proteins of the Golgi apparatus
    • Munro, S. (2011) The golgin coiled-coil proteins of the Golgi apparatus. Cold Spring Harb. Perspect. Biol. 3, a005256 https://doi.org/10.1101/cshperspect.a005256
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. a005256
    • Munro, S.1
  • 19
    • 70349335825 scopus 로고    scopus 로고
    • Golgins and GRASPs: Holding the Golgi together
    • Ramirez, I.B.-R. and Lowe, M. (2009) Golgins and GRASPs: holding the Golgi together. Semin. Cell Dev. Biol. 20, 770–779 https://doi.org/10.1016/j.semcdb.2009.03.011
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 770-779
    • Ramirez, I.B.-R.1    Lowe, M.2
  • 20
    • 0035035657 scopus 로고    scopus 로고
    • The Golgi matrix protein GM130: A specific interacting partner of the small GTPase rab1b
    • Weide, T., Bayer, M., Köster, M., Siebrasse, J.-P., Peters, R. and Barnekow, A. (2001) The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b. EMBO Rep. 2, 336–341 https://doi.org/10.1093/embo-reports/kve065
    • (2001) EMBO Rep , vol.2 , pp. 336-341
    • Weide, T.1    Bayer, M.2    Köster, M.3    Siebrasse, J.-P.4    Peters, R.5    Barnekow, A.6
  • 21
    • 0035024551 scopus 로고    scopus 로고
    • Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering
    • Moyer, B.D., Allan, B.B. and Balch, W.E. (2001) Rab1 interaction with a GM130 effector complex regulates COPII vesicle cis-Golgi tethering. Traffic 2, 268–276 https://doi.org/10.1034/j.1600-0854.2001.1o007.x
    • (2001) Traffic , vol.2 , pp. 268-276
    • Moyer, B.D.1    Allan, B.B.2    Balch, W.E.3
  • 22
    • 7244248570 scopus 로고    scopus 로고
    • The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi
    • Gillingham, A.K., Tong, A.H.Y., Boone, C. and Munro, S. (2004) The GTPase Arf1p and the ER to Golgi cargo receptor Erv14p cooperate to recruit the golgin Rud3p to the cis-Golgi. J. Cell Biol. 167, 281–292 https://doi.org/10.1083/jcb.200407088
    • (2004) J. Cell Biol. , vol.167 , pp. 281-292
    • Gillingham, A.K.1    Tong, A.H.Y.2    Boone, C.3    Munro, S.4
  • 23
    • 0036855657 scopus 로고    scopus 로고
    • CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin
    • Gillingham, A.K., Pfeifer, A.C. and Munro, S. (2002) CASP, the alternatively spliced product of the gene encoding the CCAAT-displacement protein transcription factor, is a Golgi membrane protein related to giantin. Mol. Biol. Cell 13, 3761–3774 https://doi.org/10.1091/mbc.E02-06-0349
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3761-3774
    • Gillingham, A.K.1    Pfeifer, A.C.2    Munro, S.3
  • 24
    • 0033613967 scopus 로고    scopus 로고
    • Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain
    • Bascom, R.A., Srinivasan, S. and Nussbaum, R.L. (1999) Identification and characterization of golgin-84, a novel Golgi integral membrane protein with a cytoplasmic coiled-coil domain. J. Biol. Chem. 274, 2953–2962 https://doi.org/10.1074/jbc.274.5.2953
    • (1999) J. Biol. Chem. , vol.274 , pp. 2953-2962
    • Bascom, R.A.1    Srinivasan, S.2    Nussbaum, R.L.3
  • 25
    • 0029038898 scopus 로고
    • A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus
    • Linstedt, A.D., Foguet, M., Renz, M., Seelig, H.P., Glick, B.S. and Hauri, H.P. (1995) A C-terminally-anchored Golgi protein is inserted into the endoplasmic reticulum and then transported to the Golgi apparatus. Proc. Natl Acad. Sci. U.S.A. 92, 5102–5105 https://doi.org/10.1073/pnas.92.11. 5102
    • (1995) Proc. Natl Acad. Sci. U.S.A. , vol.92 , pp. 5102-5105
    • Linstedt, A.D.1    Foguet, M.2    Renz, M.3    Seelig, H.P.4    Glick, B.S.5    Hauri, H.P.6
  • 26
    • 10444236367 scopus 로고    scopus 로고
    • TMF is a golgin that binds Rab6 and influences Golgi morphology
    • Fridmann-Sirkis, Y., Siniossoglou, S. and Pelham, H.R.B. (2004) TMF is a golgin that binds Rab6 and influences Golgi morphology. BMC Cell Biol. 5, 18 https://doi.org/10.1186/1471-2121-5-18
    • (2004) BMC Cell Biol , vol.5 , pp. 18
    • Fridmann-Sirkis, Y.1    Siniossoglou, S.2    Pelham, H.R.B.3
  • 27
    • 0141856316 scopus 로고    scopus 로고
    • Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi
    • Lu, L. and Hong, W. (2003) Interaction of Arl1-GTP with GRIP domains recruits autoantigens Golgin-97 and Golgin-245/p230 onto the Golgi. Mol. Biol. Cell 14, 3767–3781 https://doi.org/10.1091/mbc.E03-01-0864
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3767-3781
    • Lu, L.1    Hong, W.2
  • 28
    • 0037418580 scopus 로고    scopus 로고
    • Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3
    • Setty, S.R.G., Shin, M.E., Yoshino, A., Marks, M.S. and Burd, C.G. (2003) Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3. Curr. Biol. 13, 401–404 https://doi.org/10.1016/S0960-9822(03)00089-7
    • (2003) Curr. Biol. , vol.13 , pp. 401-404
    • Setty, S.R.G.1    Shin, M.E.2    Yoshino, A.3    Marks, M.S.4    Burd, C.G.5
  • 29
    • 0242266897 scopus 로고    scopus 로고
    • Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus
    • Panic, B., Perisic, O., Veprintsev, D.B., Williams, R.L. and Munro, S. (2003) Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol. Cell 12, 863–874 https://doi.org/10.1016/S1097-2765(03)00356-3
    • (2003) Mol. Cell , vol.12 , pp. 863-874
    • Panic, B.1    Perisic, O.2    Veprintsev, D.B.3    Williams, R.L.4    Munro, S.5
  • 30
    • 38749150383 scopus 로고    scopus 로고
    • Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185
    • Burguete, A.S., Fenn, T.D., Brunger, A.T. and Pfeffer, S.R. (2008) Rab and Arl GTPase family members cooperate in the localization of the golgin GCC185. Cell 132, 286–298 https://doi.org/10.1016/j.cell.2007.11.048
    • (2008) Cell , vol.132 , pp. 286-298
    • Burguete, A.S.1    Fenn, T.D.2    Brunger, A.T.3    Pfeffer, S.R.4
  • 31
    • 68749097137 scopus 로고    scopus 로고
    • The localization of the Golgin GCC185 is independent of Rab6A/A’ and Arl1
    • Houghton, F.J., Chew, P.L., Lodeho, S., Goud, B. and Gleeson, P.A. (2009) The localization of the Golgin GCC185 is independent of Rab6A/A’ and Arl1. Cell 138, 787–794 https://doi.org/10.1016/j.cell.2009.05.048
    • (2009) Cell , vol.138 , pp. 787-794
    • Houghton, F.J.1    Chew, P.L.2    Lodeho, S.3    Goud, B.4    Gleeson, P.A.5
  • 32
    • 84983436060 scopus 로고    scopus 로고
    • Coiled-coils: The long and short of it
    • Truebestein, L. and Leonard, T.A. (2016) Coiled-coils: the long and short of it. BioEssays 38, 903–916 https://doi.org/10.1002/bies.201600062
    • (2016) BioEssays , vol.38 , pp. 903-916
    • Truebestein, L.1    Leonard, T.A.2
  • 33
    • 0035842903 scopus 로고    scopus 로고
    • A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic
    • Short, B., Preisinger, C., Körner, 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, 877–884 https://doi.org/10.1083/jcb.200108079
    • (2001) J. Cell Biol. , vol.155 , pp. 877-884
    • Short, B.1    Preisinger, C.2    Körner, R.3    Kopajtich, R.4    Byron, O.5    Barr, F.A.6
  • 34
    • 0037183696 scopus 로고    scopus 로고
    • 2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information
    • 2-terminal domain of Golgin-160 contains both Golgi and nuclear targeting information. J. Biol. Chem. 277, 35833–35839 https://doi.org/10.1074/jbc.M206280200
    • (2002) J. Biol. Chem. , vol.277 , pp. 35833-35839
    • Hicks, S.W.1    Machamer, C.E.2
  • 35
    • 67651095767 scopus 로고    scopus 로고
    • Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering
    • An, Y., Chen, C.Y., Moyer, B., Rotkiewicz, P., Elsliger, M.-A., Godzik, A. et al. (2009) Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering. J. Mol. Biol. 391, 26–41 https://doi.org/10.1016/j.jmb.2009.04.062
    • (2009) J. Mol. Biol. , vol.391 , pp. 26-41
    • An, Y.1    Chen, C.Y.2    Moyer, B.3    Rotkiewicz, P.4    Elsliger, M.-A.5    Godzik, A.6
  • 36
    • 84864285674 scopus 로고    scopus 로고
    • Unusual armadillo fold in the human general vesicular transport factor p115
    • Striegl, H., Roske, Y., Kümmel, D. and Heinemann, U. (2009) Unusual Armadillo fold in the human general vesicular transport factor p115. PLoS ONE. 4, e4656 https://doi.org/10.1371/journal.pone.0004656
    • (2009) PLoS ONE , vol.4
    • Striegl, H.1    Roske, Y.2    Kümmel, D.3    Heinemann, U.4
  • 37
    • 84922753210 scopus 로고    scopus 로고
    • Toward a comprehensive map of the effectors of rab GTPases
    • Gillingham, A.K., Sinka, R., Torres, I.L., Lilley, K.S. and Munro, S. (2014) Toward a comprehensive map of the effectors of rab GTPases. Dev. Cell 31, 358–373 https://doi.org/10.1016/j.devcel.2014.10.007
    • (2014) Dev. Cell , vol.31 , pp. 358-373
    • Gillingham, A.K.1    Sinka, R.2    Torres, I.L.3    Lilley, K.S.4    Munro, S.5
  • 38
    • 85031821873 scopus 로고    scopus 로고
    • The dense-core vesicle maturation protein CCCP-1 binds RAB-2 and membranes through its C-terminal domain
    • Cattin-Ortolá, J., Topalidou, I., Dosey, A., Merz, A.J. and Ailion, M. (2017) The dense-core vesicle maturation protein CCCP-1 binds RAB-2 and membranes through its C-terminal domain. Traffic 18, 720–732 https://doi.org/10.1111/tra.12507
    • (2017) Traffic , vol.18 , pp. 720-732
    • Cattin-Ortolá, J.1    Topalidou, I.2    Dosey, A.3    Merz, A.J.4    Ailion, M.5
  • 39
    • 84897467061 scopus 로고    scopus 로고
    • Two Rab2 interactors regulate dense-core vesicle maturation
    • Ailion, M., Hannemann, M., Dalton, S., Pappas, A., Watanabe, S., Hegermann, J. et al. (2014) Two Rab2 interactors regulate dense-core vesicle maturation. Neuron 82, 167–180 https://doi.org/10.1016/j.neuron.2014.02.017
    • (2014) Neuron , vol.82 , pp. 167-180
    • Ailion, M.1    Hannemann, M.2    Dalton, S.3    Pappas, A.4    Watanabe, S.5    Hegermann, J.6
  • 40
    • 29244468267 scopus 로고    scopus 로고
    • Coiled-coil protein composition of 22 proteomes—differences and common themes in subcellular infrastructure and traffic control
    • Rose, A., Schraegle, S.J., Stahlberg, E.A. and Meier, I. (2005) Coiled-coil protein composition of 22 proteomes—differences and common themes in subcellular infrastructure and traffic control. BMC Evol. Biol. 5, 66 https://doi.org/10.1186/1471-2148-5-66
    • (2005) BMC Evol. Biol. , vol.5 , pp. 66
    • Rose, A.1    Schraegle, S.J.2    Stahlberg, E.A.3    Meier, I.4
  • 41
    • 0030807931 scopus 로고    scopus 로고
    • Coupled ER to Golgi transport reconstituted with purified cytosolic proteins
    • Barlowe, C. (1997) Coupled ER to Golgi transport reconstituted with purified cytosolic proteins. J. Cell Biol. 139, 1097–1108 https://doi.org/10.1083/jcb.139.5.1097
    • (1997) J. Cell Biol. , vol.139 , pp. 1097-1108
    • Barlowe, C.1
  • 42
    • 0032522377 scopus 로고    scopus 로고
    • Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins
    • Cao, X., Ballew, N. and Barlowe, C. (1998) Initial docking of ER-derived vesicles requires Uso1p and Ypt1p but is independent of SNARE proteins. EMBO J. 17, 2156–2165 https://doi.org/10.1093/emboj/17.8.2156
    • (1998) EMBO J , vol.17 , pp. 2156-2165
    • Cao, X.1    Ballew, N.2    Barlowe, C.3
  • 43
    • 13844317835 scopus 로고    scopus 로고
    • Golgin tethers define subpopulations of COPI vesicles
    • Malsam, J., Satoh, A., Pelletier, L. and Warren, G. (2005) Golgin tethers define subpopulations of COPI vesicles. Science 307, 1095–1098 https://doi.org/10.1126/science.1108061
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 44
    • 43249126878 scopus 로고    scopus 로고
    • Asymmetric tethering of flat and curved lipid membranes by a golgin
    • Drin, G., Morello, V., Casella, J.-F., Gounon, P. and Antonny, B. (2008) Asymmetric tethering of flat and curved lipid membranes by a golgin. Science 320, 670–673 https://doi.org/10.1126/science.1155821
    • (2008) Science , vol.320 , pp. 670-673
    • Drin, G.1    Morello, V.2    Casella, J.-F.3    Gounon, P.4    Antonny, B.5
  • 45
    • 21044446690 scopus 로고    scopus 로고
    • TGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre
    • Yoshino, A., Setty, S.R.G., Poynton, C., Whiteman, E.L., Saint-Pol, A., Burd, C.G. et al. (2005) tGolgin-1 (p230, golgin-245) modulates Shiga-toxin transport to the Golgi and Golgi motility towards the microtubule-organizing centre. J. Cell Sci. 118, 2279–2293 https://doi.org/10.1242/jcs.02358
    • (2005) J. Cell Sci. , vol.118 , pp. 2279-2293
    • Yoshino, A.1    Setty, S.R.G.2    Poynton, C.3    Whiteman, E.L.4    Saint-Pol, A.5    Burd, C.G.6
  • 46
    • 4644352428 scopus 로고    scopus 로고
    • Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network
    • Lu, L., Tai, G. and Hong, W. (2004) Autoantigen Golgin-97, an effector of Arl1 GTPase, participates in traffic from the endosome to the trans-Golgi network. Mol. Biol. Cell 15, 4426–4443 https://doi.org/10.1091/mbc.E03-12-0872
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4426-4443
    • Lu, L.1    Tai, G.2    Hong, W.3
  • 48
    • 0043162027 scopus 로고    scopus 로고
    • Long coiled-coil proteins and membrane traffic
    • Gillingham, A.K. and Munro, S. (2003) Long coiled-coil proteins and membrane traffic. Biochim. Biophys. Acta, Mol. Cell Res. 1641, 71–85 https://doi.org/10.1016/S0167-4889(03)00088-0
    • (2003) Biochim. Biophys. Acta, Mol. Cell Res. , vol.1641 , pp. 71-85
    • Gillingham, A.K.1    Munro, S.2
  • 49
    • 84910104915 scopus 로고    scopus 로고
    • Membrane trafficking. The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins
    • Wong, M. and Munro, S. (2014) Membrane trafficking. The specificity of vesicle traffic to the Golgi is encoded in the golgin coiled-coil proteins. Science 346, 1256898 https://doi.org/10.1126/science.1256898
    • (2014) Science , vol.346 , pp. 1256898
    • Wong, M.1    Munro, S.2
  • 50
    • 85030328444 scopus 로고    scopus 로고
    • The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs
    • Anderson, N.S., Mukherjee, I., Bentivoglio, C.M. and Barlowe, C. (2017) The Golgin protein Coy1 functions in intra-Golgi retrograde transport and interacts with the COG complex and Golgi SNAREs. Mol. Biol. Cell 28, 2686–2700 https://doi.org/10.1091/mbc.E17-03-0137
    • (2017) Mol. Biol. Cell , vol.28 , pp. 2686-2700
    • Anderson, N.S.1    Mukherjee, I.2    Bentivoglio, C.M.3    Barlowe, C.4
  • 51
    • 33749496326 scopus 로고    scopus 로고
    • A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling
    • Reddy, J.V., Burguete, A.S., Sridevi, K., Ganley, I.G., Nottingham, R.M. and Pfeffer, S.R. (2006) A functional role for the GCC185 golgin in mannose 6-phosphate receptor recycling. Mol. Biol. Cell 17, 4353–4363 https://doi.org/10.1091/mbc.E06-02-0153
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4353-4363
    • Reddy, J.V.1    Burguete, A.S.2    Sridevi, K.3    Ganley, I.G.4    Nottingham, R.M.5    Pfeffer, S.R.6
  • 52
    • 34249087754 scopus 로고    scopus 로고
    • The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure
    • Derby, M.C., Lieu, Z.Z., Brown, D., Stow, J.L., Goud, B. and Gleeson, P.A. (2007) The trans-Golgi network golgin, GCC185, is required for endosome-to-Golgi transport and maintenance of Golgi structure. Traffic 8, 758–773 https://doi.org/10.1111/j.1600-0854.2007.00563.x
    • (2007) Traffic , vol.8 , pp. 758-773
    • Derby, M.C.1    Lieu, Z.Z.2    Brown, D.3    Stow, J.L.4    Goud, B.5    Gleeson, P.A.6
  • 53
    • 34249305474 scopus 로고    scopus 로고
    • Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network
    • Efimov, A., Kharitonov, A., Efimova, N., Loncarek, J., Miller, P.M., Andreyeva, N. et al. (2007) Asymmetric CLASP-dependent nucleation of noncentrosomal microtubules at the trans-Golgi network. Dev. Cell 12, 917–930 https://doi.org/10.1016/j.devcel.2007.04.002
    • (2007) Dev. Cell , vol.12 , pp. 917-930
    • Efimov, A.1    Kharitonov, A.2    Efimova, N.3    Loncarek, J.4    Miller, P.M.5    Andreyeva, N.6
  • 54
    • 84979645497 scopus 로고    scopus 로고
    • A filter at the entrance of the Golgi that selects vesicles according to size and bulk lipid composition
    • Magdeleine, M., Gautier, R., Gounon, P., Barelli, H., Vanni, S. and Antonny, B. (2016) A filter at the entrance of the Golgi that selects vesicles according to size and bulk lipid composition. eLife 5, 292 https://doi.org/10.7554/eLife.16988
    • (2016) eLife , vol.5 , pp. 292
    • Magdeleine, M.1    Gautier, R.2    Gounon, P.3    Barelli, H.4    Vanni, S.5    Antonny, B.6
  • 55
    • 84960155907 scopus 로고    scopus 로고
    • Finding the Golgi: Golgin coiled-coil proteins show the way
    • Gillingham, A.K. and Munro, S. (2016) Finding the Golgi: golgin coiled-coil proteins show the way. Trends Cell Biol. 26, 399–408 https://doi.org/10.1016/j.tcb.2016.02.005
    • (2016) Trends Cell Biol , vol.26 , pp. 399-408
    • Gillingham, A.K.1    Munro, S.2
  • 56
    • 84968796233 scopus 로고    scopus 로고
    • Protein flexibility is required for vesicle tethering at the Golgi
    • Cheung, P.-Y.P., Limouse, C., Mabuchi, H. and Pfeffer, S.R. (2015) Protein flexibility is required for vesicle tethering at the Golgi. eLife 4, e12790 https://doi.org/10.7554/eLife.12790
    • (2015) eLife , vol.4 , pp. e12790
    • Cheung, P.-Y.P.1    Limouse, C.2    Mabuchi, H.3    Pfeffer, S.R.4
  • 57
    • 84930630268 scopus 로고    scopus 로고
    • GM130 is a parallel tetramer with a flexible rod-like structure and N-terminally open (Y-shaped) and closed (I-shaped) conformations
    • Ishida, R., Yamamoto, A., Nakayama, K., Sohda, M., Misumi, Y., Yasunaga, T. et al. (2015) GM130 is a parallel tetramer with a flexible rod-like structure and N-terminally open (Y-shaped) and closed (I-shaped) conformations. FEBS J. 282, 2232–2244 https://doi.org/10.1111/febs.13271
    • (2015) FEBS J , vol.282 , pp. 2232-2244
    • Ishida, R.1    Yamamoto, A.2    Nakayama, K.3    Sohda, M.4    Misumi, Y.5    Yasunaga, T.6
  • 58
    • 85010303342 scopus 로고    scopus 로고
    • The golgin coiled-coil proteins capture different types of transport carriers via distinct N-terminal motifs
    • Wong, M., Gillingham, A.K. and Munro, S. (2017) The golgin coiled-coil proteins capture different types of transport carriers via distinct N-terminal motifs. BMC Biol. 15, 3 https://doi.org/10.1186/s12915-016-0345-3
    • (2017) BMC Biol , vol.15 , pp. 3
    • Wong, M.1    Gillingham, A.K.2    Munro, S.3
  • 59
    • 85035067361 scopus 로고    scopus 로고
    • TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at the trans-Golgi
    • Shin, J.J.H., Gillingham, A.K., Begum, F., Chadwick, J. and Munro, S. (2017) TBC1D23 is a bridging factor for endosomal vesicle capture by golgins at the trans-Golgi. Nat. Cell Biol. 19, 1424–1432 https://doi.org/10.1038/ncb3627
    • (2017) Nat. Cell Biol. , vol.19 , pp. 1424-1432
    • Shin, J.J.H.1    Gillingham, A.K.2    Begum, F.3    Chadwick, J.4    Munro, S.5
  • 60
    • 84864843505 scopus 로고    scopus 로고
    • Formation of Golgi-derived active zone precursor vesicles
    • Maas, C., Torres, V.I., Altrock, W.D., Leal-Ortiz, S., Wagh, D., Terry-Lorenzo, R.T. et al. (2012) Formation of Golgi-derived active zone precursor vesicles. J. Neurosci. 32, 11095–11108 https://doi.org/10.1523/JNEUROSCI.0195-12.2012
    • (2012) J. Neurosci. , vol.32 , pp. 11095-11108
    • Maas, C.1    Torres, V.I.2    Altrock, W.D.3    Leal-Ortiz, S.4    Wagh, D.5    Terry-Lorenzo, R.T.6
  • 61
    • 84978792169 scopus 로고    scopus 로고
    • ELKS controls the pool of readily releasable vesicles at excitatory synapses through its N-terminal coiled-coil domains
    • Held, R.G., Liu, C. and Kaeser, P.S. (2016) ELKS controls the pool of readily releasable vesicles at excitatory synapses through its N-terminal coiled-coil domains. eLife 5, e14862 https://doi.org/10.7554/eLife.14862
    • (2016) eLife , vol.5 , pp. e14862
    • Held, R.G.1    Liu, C.2    Kaeser, P.S.3
  • 62
    • 58149181656 scopus 로고    scopus 로고
    • Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins
    • Sinka, R., Gillingham, A.K., Kondylis, V. and Munro, S. (2008) Golgi coiled-coil proteins contain multiple binding sites for Rab family G proteins. J. Cell Biol. 183, 607–615 https://doi.org/10.1083/jcb.200808018
    • (2008) J. Cell Biol. , vol.183 , pp. 607-615
    • Sinka, R.1    Gillingham, A.K.2    Kondylis, V.3    Munro, S.4
  • 63
    • 0030010763 scopus 로고    scopus 로고
    • Uso1 protein is a dimer with two globular heads and a long coiled-coil tail
    • Yamakawa, H., Seog, D.-H., Yoda, K., Yamasaki, M. and Wakabayashi, T. (1996) Uso1 protein is a dimer with two globular heads and a long coiled-coil tail. J. Struct. Biol. 116, 356–365 https://doi.org/10.1006/jsbi.1996.0053
    • (1996) J. Struct. Biol. , vol.116 , pp. 356-365
    • Yamakawa, H.1    Seog, D.-H.2    Yoda, K.3    Yamasaki, M.4    Wakabayashi, T.5
  • 64
    • 0034723203 scopus 로고    scopus 로고
    • The amino-terminal domain of the Golgi protein giantin interacts directly with the vesicle-tethering protein p115
    • Lesa, G.M., Seemann, J., Shorter, J., Vandekerckhove, J. and Warren, G. (2000) The amino-terminal domain of the Golgi protein giantin interacts directly with the vesicle-tethering protein p115. J. Biol. Chem. 275, 2831–2836 https://doi.org/10.1074/jbc.275.4.2831
    • (2000) J. Biol. Chem. , vol.275 , pp. 2831-2836
    • Lesa, G.M.1    Seemann, J.2    Shorter, J.3    Vandekerckhove, J.4    Warren, G.5
  • 65
    • 0032478142 scopus 로고    scopus 로고
    • Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
    • Orci, L., Perrelet, A. and Rothman, J.E. (1998) Vesicles on strings: morphological evidence for processive transport within the Golgi stack. Proc. Natl Acad. Sci. U.S.A. 95, 2279–2283 https://doi.org/10.1073/pnas.95.5.2279
    • (1998) Proc. Natl Acad. Sci. U.S.A. , vol.95 , pp. 2279-2283
    • Orci, L.1    Perrelet, A.2    Rothman, J.E.3
  • 66
    • 0028009409 scopus 로고
    • Isolation of a matrix that binds medial Golgi enzymes
    • Slusarewicz, P., Nilsson, T., Hui, N., Watson, R. and Warren, G. (1994) Isolation of a matrix that binds medial Golgi enzymes. J. Cell Biol. 124, 405–413 https://doi.org/10.1083/jcb.124.4.405
    • (1994) J. Cell Biol. , vol.124 , pp. 405-413
    • Slusarewicz, P.1    Nilsson, T.2    Hui, N.3    Watson, R.4    Warren, G.5
  • 67
    • 0027519664 scopus 로고
    • Cytoarchitecture of size-excluding compartments in living cells
    • PMID:7980739
    • Provance, D.W., McDowall, A., Marko, M. and Luby-Phelps, K. (1993) Cytoarchitecture of size-excluding compartments in living cells. J. Cell. Sci. 106 (Pt 2), 565–577 PMID:7980739
    • (1993) J. Cell. Sci. , vol.106 , pp. 565-577
    • Provance, D.W.1    McDowall, A.2    Marko, M.3    Luby-Phelps, K.4
  • 68
    • 84921882527 scopus 로고    scopus 로고
    • Coupling of vesicle tethering and Rab binding is required for in vivo functionality of the golgin GMAP-210
    • Sato, K., Roboti, P., Mironov, A.A. and Lowe, M. (2015) Coupling of vesicle tethering and Rab binding is required for in vivo functionality of the golgin GMAP-210. Mol. Biol. Cell 26, 537–553 https://doi.org/10.1091/mbc.E14-10-1450
    • (2015) Mol. Biol. Cell , vol.26 , pp. 537-553
    • Sato, K.1    Roboti, P.2    Mironov, A.A.3    Lowe, M.4
  • 69
    • 84984653623 scopus 로고    scopus 로고
    • An endosomal tether undergoes an entropic collapse to bring vesicles together
    • Murray, D.H., Jahnel, M., Lauer, J., Avellaneda, M.J., Brouilly, N., Cezanne, A. et al. (2016) An endosomal tether undergoes an entropic collapse to bring vesicles together. Nature 537, 107–111 https://doi.org/10.1038/nature19326
    • (2016) Nature , vol.537 , pp. 107-111
    • Murray, D.H.1    Jahnel, M.2    Lauer, J.3    Avellaneda, M.J.4    Brouilly, N.5    Cezanne, A.6
  • 70
    • 84921438038 scopus 로고    scopus 로고
    • P115-SNARE interactions: A dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles
    • Wang, T., Grabski, R., Sztul, E. and Hay, J.C. (2015) p115-SNARE interactions: a dynamic cycle of p115 binding monomeric SNARE motifs and releasing assembled bundles. Traffic 16, 148–171 https://doi.org/10.1111/tra.12242
    • (2015) Traffic , vol.16 , pp. 148-171
    • Wang, T.1    Grabski, R.2    Sztul, E.3    Hay, J.C.4
  • 71
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • Shorter, J., Beard, M.B., Seemann, J., Dirac-Svejstrup, A.B. and Warren, G. (2002) Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J. Cell Biol. 157, 45–62 https://doi.org/10.1083/jcb.200112127
    • (2002) J. Cell Biol. , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seemann, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 72
    • 84873630243 scopus 로고    scopus 로고
    • Molecular insights into vesicle tethering at the Golgi by the conserved oligomeric Golgi (COG) complex and the golgin TATA element modulatory factor (TMF)
    • Miller, V.J., Sharma, P., Kudlyk, T.A., Frost, L., Rofe, A.P., Watson, I.J. et al. (2013) Molecular insights into vesicle tethering at the Golgi by the conserved oligomeric Golgi (COG) complex and the golgin TATA element modulatory factor (TMF). J. Biol. Chem. 288, 4229–4240 https://doi.org/10.1074/jbc.M112.426767
    • (2013) J. Biol. Chem. , vol.288 , pp. 4229-4240
    • Miller, V.J.1    Sharma, P.2    Kudlyk, T.A.3    Frost, L.4    Rofe, A.P.5    Watson, I.J.6
  • 73
    • 78349291116 scopus 로고    scopus 로고
    • Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport
    • Sohda, M., Misumi, Y., Yamamoto, A., Nakamura, N., Ogata, S., Sakisaka, S. et al. (2010) Interaction of Golgin-84 with the COG complex mediates the intra-Golgi retrograde transport. Traffic 11, 1552–1566 https://doi.org/10.1111/j.1600-0854.2010.01123.x
    • (2010) Traffic , vol.11 , pp. 1552-1566
    • Sohda, M.1    Misumi, Y.2    Yamamoto, A.3    Nakamura, N.4    Ogata, S.5    Sakisaka, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.