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Volumn 3, Issue JAN, 2016, Pages

The golgin family of coiled-coil tethering proteins

Author keywords

Cytoskeleton; Golgi apparatus; Golgin; Tether; Vesicle trafficking

Indexed keywords


EID: 85043368012     PISSN: None     EISSN: 2296634X     Source Type: Journal    
DOI: 10.3389/fcell.2015.00086     Document Type: Review
Times cited : (81)

References (57)
  • 1
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • 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. doi: 10.1016/S0092-8674(00)80407-9
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 2
    • 84923250091 scopus 로고    scopus 로고
    • Spatial control of Cdc42 signalling by a GM130-RasGRF complex regulates polarity and tumorigenesis
    • Baschieri, F., Confalonieri, S., Bertalot, G., Di Fiore, P. P., Dietmaier, W., Leist, M., et al. (2014). Spatial control of Cdc42 signalling by a GM130-RasGRF complex regulates polarity and tumorigenesis. Nat. Commun. 5:4839. doi: 10.1038/ncomms5839
    • (2014) Nat. Commun , vol.5 , pp. 4839
    • Baschieri, F.1    Confalonieri, S.2    Bertalot, G.3    Di Fiore, P.P.4    Dietmaier, W.5    Leist, M.6
  • 3
    • 84897564042 scopus 로고    scopus 로고
    • Reprogrammed and transmissible intestinal microbiota confer diminished susceptibility to induced colitis in TMF-/-mice
    • Bel, S., Elkis, Y., Elifantz, H., Koren, O., Ben-Hamo, R., Lerer-Goldshtein, T., et al. (2014). Reprogrammed and transmissible intestinal microbiota confer diminished susceptibility to induced colitis in TMF-/-mice. Proc. Natl. Acad. Sci. U.S.A. 111, 4964-4969. doi: 10.1073/pnas.1319114111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 4964-4969
    • Bel, S.1    Elkis, Y.2    Elifantz, H.3    Koren, O.4    Ben-Hamo, R.5    Lerer-Goldshtein, T.6
  • 4
    • 84864090540 scopus 로고    scopus 로고
    • Loss of TMF/ARA160 protein renders colonic mucus refractory to bacterial colonization and diminishes intestinal susceptibility to acute colitis
    • Bel, S., Elkis, Y., Lerer-Goldstein, T., Nyska, A., Shpungin, S., and Nir, U. (2012). Loss of TMF/ARA160 protein renders colonic mucus refractory to bacterial colonization and diminishes intestinal susceptibility to acute colitis. J. Biol. Chem. 287, 25631-25639. doi: 10.1074/jbc.M112.364786
    • (2012) J. Biol. Chem , vol.287 , pp. 25631-25639
    • Bel, S.1    Elkis, Y.2    Lerer-Goldstein, T.3    Nyska, A.4    Shpungin, S.5    Nir, U.6
  • 5
    • 84968796233 scopus 로고    scopus 로고
    • Protein flexibility is required for vesicle tethering at the Golgi
    • [Epub ahead of print]
    • Cheung, P. P., Limouse, C., Mabuchi, H., and Pfeffer, S. R. (2015). Protein flexibility is required for vesicle tethering at the Golgi. eLife. doi: 10.7554/eLife.12790. [Epub ahead of print]
    • (2015) ELife
    • Cheung, P.P.1    Limouse, C.2    Mabuchi, H.3    Pfeffer, S.R.4
  • 6
    • 43749087389 scopus 로고    scopus 로고
    • Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner
    • Diao, A., Frost, L., Morohashi, Y., and Lowe, M. (2008). Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner. J. Biol. Chem. 283, 6957-6967. doi: 10.1074/jbc.M708401200
    • (2008) J. Biol. Chem , vol.283 , pp. 6957-6967
    • Diao, A.1    Frost, L.2    Morohashi, Y.3    Lowe, M.4
  • 7
    • 0037455546 scopus 로고    scopus 로고
    • The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation
    • Diao, A., Rahman, D., Pappin, D. J., Lucocq, J., and Lowe, M. (2003). The coiled-coil membrane protein golgin-84 is a novel rab effector required for Golgi ribbon formation. J. Cell Biol. 160, 201-212. doi: 10.1083/jcb.200207045
    • (2003) J. Cell Biol , vol.160 , pp. 201-212
    • Diao, A.1    Rahman, D.2    Pappin, D.J.3    Lucocq, J.4    Lowe, M.5
  • 9
    • 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. doi: 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
  • 10
    • 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. doi: 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
  • 11
    • 70450223698 scopus 로고    scopus 로고
    • The plant Golgi apparatus: last 10 years of answered and open questions
    • Faso, C., Boulaflous, A., and Brandizzi, F. (2009). The plant Golgi apparatus: last 10 years of answered and open questions. FEBS Lett. 583, 3752-3757. doi: 10.1016/j.febslet.2009.09.046
    • (2009) FEBS Lett , vol.583 , pp. 3752-3757
    • Faso, C.1    Boulaflous, A.2    Brandizzi, F.3
  • 12
    • 38349014268 scopus 로고    scopus 로고
    • A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells
    • Ganley, I. G., Espinosa, E., and Pfeffer, S. R. (2008). A syntaxin 10-SNARE complex distinguishes two distinct transport routes from endosomes to the trans-Golgi in human cells. J. Cell Biol. 180, 159-172. doi: 10.1083/jcb.200707136
    • (2008) J. Cell Biol , vol.180 , pp. 159-172
    • Ganley, I.G.1    Espinosa, E.2    Pfeffer, S.R.3
  • 13
    • 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. doi: 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
  • 14
    • 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., 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. doi: 10.1083/jcb.200407088
    • (2004) J. Cell Biol , vol.167 , pp. 281-292
    • Gillingham, A.K.1    Tong, A.H.2    Boone, C.3    Munro, S.4
  • 15
    • 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. doi: 10.1101/cshperspect.a005215
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Glick, B.S.1    Luini, A.2
  • 16
    • 84931028263 scopus 로고    scopus 로고
    • Protein sorting at the trans-Golgi network
    • Guo, Y., Sirkis, D. W., and Schekman, R. (2014). Protein sorting at the trans-Golgi network. Annu. Rev. Cell Dev. Biol. 30, 169-206. doi: 10.1146/annurev-cellbio-100913-013012
    • (2014) Annu. Rev. Cell Dev. Biol , vol.30 , pp. 169-206
    • Guo, Y.1    Sirkis, D.W.2    Schekman, R.3
  • 17
    • 63049094599 scopus 로고    scopus 로고
    • Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi
    • Hayes, G. L., Brown, F. C., Haas, A. K., Nottingham, R. M., Barr, F. A., and Pfeffer, S. R. (2009). Multiple Rab GTPase binding sites in GCC185 suggest a model for vesicle tethering at the trans-Golgi. Mol. Biol. Cell 20, 209-217. doi: 10.1091/mbc.E08-07-0740
    • (2009) Mol. Biol. Cell , vol.20 , pp. 209-217
    • Hayes, G.L.1    Brown, F.C.2    Haas, A.K.3    Nottingham, R.M.4    Barr, F.A.5    Pfeffer, S.R.6
  • 18
    • 20544435937 scopus 로고    scopus 로고
    • Golgi structure in stress sensing and apoptosis
    • Hicks, S. W., and Machamer, C. E. (2005). Golgi structure in stress sensing and apoptosis. Biochim. Biophys. Acta 1744, 406-414. doi: 10.1016/j.bbamcr.2005.03.002
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 406-414
    • Hicks, S.W.1    Machamer, C.E.2
  • 19
    • 0033526005 scopus 로고    scopus 로고
    • GMAP-210, A cis-Golgi network-associated protein, is a minus end microtubule-binding protein
    • Infante, C., Ramos-Morales, F., Fedriani, C., Bornens, M., and Rios, R. M. (1999). GMAP-210, A cis-Golgi network-associated protein, is a minus end microtubule-binding protein. J. Cell Biol. 145, 83-98. doi: 10.1083/jcb.145.1.83
    • (1999) J. Cell Biol , vol.145 , pp. 83-98
    • Infante, C.1    Ramos-Morales, F.2    Fedriani, C.3    Bornens, M.4    Rios, R.M.5
  • 20
    • 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. doi: 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
  • 21
    • 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. doi: 10.1091/mbc.12.6.1811
    • (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
  • 22
    • 84953373631 scopus 로고    scopus 로고
    • Activation of ULK kinase and autophagy by GABARAP trafficking from the centrosome is regulated by WAC and GM130
    • Joachim, J., Jefferies, H. B., Razi, M., Frith, D., Snijders, A. P., Chakravarty, P., et al. (2015). Activation of ULK kinase and autophagy by GABARAP trafficking from the centrosome is regulated by WAC and GM130. Mol. Cell. 60, 899-913. doi: 10.1016/j.molcel.2015.11.018
    • (2015) Mol. Cell , vol.60 , pp. 899-913
    • Joachim, J.1    Jefferies, H.B.2    Razi, M.3    Frith, D.4    Snijders, A.P.5    Chakravarty, P.6
  • 23
    • 80054845829 scopus 로고    scopus 로고
    • Insertional mutation in the Golgb1 gene is associated with osteochondrodysplasia and systemic edema in the OCD rat
    • Katayama, K., Sasaki, T., Goto, S., Ogasawara, K., Maru, H., Suzuki, K., et al. (2011). Insertional mutation in the Golgb1 gene is associated with osteochondrodysplasia and systemic edema in the OCD rat. Bone 49, 1027-1036. doi: 10.1016/j.bone.2011.08.001
    • (2011) Bone , vol.49 , pp. 1027-1036
    • Katayama, K.1    Sasaki, T.2    Goto, S.3    Ogasawara, K.4    Maru, H.5    Suzuki, K.6
  • 24
    • 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. doi: 10.1101/cshperspect.a005181
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Klumperman, J.1
  • 25
    • 64149084265 scopus 로고    scopus 로고
    • GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization
    • Kodani, A., Kristensen, I., Huang, L., and Sütterlin, C. (2009). GM130-dependent control of Cdc42 activity at the Golgi regulates centrosome organization. Mol. Biol. Cell 20, 1192-1200. doi: 10.1091/mbc.E08-08-0834
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1192-1200
    • Kodani, A.1    Kristensen, I.2    Huang, L.3    Sütterlin, C.4
  • 26
    • 79951558394 scopus 로고    scopus 로고
    • Structural organization of the Golgi apparatus
    • Lowe, M. (2011). Structural organization of the Golgi apparatus. Curr. Opin. Cell Biol. 23, 85-93. doi: 10.1016/j.ceb.2010.10.004
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 85-93
    • Lowe, M.1
  • 27
    • 0032544440 scopus 로고    scopus 로고
    • Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis
    • Lowe, M., Rabouille, C., Nakamura, N., Watson, R., Jackman, M., Jämsä, E., et al. (1998). Cdc2 kinase directly phosphorylates the cis-Golgi matrix protein GM130 and is required for Golgi fragmentation in mitosis. Cell 94, 783-793. doi: 10.1016/S0092-8674(00)81737-7
    • (1998) Cell , vol.94 , pp. 783-793
    • Lowe, M.1    Rabouille, C.2    Nakamura, N.3    Watson, R.4    Jackman, M.5    Jämsä, E.6
  • 28
    • 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. doi: 10.1126/science.1108061
    • (2005) Science , vol.307 , pp. 1095-1098
    • Malsam, J.1    Satoh, A.2    Pelletier, L.3    Warren, G.4
  • 29
    • 79251476231 scopus 로고    scopus 로고
    • Reelin and stk25 have opposing roles in neuronal polarization and dendritic Golgi deployment
    • Matsuki, T., Matthews, R. T., Cooper, J. A., van der Brug, M. P., Cookson, M. R., Hardy, J. A., et al. (2010). Reelin and stk25 have opposing roles in neuronal polarization and dendritic Golgi deployment. Cell 143, 826-836. doi: 10.1016/j.cell.2010.10.029
    • (2010) Cell , vol.143 , pp. 826-836
    • Matsuki, T.1    Matthews, R.T.2    Cooper, J.A.3    van der Brug, M.P.4    Cookson, M.R.5    Hardy, J.A.6
  • 30
    • 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. doi: 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
  • 31
    • 0035794232 scopus 로고    scopus 로고
    • An essential cytoplasmic domain for the Golgi localization of coiled-coil proteins with a COOH-terminal membrane anchor
    • Misumi, Y., Sohda, M., Tashiro, A., Sato, H., and Ikehara, Y. (2001). An essential cytoplasmic domain for the Golgi localization of coiled-coil proteins with a COOH-terminal membrane anchor. J. Biol. Chem. 276, 6867-6873. doi: 10.1074/jbc.M010121200
    • (2001) J. Biol. Chem , vol.276 , pp. 6867-6873
    • Misumi, Y.1    Sohda, M.2    Tashiro, A.3    Sato, H.4    Ikehara, Y.5
  • 32
    • 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. doi: 10.1101/cshperspect.a005256
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Munro, S.1
  • 33
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., Lowe, M., Levine, T. P., Rabouille, C., and Warren, G. (1997). The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89, 445-455. doi: 10.1016/S0092-8674(00)80225-1
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 34
    • 20444393413 scopus 로고    scopus 로고
    • The golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization
    • Papoulas, O., Hays, T. S., and Sisson, J. C. (2005). The golgin Lava lamp mediates dynein-based Golgi movements during Drosophila cellularization. Nat. Cell Biol. 7, 612-618. doi: 10.1038/ncb1264
    • (2005) Nat. Cell Biol , vol.7 , pp. 612-618
    • Papoulas, O.1    Hays, T.S.2    Sisson, J.C.3
  • 35
    • 84930680961 scopus 로고    scopus 로고
    • Coordinated regulation of bidirectional COPI transport at the Golgi by CDC42
    • Park, S. Y., Yang, J. S., Schmider, A. B., Soberman, R. J., and Hsu, V. W. (2015). Coordinated regulation of bidirectional COPI transport at the Golgi by CDC42. Nature 521, 529-532. doi: 10.1038/nature14457
    • (2015) Nature , vol.521 , pp. 529-532
    • Park, S.Y.1    Yang, J.S.2    Schmider, A.B.3    Soberman, R.J.4    Hsu, V.W.5
  • 36
    • 79960279832 scopus 로고    scopus 로고
    • alpha-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding
    • Pranke, I. M., Morello, V., Bigay, J., Gibson, K., Verbavatz, J. M., Antonny, B., et al. (2013). alpha-Synuclein and ALPS motifs are membrane curvature sensors whose contrasting chemistry mediates selective vesicle binding. J. Cell Biol. 194, 89-103. doi: 10.1083/jcb.201011118
    • (2013) J. Cell Biol , vol.194 , pp. 89-103
    • Pranke, I.M.1    Morello, V.2    Bigay, J.3    Gibson, K.4    Verbavatz, J.M.5    Antonny, B.6
  • 37
    • 1842613600 scopus 로고    scopus 로고
    • YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta
    • Preisinger, C., Short, B., De Corte, V., Bruyneel, E., Haas, A., Kopajtich, R., et al. (2004). YSK1 is activated by the Golgi matrix protein GM130 and plays a role in cell migration through its substrate 14-3-3zeta. J. Cell Biol. 164, 1009-1020. doi: 10.1083/jcb.200310061
    • (2004) J. Cell Biol , vol.164 , pp. 1009-1020
    • Preisinger, C.1    Short, B.2    De Corte, V.3    Bruyneel, E.4    Haas, A.5    Kopajtich, R.6
  • 38
    • 4043107077 scopus 로고    scopus 로고
    • GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation
    • Ríos, R. M., Sanchís, A., Tassin, A. M., Fedriani, C., and Bornens, M. (2004). GMAP-210 recruits gamma-tubulin complexes to cis-Golgi membranes and is required for Golgi ribbon formation. Cell 118, 323-335. doi: 10.1016/j.cell.2004.07.012
    • (2004) Cell , vol.118 , pp. 323-335
    • Ríos, R.M.1    Sanchís, A.2    Tassin, A.M.3    Fedriani, C.4    Bornens, M.5
  • 39
    • 67349287493 scopus 로고    scopus 로고
    • Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130
    • Rivero, S., Cardenas, J., Bornens, M., and Rios, R. M. (2009). Microtubule nucleation at the cis-side of the Golgi apparatus requires AKAP450 and GM130. EMBO J. 28, 1016-1028. doi: 10.1038/emboj.2009.47
    • (2009) EMBO J , vol.28 , pp. 1016-1028
    • Rivero, S.1    Cardenas, J.2    Bornens, M.3    Rios, R.M.4
  • 40
    • 84928528013 scopus 로고    scopus 로고
    • The golgin GMAP-210 is required for efficient membrane trafficking in the early secretory pathway
    • Roboti, P., Sato, K., and Lowe, M. (2015). The golgin GMAP-210 is required for efficient membrane trafficking in the early secretory pathway. J. Cell Sci. 128, 1595-1606. doi: 10.1242/jcs.166710
    • (2015) J. Cell Sci , vol.128 , pp. 1595-1606
    • Roboti, P.1    Sato, K.2    Lowe, M.3
  • 41
    • 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. doi: 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
  • 42
    • 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. doi: 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
  • 43
    • 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. doi: 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
  • 44
    • 74849098404 scopus 로고    scopus 로고
    • Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210
    • Smits, P., Bolton, A. D., Funari, V., Hong, M., Boyden, E. D., Lu, L., et al. (2010). Lethal skeletal dysplasia in mice and humans lacking the golgin GMAP-210. N. Engl. J. Med. 362, 206-216. doi: 10.1056/NEJMoa0900158
    • (2010) N. Engl. J. Med , vol.362 , pp. 206-216
    • Smits, P.1    Bolton, A.D.2    Funari, V.3    Hong, M.4    Boyden, E.D.5    Lu, L.6
  • 45
    • 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. doi: 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
  • 46
    • 0035976927 scopus 로고    scopus 로고
    • Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin
    • Sohda, M., Misumi, Y., Yamamoto, A., Yano, A., Nakamura, N., and Ikehara, Y. (2001). Identification and characterization of a novel Golgi protein, GCP60, that interacts with the integral membrane protein giantin. J. Biol. Chem. 276, 45298-45306. doi: 10.1074/jbc.M108961200
    • (2001) J. Biol. Chem , vol.276 , pp. 45298-45306
    • Sohda, M.1    Misumi, Y.2    Yamamoto, A.3    Yano, A.4    Nakamura, N.5    Ikehara, Y.6
  • 47
    • 84875123474 scopus 로고    scopus 로고
    • Retrograde traffic from the Golgi to the endoplasmic reticulum
    • Spang, A. (2011). Retrograde traffic from the Golgi to the endoplasmic reticulum. Cold Spring Harb. Perspect. Biol. 5:a013391. doi: 10.1101/cshperspect.a013391
    • (2011) Cold Spring Harb. Perspect. Biol , vol.5
    • Spang, A.1
  • 49
    • 0022395805 scopus 로고
    • Organelle division and membrane traffic
    • Warren, G. (1985). Organelle division and membrane traffic. Trends Biochem. Sci. 10, 439-443. doi: 10.1016/0968-0004(85)90027-1
    • (1985) Trends Biochem. Sci , vol.10 , pp. 439-443
    • Warren, G.1
  • 50
    • 70349334137 scopus 로고    scopus 로고
    • Mitotic division of the mammalian Golgi apparatus
    • Wei, J. H., and Seemann, J. (2009). Mitotic division of the mammalian Golgi apparatus. Semin. Cell Dev. Biol. 20, 810-816. doi: 10.1016/j.semcdb.2009.03.010
    • (2009) Semin. Cell Dev. Biol , vol.20 , pp. 810-816
    • Wei, J.H.1    Seemann, J.2
  • 51
    • 84937250948 scopus 로고    scopus 로고
    • GM130 regulates golgi-derived spindle assembly by activating TPX2 and capturing microtubules
    • Wei, J. H., Zhang, Z. C., Wynn, R. M., and Seemann, J. (2015). GM130 regulates golgi-derived spindle assembly by activating TPX2 and capturing microtubules. Cell 162, 287-299. doi: 10.1016/j.cell.2015.06.014
    • (2015) Cell , vol.162 , pp. 287-299
    • Wei, J.H.1    Zhang, Z.C.2    Wynn, R.M.3    Seemann, J.4
  • 52
    • 84887478931 scopus 로고    scopus 로고
    • The Golgi puppet master: COG complex at center stage of membrane trafficking interactions
    • Willett, R., Ungar, D., and Lupashin, V. (2013). The Golgi puppet master: COG complex at center stage of membrane trafficking interactions. Histochem. Cell Biol. 140, 271-283. doi: 10.1007/s00418-013-1117-6
    • (2013) Histochem. Cell Biol , vol.140 , pp. 271-283
    • Willett, R.1    Ungar, D.2    Lupashin, V.3
  • 53
    • 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. doi: 10.1126/science.1256898
    • (2014) Science , vol.346
    • Wong, M.1    Munro, S.2
  • 54
    • 79958257226 scopus 로고    scopus 로고
    • New components of the Golgi matrix
    • Xiang, Y., and Wang, Y. (2011). New components of the Golgi matrix. Cell Tissue Res. 344, 365-379. doi: 10.1007/s00441-011-1166-x
    • (2011) Cell Tissue Res , vol.344 , pp. 365-379
    • Xiang, Y.1    Wang, Y.2
  • 56
    • 84864004215 scopus 로고    scopus 로고
    • Golgin160 recruits the dynein motor to position the Golgi apparatus
    • Yadav, S., Puthenveedu, M. A., and Linstedt, A. D. (2012). Golgin160 recruits the dynein motor to position the Golgi apparatus. Dev. Cell 23, 153-165. doi: 10.1016/j.devcel.2012.05.023
    • (2012) Dev. Cell , vol.23 , pp. 153-165
    • Yadav, S.1    Puthenveedu, M.A.2    Linstedt, A.D.3
  • 57
    • 33947729578 scopus 로고    scopus 로고
    • The mammalian Golgi regulates numb signaling in asymmetric cell division by releasing ACBD3 during mitosis
    • Zhou, Y., Atkins, J. B., Rompani, S. B., Bancescu, D. L., Petersen, P. H., Tang, H., et al. (2007). The mammalian Golgi regulates numb signaling in asymmetric cell division by releasing ACBD3 during mitosis. Cell 129, 163-178. doi: 10.1016/j.cell.2007.02.037
    • (2007) Cell , vol.129 , pp. 163-178
    • Zhou, Y.1    Atkins, J.B.2    Rompani, S.B.3    Bancescu, D.L.4    Petersen, P.H.5    Tang, H.6


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