메뉴 건너뛰기




Volumn 2, Issue JUN, 2014, Pages

Moonlighting functions of the NRZ (mammalian Dsl1) complex

Author keywords

Autophagy; CATCHR tether complex; Cell cycle; Endoplasmic reticulum; MRNA decay; NAG; RINT1; ZW10

Indexed keywords


EID: 84991982654     PISSN: None     EISSN: 2296634X     Source Type: Journal    
DOI: 10.3389/fcell.2014.00025     Document Type: Review
Times cited : (30)

References (108)
  • 1
    • 84885358006 scopus 로고    scopus 로고
    • Emerging role of the endoplasmic reticulum in peroxisome biogenesis
    • Agrawal, G., and Subramani, S. (2013). Emerging role of the endoplasmic reticulum in peroxisome biogenesis. Front. Physiol. 4:286. doi: 10.3389/fphys.2013.00286
    • (2013) Front. Physiol , vol.4 , pp. 286
    • Agrawal, G.1    Subramani, S.2
  • 2
    • 79955954056 scopus 로고    scopus 로고
    • Dhx34 and Nbas function in the NMD pathway and are required for embryonic development in zebrafish
    • Anastasaki, C., Longman, D., Capper, A., Patton, E. E., and Cáceres, J. F. (2011). Dhx34 and Nbas function in the NMD pathway and are required for embryonic development in zebrafish. Nucleic Acids Res. 39, 3686-3694. doi: 10.1093/nar/gkq1319
    • (2011) Nucleic Acids Res , vol.39 , pp. 3686-3694
    • Anastasaki, C.1    Longman, D.2    Capper, A.3    Patton, E.E.4    Cáceres, J.F.5
  • 3
    • 0035914416 scopus 로고    scopus 로고
    • The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast
    • Andag, U., Neumann, T., and Schmitt, H. D. (2001). The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast. J. Biol. Chem. 276, 39150-39160. doi: 10.1074/jbc.M105833200
    • (2001) J. Biol. Chem , vol.276 , pp. 39150-39160
    • Andag, U.1    Neumann, T.2    Schmitt, H.D.3
  • 4
    • 0347695021 scopus 로고    scopus 로고
    • Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat
    • Andag, U., and Schmitt, H. D. (2003). Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coat. J. Biol. Chem. 278, 51722-51734. doi: 10.1074/jbc.M308740200
    • (2003) J. Biol. Chem , vol.278 , pp. 51722-51734
    • Andag, U.1    Schmitt, H.D.2
  • 5
    • 66349116721 scopus 로고    scopus 로고
    • Identification of the neuroblastoma-amplified gene product as a component of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum retrograde transport
    • Aoki, T., Ichimura, S., Itoh, A., Kuramoto, M., Shinkawa, T., Isobe, T., et al. (2009). Identification of the neuroblastoma-amplified gene product as a component of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum retrograde transport. Mol. Biol. Cell 20, 2639-2649. doi: 10.1091/mbc.E08-11-1104
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2639-2649
    • Aoki, T.1    Ichimura, S.2    Itoh, A.3    Kuramoto, M.4    Shinkawa, T.5    Isobe, T.6
  • 6
    • 39749131549 scopus 로고    scopus 로고
    • Sec22b-dependent assembly of endoplasmic reticulum Q-SNARE proteins
    • Aoki, T., Kojima, M., Tani, K., and Tagaya, M. (2008). Sec22b-dependent assembly of endoplasmic reticulum Q-SNARE proteins. Biochem. J. 410, 93-100. doi: 10.1042/BJ20071304
    • (2008) Biochem. J , vol.410 , pp. 93-100
    • Aoki, T.1    Kojima, M.2    Tani, K.3    Tagaya, M.4
  • 7
    • 84884475631 scopus 로고    scopus 로고
    • A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex
    • Arasaki, K., Takagi, D., Furuno, A., Sohda, M., Misumi, Y., Wakana, Y., et al. (2013). A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex. Mol. Biol. Cell 24, 2907-2917. doi: 10.1091/mbc.E13-01-0014
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2907-2917
    • Arasaki, K.1    Takagi, D.2    Furuno, A.3    Sohda, M.4    Misumi, Y.5    Wakana, Y.6
  • 8
    • 33744768658 scopus 로고    scopus 로고
    • RINT-1 regulates the localization and entry of ZW10 to the syntaxin 18 complex
    • Arasaki, K., Taniguchi, M., Tani, K., and Tagaya, M. (2006). RINT-1 regulates the localization and entry of ZW10 to the syntaxin 18 complex. Mol. Biol. Cell 17, 2780-2788. doi: 10.1091/mbc.E05-10-0973
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2780-2788
    • Arasaki, K.1    Taniguchi, M.2    Tani, K.3    Tagaya, M.4
  • 9
    • 34250170864 scopus 로고    scopus 로고
    • Correlation of Golgi localization of ZW10 and centrosomal accumulation of dynactin
    • Arasaki, K., Uemura, T., Tani, K., and Tagaya, M. (2007). Correlation of Golgi localization of ZW10 and centrosomal accumulation of dynactin. Biochem. Biophys. Res. Commun. 359, 811-816. doi: 10.1016/j.bbrc.2007.05.188
    • (2007) Biochem. Biophys. Res. Commun , vol.359 , pp. 811-816
    • Arasaki, K.1    Uemura, T.2    Tani, K.3    Tagaya, M.4
  • 10
    • 0033662264 scopus 로고    scopus 로고
    • Rough deal and Zw10 are required for the metaphase checkpoint in Drosophila
    • Basto, R., Gomes, R., and Karess, R. E. (2000). Rough deal and Zw10 are required for the metaphase checkpoint in Drosophila. Nat. Cell Biol. 2, 939-943. doi: 10.1038/35046592
    • (2000) Nat. Cell Biol , vol.2 , pp. 939-943
    • Basto, R.1    Gomes, R.2    Karess, R.E.3
  • 11
    • 0346335796 scopus 로고    scopus 로고
    • In vivo dynamics of the rough deal checkpoint protein during Drosophila mitosis
    • Basto, R., Scaerou, F., Mische, S., Wojcik, E., Lefebvre, C., Gomes, R., et al. (2004). In vivo dynamics of the rough deal checkpoint protein during Drosophila mitosis. Curr. Biol. 14, 56-61. doi: 10.1016/j.cub.2003.12.025
    • (2004) Curr. Biol , vol.14 , pp. 56-61
    • Basto, R.1    Scaerou, F.2    Mische, S.3    Wojcik, E.4    Lefebvre, C.5    Gomes, R.6
  • 12
    • 79953071205 scopus 로고    scopus 로고
    • The FRA2C common fragile site maps to the borders of MYCN amplicons in neuroblastoma and is associated with gross chromosomal rearrangements in different cancers
    • Blumrich, A., Zapatka, M., Brueckner, L. M., Zheglo, D., Schwab, M., and Savelyeva, L. (2011). The FRA2C common fragile site maps to the borders of MYCN amplicons in neuroblastoma and is associated with gross chromosomal rearrangements in different cancers. Hum. Mol. Genet. 20, 1488-1501. doi: 10.1093/hmg/ddr027
    • (2011) Hum. Mol. Genet , vol.20 , pp. 1488-1501
    • Blumrich, A.1    Zapatka, M.2    Brueckner, L.M.3    Zheglo, D.4    Schwab, M.5    Savelyeva, L.6
  • 13
    • 79952401083 scopus 로고    scopus 로고
    • A Nup133-dependent NPC-anchored network tethers centrosomes to the nuclear envelope in prophase
    • Bolhy, S., Bouhlel, I., Dultz, E., Nayak, T., Zuccolo, M., Gatti, X., et al. (2011). A Nup133-dependent NPC-anchored network tethers centrosomes to the nuclear envelope in prophase. J. Cell Biol. 192, 855-871. doi: 10.1083/jcb.201007118
    • (2011) J. Cell Biol , vol.192 , pp. 855-871
    • Bolhy, S.1    Bouhlel, I.2    Dultz, E.3    Nayak, T.4    Zuccolo, M.5    Gatti, X.6
  • 14
    • 79952103459 scopus 로고    scopus 로고
    • Transport according to GARP: receiving retrograde cargo at the trans-Golgi network
    • Bonifacino, J. S., and Hierro, A. (2011). Transport according to GARP: receiving retrograde cargo at the trans-Golgi network. Trends Cell Biol. 21, 159-167. doi: 10.1016/j.tcb.2010.11.003
    • (2011) Trends Cell Biol , vol.21 , pp. 159-167
    • Bonifacino, J.S.1    Hierro, A.2
  • 15
    • 78149306025 scopus 로고    scopus 로고
    • Multisubunit tethering complexes and their role in membrane fusion
    • Bröker, C., Engelbrecht-Vandé, S., and Ungermann, C. (2010). Multisubunit tethering complexes and their role in membrane fusion. Curr. Biol. 20, R943-R952. doi: 10.1016/j.cub.2010.09.015
    • (2010) Curr. Biol , vol.20 , pp. R943-R952
    • Bröker, C.1    Engelbrecht-Vandé, S.2    Ungermann, C.3
  • 16
    • 78650138725 scopus 로고    scopus 로고
    • An update on transport vesicle tethering
    • Brown, F. C., and Pfeffer, S. R. (2010). An update on transport vesicle tethering. Mol. Membr. Biol. 27, 457-461. doi: 10.3109/09687688.2010.501765
    • (2010) Mol. Membr. Biol , vol.27 , pp. 457-461
    • Brown, F.C.1    Pfeffer, S.R.2
  • 17
    • 18844449387 scopus 로고    scopus 로고
    • Recruitment of MAD2 to the kinetochore requires the Rod/Zw10 complex
    • Buffin, E., Lefebvre, C., Huang, J., Gagou, M. E., and Karess, R. E. (2005). Recruitment of MAD2 to the kinetochore requires the Rod/Zw10 complex. Curr. Biol. 15, 856-861. doi: 10.1016/j.cub.2005.03.052
    • (2005) Curr. Biol , vol.15 , pp. 856-861
    • Buffin, E.1    Lefebvre, C.2    Huang, J.3    Gagou, M.E.4    Karess, R.E.5
  • 18
    • 0033672239 scopus 로고    scopus 로고
    • Human Zw10 and ROD are mitotic checkpoint proteins that bind to kinetochores
    • Chan, G. K. T., Jablonski, S. A., Starr, D. A., Goldberg, M. L., and Yen, T. J. (2000). Human Zw10 and ROD are mitotic checkpoint proteins that bind to kinetochores. Nat. Cell Biol. 2, 944-947. doi: 10.1038/35046598
    • (2000) Nat. Cell Biol , vol.2 , pp. 944-947
    • Chan, G.K.T.1    Jablonski, S.A.2    Starr, D.A.3    Goldberg, M.L.4    Yen, T.J.5
  • 19
    • 34247197937 scopus 로고    scopus 로고
    • The nonsense-mediated decay RNA surveillance pathway
    • Chang, Y. F., Imam, J. S., and Wilkinson, M. F. (2007). The nonsense-mediated decay RNA surveillance pathway. Annu. Rev. Biochem. 76, 51-74. doi: 10.1146/annurev.biochem.76.050106.093909
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 51-74
    • Chang, Y.F.1    Imam, J.S.2    Wilkinson, M.F.3
  • 20
    • 77952613898 scopus 로고    scopus 로고
    • Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery
    • Civril, F., Wehenkel, A., Giorgi, F. M., Santaguida, S., Di Fonzo, A., Grigorean, G., et al. (2010). Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery. Structure 18, 616-626. doi: 10.1016/j.str.2010.02.014
    • (2010) Structure , vol.18 , pp. 616-626
    • Civril, F.1    Wehenkel, A.2    Giorgi, F.M.3    Santaguida, S.4    Di Fonzo, A.5    Grigorean, G.6
  • 21
    • 84862324402 scopus 로고    scopus 로고
    • Moonlighting is mainstream: paradigm adjustment required
    • Copley, S. D. (2012). Moonlighting is mainstream: paradigm adjustment required. Bioessays 34, 578-588. doi: 10.1002/bies.201100191
    • (2012) Bioessays , vol.34 , pp. 578-588
    • Copley, S.D.1
  • 22
    • 79960133821 scopus 로고    scopus 로고
    • The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae
    • Diefenbacher, M., Thorsteinsdottir, H., and Spang, A. (2011). The Dsl1 tethering complex actively participates in soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor (SNARE) complex assembly at the endoplasmic reticulum in Saccharomyces cerevisiae. J. Biol. Chem. 286, 25027-25038. doi: 10.1074/jbc.M110.215657
    • (2011) J. Biol. Chem , vol.286 , pp. 25027-25038
    • Diefenbacher, M.1    Thorsteinsdottir, H.2    Spang, A.3
  • 23
    • 0029913484 scopus 로고    scopus 로고
    • Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis
    • Echeverri, C. J., Paschal, B. M., Vaughan, K. T., and Vallee, R. B. (1996). Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis. J. Cell Biol. 132, 617-633. doi: 10.1083/jcb.132.4.617
    • (1996) J. Cell Biol , vol.132 , pp. 617-633
    • Echeverri, C.J.1    Paschal, B.M.2    Vaughan, K.T.3    Vallee, R.B.4
  • 24
    • 39049107627 scopus 로고    scopus 로고
    • Stable hZW10 kinetochore residency, mediated by hZwint-1 interaction, is essential for the mitotic checkpoint
    • Famulski, J. K., Vos, L., Sun, X., and Chan, G. (2008). Stable hZW10 kinetochore residency, mediated by hZwint-1 interaction, is essential for the mitotic checkpoint. J. Cell Biol. 180, 507-520. doi: 10.1083/jcb.200708021
    • (2008) J. Cell Biol , vol.180 , pp. 507-520
    • Famulski, J.K.1    Vos, L.2    Sun, X.3    Chan, G.4
  • 25
    • 79551554157 scopus 로고    scopus 로고
    • Dynein/Dynactin-mediated transport of kinetochore components off kinetochores and onto spindle poles induced by nordihydroguaiaretic acid
    • Famulski, J. K., Vos, L. J., Rattner, J. B., and Chan, G. K. (2011). Dynein/Dynactin-mediated transport of kinetochore components off kinetochores and onto spindle poles induced by nordihydroguaiaretic acid. PLoS ONE 6:16494. doi: 10.1371/journal.pone.0016494
    • (2011) PLoS ONE , vol.6 , pp. 16494
    • Famulski, J.K.1    Vos, L.J.2    Rattner, J.B.3    Chan, G.K.4
  • 26
    • 84876476422 scopus 로고    scopus 로고
    • Beclin-1 is required for chromosome congression and proper outer kinetochore assembly
    • Frémont, S., Gérard, A., Galloux, M., Janvier, K., Karess, R. E., and Berlioz-Torrent, C. (2013). Beclin-1 is required for chromosome congression and proper outer kinetochore assembly. EMBO Rep. 14, 364-372. doi: 10.1038/embor.2013.23
    • (2013) EMBO Rep , vol.14 , pp. 364-372
    • Frémont, S.1    Gérard, A.2    Galloux, M.3    Janvier, K.4    Karess, R.E.5    Berlioz-Torrent, C.6
  • 27
    • 33749134437 scopus 로고    scopus 로고
    • DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation
    • Fuller-Pace, F. V. (2006). DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res. 34, 4206-4215. doi: 10.1093/nar/gkl460
    • (2006) Nucleic Acids Res , vol.34 , pp. 4206-4215
    • Fuller-Pace, F.V.1
  • 28
    • 77951875761 scopus 로고    scopus 로고
    • Removal of Spindly from microtubule-attached kinetochores controls spindle checkpoint silencing in human cells
    • Gassmann, R., Holland, A. J., Varma, D., Wan, X., Civril, F., Cleveland, D. W., et al. (2010). Removal of Spindly from microtubule-attached kinetochores controls spindle checkpoint silencing in human cells. Genes Dev. 24, 957-971. doi: 10.1101/gad.1886810
    • (2010) Genes Dev , vol.24 , pp. 957-971
    • Gassmann, R.1    Holland, A.J.2    Varma, D.3    Wan, X.4    Civril, F.5    Cleveland, D.W.6
  • 29
    • 84891817822 scopus 로고    scopus 로고
    • SIP30 is required for neuropathic pain-evoked aversion in rats
    • Han, M., Xiao, X., Yang, Y., Huang, R. Y., Cao, H., Zhao, Z. Q., et al. (2014). SIP30 is required for neuropathic pain-evoked aversion in rats. J. Neurosci. 34, 346-355. doi: 10.1523/JNEUROSCI.3160-13.2014
    • (2014) J. Neurosci , vol.34 , pp. 346-355
    • Han, M.1    Xiao, X.2    Yang, Y.3    Huang, R.Y.4    Cao, H.5    Zhao, Z.Q.6
  • 30
    • 0034607967 scopus 로고    scopus 로고
    • Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking
    • Hatsuzawa, K., Hirose, H., Tani, K., Yamamoto, A., Scheller, R. H., and Tagaya, M. (2000). Syntaxin 18, a SNAP receptor that functions in the endoplasmic reticulum, intermediate compartment, and cis-Golgi vesicle trafficking. J. Biol. Chem. 275, 13713-13720. doi: 10.1074/jbc.275.18.13713
    • (2000) J. Biol. Chem , vol.275 , pp. 13713-13720
    • Hatsuzawa, K.1    Hirose, H.2    Tani, K.3    Yamamoto, A.4    Scheller, R.H.5    Tagaya, M.6
  • 31
    • 84885175531 scopus 로고    scopus 로고
    • PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex
    • He, S., Ni, D., Ma, B., Lee, J.-H., Zhang, T., Ghozalli, I., et al. (2013). PtdIns(3)P-bound UVRAG coordinates Golgi-ER retrograde and Atg9 transport by differential interactions with the ER tether and the beclin 1 complex. Nat. Cell Biol. 15, 1206-1219. doi: 10.1038/ncb2848
    • (2013) Nat. Cell Biol , vol.15 , pp. 1206-1219
    • He, S.1    Ni, D.2    Ma, B.3    Lee, J.-H.4    Zhang, T.5    Ghozalli, I.6
  • 32
    • 11144354092 scopus 로고    scopus 로고
    • Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi
    • Hirose, H., Arasaki, K., Dohmae, N., Takio, K., Hatsuzawa, K., Nagahama, M., et al. (2004). Implication of ZW10 in membrane trafficking between the endoplasmic reticulum and Golgi. EMBO J. 23, 1267-1278. doi: 10.1038/sj.emboj.7600135
    • (2004) EMBO J , vol.23 , pp. 1267-1278
    • Hirose, H.1    Arasaki, K.2    Dohmae, N.3    Takio, K.4    Hatsuzawa, K.5    Nagahama, M.6
  • 33
    • 84890884015 scopus 로고    scopus 로고
    • Tetherig the assembly of SNARE complexes
    • Hong, W., and Lev, S. (2014). Tetherig the assembly of SNARE complexes. Trends Cell Biol. 24, 35-43. doi: 10.1016/j.tcb.2013.09.006
    • (2014) Trends Cell Biol , vol.24 , pp. 35-43
    • Hong, W.1    Lev, S.2
  • 34
    • 0035945356 scopus 로고    scopus 로고
    • Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation
    • Howell, B. J., McEwen, B. F., Canman, J. C., Hoffman, D. B., Farrar, E. M., Rieder, C. L., et al. (2001). Cytoplasmic dynein/dynactin drives kinetochore protein transport to the spindle poles and has a role in mitotic spindle checkpoint inactivation. J. Cell Biol. 155, 1159-1172. doi: 10.1083/jcb.200105093
    • (2001) J. Cell Biol , vol.155 , pp. 1159-1172
    • Howell, B.J.1    McEwen, B.F.2    Canman, J.C.3    Hoffman, D.B.4    Farrar, E.M.5    Rieder, C.L.6
  • 35
    • 77951819088 scopus 로고    scopus 로고
    • Systematic analysis of human protein complexes identifies chromosome segregation proteins
    • Hutchins, J. R., Toyoda, Y., Hegemann, B., Poser, I., Hériché, J. K., Sykora, M. M., et al. (2010). Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science 328, 593-599. doi: 10.1126/science.1181348
    • (2010) Science , vol.328 , pp. 593-599
    • Hutchins, J.R.1    Toyoda, Y.2    Hegemann, B.3    Poser, I.4    Hériché, J.K.5    Sykora, M.M.6
  • 36
    • 48649088279 scopus 로고    scopus 로고
    • N-terminal region of ZW10 serves not only as a determinant for localization but also as a link with dynein function
    • Inoue, M., Arasaki, K., Ueda, A., Aoki, T., and Tagaya, M. (2008). N-terminal region of ZW10 serves not only as a determinant for localization but also as a link with dynein function. Genes Cells 13, 905-914. doi: 10.1111/j.1365-2443.2008.01215.x
    • (2008) Genes Cells , vol.13 , pp. 905-914
    • Inoue, M.1    Arasaki, K.2    Ueda, A.3    Aoki, T.4    Tagaya, M.5
  • 37
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura, E., Kishi, C., Inoue, K., and Mizushima, N. (2008). Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol. Biol. Cell 19, 5360-5372. doi: 10.1091/mbc.E08-01-0080
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 38
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • Jeffery, C. J. (1999). Moonlighting proteins. Trends Biochem. Sci. 24, 8-11. doi: 10.1016/S0968-0004(98)01335-8
    • (1999) Trends Biochem. Sci , vol.24 , pp. 8-11
    • Jeffery, C.J.1
  • 39
    • 33846427327 scopus 로고    scopus 로고
    • Relationship of DDX1 and NAG gene amplification/overexpression to the prognosis of patients with MYCN-amplified neuroblastoma
    • Kaneko, S., Ohira, M., Nakamura, Y., Isogai, E., Nakagawara, A., and Kaneko, M. (2007). Relationship of DDX1 and NAG gene amplification/overexpression to the prognosis of patients with MYCN-amplified neuroblastoma. J. Cancer Res. Clin. Oncol. 133, 185-192. doi: 10.1007/s00432-006-0156-y
    • (2007) J. Cancer Res. Clin. Oncol , vol.133 , pp. 185-192
    • Kaneko, S.1    Ohira, M.2    Nakamura, Y.3    Isogai, E.4    Nakagawara, A.5    Kaneko, M.6
  • 40
    • 21744436611 scopus 로고    scopus 로고
    • Rod-Zw10-Zwilch: a key player in the spindle checkpoint
    • Karess, R. (2005). Rod-Zw10-Zwilch: a key player in the spindle checkpoint. Trends Cell Biol. 15, 386-392. doi: 10.1016/j.tcb.2005.05.003
    • (2005) Trends Cell Biol , vol.15 , pp. 386-392
    • Karess, R.1
  • 41
    • 0024799096 scopus 로고
    • Rough deal: a gene required for proper mitotic segregation in Drosophila
    • Karess, R. E., and Glover, D. M. (1989). Rough deal: a gene required for proper mitotic segregation in Drosophila. J. Cell Biol. 1109, 2951-2961. doi: 10.1083/jcb.109.6.2951
    • (1989) J. Cell Biol , vol.1109 , pp. 2951-2961
    • Karess, R.E.1    Glover, D.M.2
  • 42
    • 33645985136 scopus 로고    scopus 로고
    • The Rb-related p130 protein controls telomere lengthening through an interaction with a Rad50-interacting protein, RINT-1
    • Kong, L. J., Meloni, A. R., and Nevins, J. R. (2006). The Rb-related p130 protein controls telomere lengthening through an interaction with a Rad50-interacting protein, RINT-1. Mol. Cell 22, 63-71. doi: 10.1016/j.molcel.2006.02.016
    • (2006) Mol. Cell , vol.22 , pp. 63-71
    • Kong, L.J.1    Meloni, A.R.2    Nevins, J.R.3
  • 43
    • 17644396387 scopus 로고    scopus 로고
    • ZW10 links mitotic checkpoint signaling to the structural kinetochore
    • Kops, G. J., Kim, Y., Weaver, B. A., Mao, Y., McLeod, I., Yates, J. R. 3rd., et al. (2005). ZW10 links mitotic checkpoint signaling to the structural kinetochore. J. Cell Biol. 169, 49-60. doi: 10.1083/jcb.200411118
    • (2005) J. Cell Biol , vol.169 , pp. 49-60
    • Kops, G.J.1    Kim, Y.2    Weaver, B.A.3    Mao, Y.4    McLeod, I.5    Yates, J.R.6
  • 44
    • 24344480456 scopus 로고    scopus 로고
    • Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast
    • Kraynack, B. A., Chan, A., Rosenthal, E., Essid, M., Umansky, B., Waters, M. G., et al. (2005). Dsl1p, Tip20p, and the novel Dsl3(Sec39) protein are required for the stability of the Q/t-SNARE complex at the endoplasmic reticulum in yeast. Mol. Biol. Cell 16, 3963-3977. doi: 10.1091/mbc.E05-01-0056
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3963-3977
    • Kraynack, B.A.1    Chan, A.2    Rosenthal, E.3    Essid, M.4    Umansky, B.5    Waters, M.G.6
  • 45
    • 84888380983 scopus 로고    scopus 로고
    • The autophagosome: origins unknown, biogenesis complex
    • Lamb, C. A., Yoshimori, T., and Tooze, S. A. (2013). The autophagosome: origins unknown, biogenesis complex. Nat. Rev. Mol. Cell Biol. 14, 759-774. doi: 10.1038/nrm3696
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 759-774
    • Lamb, C.A.1    Yoshimori, T.2    Tooze, S.A.3
  • 46
    • 80052572363 scopus 로고    scopus 로고
    • The COG complex interacts directly with syntaxin 6 and positively regulates endosome-to-TGN retrograde transport
    • Laufman, O., Hong, W., and Lev, S. (2011). The COG complex interacts directly with syntaxin 6 and positively regulates endosome-to-TGN retrograde transport. J. Cell Biol. 194, 459-472. doi: 10.1083/jcb.201102045
    • (2011) J. Cell Biol , vol.194 , pp. 459-472
    • Laufman, O.1    Hong, W.2    Lev, S.3
  • 47
    • 84877912314 scopus 로고    scopus 로고
    • The COG complex interacts with multiple Golgi SNAREs and enhances fusogenic assembly of SNARE complexes
    • Laufman, O., Hong, W., and Lev, S. (2013). The COG complex interacts with multiple Golgi SNAREs and enhances fusogenic assembly of SNARE complexes. J. Cell Sci. 126, 1506-1516. doi: 10.1242/jcs.122101
    • (2013) J. Cell Sci , vol.126 , pp. 1506-1516
    • Laufman, O.1    Hong, W.2    Lev, S.3
  • 48
    • 67651166603 scopus 로고    scopus 로고
    • Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing
    • Laufman, O., Kedan, A., Hong, W., and Lev, S. (2009). Direct interaction between the COG complex and the SM protein, Sly1, is required for Golgi SNARE pairing. EMBO J. 28, 2006-2017. doi: 10.1038/emboj.2009.168
    • (2009) EMBO J , vol.28 , pp. 2006-2017
    • Laufman, O.1    Kedan, A.2    Hong, W.3    Lev, S.4
  • 49
    • 0036312094 scopus 로고    scopus 로고
    • Identification of a novel SNAP25 interacting protein (SIP30)
    • Lee, H. K., Safieddine, S., Petralia, R. S., and Wenthold, R. J. (2002). Identification of a novel SNAP25 interacting protein (SIP30). J. Neurochem. 81, 1338-1347. doi: 10.1046/j.1471-4159.2002.00937.x
    • (2002) J. Neurochem , vol.81 , pp. 1338-1347
    • Lee, H.K.1    Safieddine, S.2    Petralia, R.S.3    Wenthold, R.J.4
  • 50
    • 84876670115 scopus 로고    scopus 로고
    • Silencing of nicotiana benthamiana neuroblastoma-amplified gene causes ER stress and cell death
    • Lee, J. Y., Sarowar, S., Kim, H. S., Kim, H., Hwang, I., Kim, Y. J., et al. (2013). Silencing of nicotiana benthamiana neuroblastoma-amplified gene causes ER stress and cell death. BMC Plant Biol. 13:69. doi: 10.1186/1471-2229-13-69
    • (2013) BMC Plant Biol , vol.13 , pp. 69
    • Lee, J.Y.1    Sarowar, S.2    Kim, H.S.3    Kim, H.4    Hwang, I.5    Kim, Y.J.6
  • 51
    • 84889085029 scopus 로고    scopus 로고
    • MAG2 and three MAG2-INTERACTING PROTEINs form an ER-localized complex to facilitate storage protein transport in Arabidopsis thaliana
    • Li, L., Shimada, T., Takahashi, H., Koumoto, Y., Shirakawa, M., Takagi, J., et al. (2013). MAG2 and three MAG2-INTERACTING PROTEINs form an ER-localized complex to facilitate storage protein transport in Arabidopsis thaliana. Plant J. 76, 781-791. doi: 10.1111/tpj.12347
    • (2013) Plant J , vol.76 , pp. 781-791
    • Li, L.1    Shimada, T.2    Takahashi, H.3    Koumoto, Y.4    Shirakawa, M.5    Takagi, J.6
  • 52
    • 33947514836 scopus 로고    scopus 로고
    • MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana
    • Li, L., Shimada, T., Takahashi, H., Ueda, H., Fukao, Y., Kondo, M., et al. (2006). MAIGO2 is involved in exit of seed storage proteins from the endoplasmic reticulum in Arabidopsis thaliana. Plant Cell 18, 3535-3547. doi: 10.1105/tpc.106.046151
    • (2006) Plant Cell , vol.18 , pp. 3535-3547
    • Li, L.1    Shimada, T.2    Takahashi, H.3    Ueda, H.4    Fukao, Y.5    Kondo, M.6
  • 53
    • 33745751085 scopus 로고    scopus 로고
    • Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
    • Liang, C., Feng, P., Ku, B., Dotan, I., Canaani, D., Oh, B. H., et al. (2006). Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG. Nat. Cell Biol. 8, 688-699. doi: 10.1038/ncb1426
    • (2006) Nat. Cell Biol , vol.8 , pp. 688-699
    • Liang, C.1    Feng, P.2    Ku, B.3    Dotan, I.4    Canaani, D.5    Oh, B.H.6
  • 54
    • 46449120732 scopus 로고    scopus 로고
    • Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking
    • Liang, C., Lee, J. S., Inn, K. S., Gack, M. U., Li, Q., Roberts, E. A., et al. (2008). Beclin1-binding UVRAG targets the class C Vps complex to coordinate autophagosome maturation and endocytic trafficking. Nat. Cell Biol. 10, 776-787. doi: 10.1038/ncb1740
    • (2008) Nat. Cell Biol , vol.10 , pp. 776-787
    • Liang, C.1    Lee, J.S.2    Inn, K.S.3    Gack, M.U.4    Li, Q.5    Roberts, E.A.6
  • 55
    • 34347329213 scopus 로고    scopus 로고
    • RINT-1 serves as a tumor suppressor and maintains Golgi dynamics and centrosome integrity for cell survival
    • Lin, X., Liu, C. C., Gao, Q., Zhang, X., Wu, G., and Lee, W. H. (2007). RINT-1 serves as a tumor suppressor and maintains Golgi dynamics and centrosome integrity for cell survival. Mol. Cell. Biol. 27, 4905-4916. doi: 10.1128/MCB.02396-06
    • (2007) Mol. Cell. Biol , vol.27 , pp. 4905-4916
    • Lin, X.1    Liu, C.C.2    Gao, Q.3    Zhang, X.4    Wu, G.5    Lee, W.H.6
  • 56
    • 84884935892 scopus 로고    scopus 로고
    • DHX34 and NBAS form part of an autoregulatory NMD circuit that regulates endogenous RNA targets in human cells, zebrafish and Caenorhabditis elegans
    • Longman, D., Hug, N., Keith, M., Anastasaki, C., Patton, E. E., Grimes, G., et al. (2013). DHX34 and NBAS form part of an autoregulatory NMD circuit that regulates endogenous RNA targets in human cells, zebrafish and Caenorhabditis elegans. Nucleic Acids Res. 41, 8319-8331. doi: 10.1093/nar/gkt585
    • (2013) Nucleic Acids Res , vol.41 , pp. 8319-8331
    • Longman, D.1    Hug, N.2    Keith, M.3    Anastasaki, C.4    Patton, E.E.5    Grimes, G.6
  • 57
    • 34247556560 scopus 로고    scopus 로고
    • Mechanistic insights and identification of two novel factors in the C. elegans NMD pathway
    • Longman, D., Plasterk, R. H., Johnstone, I. L., and Cáceres, J. F. (2007). Mechanistic insights and identification of two novel factors in the C. elegans NMD pathway. Genes Dev. 21, 1075-1085. doi: 10.1101/gad.417707
    • (2007) Genes Dev , vol.21 , pp. 1075-1085
    • Longman, D.1    Plasterk, R.H.2    Johnstone, I.L.3    Cáceres, J.F.4
  • 58
    • 84899940450 scopus 로고    scopus 로고
    • Distinct sets of Rab6 effectors contribute to ZW10-and COG-dependent Golgi homeostasis
    • Majeed, W., Liu, S., and Storrie, B. (2014). Distinct sets of Rab6 effectors contribute to ZW10-and COG-dependent Golgi homeostasis. Traffic. 15, 630-647. doi: 10.1111/tra.12167
    • (2014) Traffic , vol.15 , pp. 630-647
    • Majeed, W.1    Liu, S.2    Storrie, B.3
  • 59
    • 77956130441 scopus 로고    scopus 로고
    • Neuroblastoma amplified sequence gene is associated with a novel short stature syndrome characterised by optic nerve atrophy and Pelger-Huët anomaly
    • Maksimova, N., Hara, K., Nikolaeva, I., Chun-Feng, T., Usui, T., Takagi, M., et al. (2010). Neuroblastoma amplified sequence gene is associated with a novel short stature syndrome characterised by optic nerve atrophy and Pelger-Huët anomaly. J. Med. Genet. 47, 538-548. doi: 10.1136/jmg.2009.074815
    • (2010) J. Med. Genet , vol.47 , pp. 538-548
    • Maksimova, N.1    Hara, K.2    Nikolaeva, I.3    Chun-Feng, T.4    Usui, T.5    Takagi, M.6
  • 60
    • 0037128205 scopus 로고    scopus 로고
    • Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform
    • Mallard, F., Tang, B. L., Galli, T., Tenza, D., Saint-Pol, A., Yue, X., et al. (2002). Early/recycling endosomes-to-TGN transport involves two SNARE complexes and a Rab6 isoform. J. Cell Biol. 156, 653-664. doi: 10.1083/jcb.200110081
    • (2002) J. Cell Biol , vol.156 , pp. 653-664
    • Mallard, F.1    Tang, B.L.2    Galli, T.3    Tenza, D.4    Saint-Pol, A.5    Yue, X.6
  • 61
    • 79960118861 scopus 로고    scopus 로고
    • The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation
    • Meiringer, C. T., Rethmeier, R., Auffarth, K., Wilson, J., Perz, A., Barlowe, C., et al. (2011). The Dsl1 protein tethering complex is a resident endoplasmic reticulum complex, which interacts with five soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptors (SNAREs): implications for fusion and fusion regulation. J. Biol. Chem. 286, 25039-25046. doi: 10.1074/jbc.M110.215327
    • (2011) J. Biol. Chem , vol.286 , pp. 25039-25046
    • Meiringer, C.T.1    Rethmeier, R.2    Auffarth, K.3    Wilson, J.4    Perz, A.5    Barlowe, C.6
  • 62
    • 3142536716 scopus 로고    scopus 로고
    • Exploration of essential gene functions via titratable promoter alleles
    • Mnaimneh, S., Davierwala, A. P., Haynes, J., Moffat, J., Peng, W. T., Zhang, W., et al. (2004). Exploration of essential gene functions via titratable promoter alleles. Cell 118, 31-34. doi: 10.1016/j.cell.2004.06.013
    • (2004) Cell , vol.118 , pp. 31-34
    • Mnaimneh, S.1    Davierwala, A.P.2    Haynes, J.3    Moffat, J.4    Peng, W.T.5    Zhang, W.6
  • 63
    • 73549108735 scopus 로고    scopus 로고
    • Divide et impera: the dictum of peroxisomes
    • Nagotu, S., Veenhuis, M., and van der Klei, I. J. (2010). Divide et impera: the dictum of peroxisomes. Traffic 11, 175-184. doi: 10.1111/j.1600-0854.2009.01019.x
    • (2010) Traffic , vol.11 , pp. 175-184
    • Nagotu, S.1    Veenhuis, M.2    van der Klei, I.J.3
  • 64
    • 4444304199 scopus 로고    scopus 로고
    • Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion
    • Nakajima, K., Hirose, H., Taniguchi, M., Kurashina, H., Arasaki, K., Nagahama, M., et al. (2004). Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane fusion. EMBO J. 23, 3216-3226. doi: 10.1038/sj.emboj.7600333
    • (2004) EMBO J , vol.23 , pp. 3216-3226
    • Nakajima, K.1    Hirose, H.2    Taniguchi, M.3    Kurashina, H.4    Arasaki, K.5    Nagahama, M.6
  • 65
    • 25444466999 scopus 로고    scopus 로고
    • Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5-and COG7-deficient mammalian cells
    • Oka, T., Vasile, E., Penman, M., Novina, C. D., Dykxhoorn, D. M., Ungar, D., et al. (2005). Genetic analysis of the subunit organization and function of the conserved oligomeric golgi (COG) complex: studies of COG5-and COG7-deficient mammalian cells. J. Biol. Chem. 280, 32736-32745. doi: 10.1074/jbc.M505558200
    • (2005) J. Biol. Chem , vol.280 , pp. 32736-32745
    • Oka, T.1    Vasile, E.2    Penman, M.3    Novina, C.D.4    Dykxhoorn, D.M.5    Ungar, D.6
  • 66
    • 70349319578 scopus 로고    scopus 로고
    • Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network
    • Pérez-Victoria, F. J., and Bonifacino, J. S. (2009). Dual roles of the mammalian GARP complex in tethering and SNARE complex assembly at the trans-golgi network. Mol. Cell. Biol. 29, 5251-5263. doi: 10.1128/MCB.00495-09
    • (2009) Mol. Cell. Biol , vol.29 , pp. 5251-5263
    • Pérez-Victoria, F.J.1    Bonifacino, J.S.2
  • 67
    • 77958033412 scopus 로고    scopus 로고
    • Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex
    • Pérez-Victoria, F. J., Schindler, C., Magadán, J. G., Mardones, G. A., Delevoye, C., Romao, M., et al. (2010). Ang2/fat-free is a conserved subunit of the Golgi-associated retrograde protein complex. Mol. Biol. Cell 21, 3386-3395. doi: 10.1091/mbc.E10-05-0392
    • (2010) Mol. Biol. Cell , vol.21 , pp. 3386-3395
    • Pérez-Victoria, F.J.1    Schindler, C.2    Magadán, J.G.3    Mardones, G.A.4    Delevoye, C.5    Romao, M.6
  • 68
    • 66749160940 scopus 로고    scopus 로고
    • Endoplasmic reticulum-associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis
    • Perry, R. J., Mast, F. D., and Rachubinski, R. A. (2009). Endoplasmic reticulum-associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis. Eukaryotic Cell 8, 830-843. doi: 10.1128/EC.00024-09
    • (2009) Eukaryotic Cell , vol.8 , pp. 830-843
    • Perry, R.J.1    Mast, F.D.2    Rachubinski, R.A.3
  • 70
    • 84868031743 scopus 로고    scopus 로고
    • Integrative functional genomics identifies RINT1 as a novel GBM oncogene
    • Quayle, S. N., Chheda, M. G., Shukla, S. A., Wiedemeyer, R., Tamayo, P., Dewan, R. W., et al. (2012). Integrative functional genomics identifies RINT1 as a novel GBM oncogene. Neuro Oncol. 14, 1325-1331. doi: 10.1093/neuonc/nos246
    • (2012) Neuro Oncol , vol.14 , pp. 1325-1331
    • Quayle, S.N.1    Chheda, M.G.2    Shukla, S.A.3    Wiedemeyer, R.4    Tamayo, P.5    Dewan, R.W.6
  • 71
    • 0035661564 scopus 로고    scopus 로고
    • Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit
    • Reilly, B. A., Kraynack, B. A., VanRheenen, S. M., and Waters, M. G. (2001). Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunit. Mol. Biol. Cell 12, 3783-3796. doi: 10.1091/mbc.12.12.3783
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3783-3796
    • Reilly, B.A.1    Kraynack, B.A.2    VanRheenen, S.M.3    Waters, M.G.4
  • 72
    • 71149117138 scopus 로고    scopus 로고
    • A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1
    • Ren, Y., Yip, C. K., Tripathi, A., Huie, D., Jeffrey, P. D., Walz, T., et al. (2009). A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1. Cell 139, 1119-1129. doi: 10.1016/j.cell.2009.11.002
    • (2009) Cell , vol.139 , pp. 1119-1129
    • Ren, Y.1    Yip, C.K.2    Tripathi, A.3    Huie, D.4    Jeffrey, P.D.5    Walz, T.6
  • 73
    • 84883148466 scopus 로고    scopus 로고
    • Protein adaptation: mitotic functions for membrane trafficking proteins
    • Royle, S. J. (2013). Protein adaptation: mitotic functions for membrane trafficking proteins. Nat. Rev. Mol. Cell Biol. 14, 592-599. doi: 10.1038/nrm3641
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 592-599
    • Royle, S.J.1
  • 74
    • 77957770103 scopus 로고    scopus 로고
    • Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation
    • Ryu, H., and Azuma, Y. (2010). Rod/Zw10 complex is required for PIASy-dependent centromeric SUMOylation. J. Biol. Chem. 285, 32576-32585. doi: 10.1074/jbc.M110.153817
    • (2010) J. Biol. Chem , vol.285 , pp. 32576-32585
    • Ryu, H.1    Azuma, Y.2
  • 75
    • 84873267192 scopus 로고    scopus 로고
    • Beclin 1 interactome controls the crosstalk between apoptosis, autophagy and inflammasome activation: impact on the aging process
    • Salminen, A., Kaarniranta, K., and Kauppinen, A. (2013). Beclin 1 interactome controls the crosstalk between apoptosis, autophagy and inflammasome activation: impact on the aging process. Ageing Res. Rev. 12, 520-534. doi: 10.1016/j.arr.2012.11.004
    • (2013) Ageing Res. Rev , vol.12 , pp. 520-534
    • Salminen, A.1    Kaarniranta, K.2    Kauppinen, A.3
  • 76
    • 0032693291 scopus 로고    scopus 로고
    • The rough deal protein is a new kinetochore component required for accurate chromosome segregation in Drosophila
    • Scaërou, F., Aguilera, I., Saunders, R., Kane, N., Blottiere, L., and Karess, R. (1999). The rough deal protein is a new kinetochore component required for accurate chromosome segregation in Drosophila. J. Cell Sci. 112, 3757-3768
    • (1999) J. Cell Sci , vol.112 , pp. 3757-3768
    • Scaërou, F.1    Aguilera, I.2    Saunders, R.3    Kane, N.4    Blottiere, L.5    Karess, R.6
  • 77
    • 0034799722 scopus 로고    scopus 로고
    • The ZW10 and rough deal checkpoint proteins function together in a large, evolutionarily conserved complex targeted to the kinetochore
    • Scaërou, F., Starr, D. A., Piano, F., Papoulas, O., Karess, R. E., and Goldberg, M. L. (2001). The ZW10 and rough deal checkpoint proteins function together in a large, evolutionarily conserved complex targeted to the kinetochore. J. Cell Sci. 114, 3103-3114
    • (2001) J. Cell Sci , vol.114 , pp. 3103-3114
    • Scaërou, F.1    Starr, D.A.2    Piano, F.3    Papoulas, O.4    Karess, R.E.5    Goldberg, M.L.6
  • 78
    • 77952554428 scopus 로고    scopus 로고
    • Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules
    • Schmitt, H. D. (2010). Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules. Trends Cell Biol. 20, 257-268. doi: 10.1016/j.tcb.2010.02.001
    • (2010) Trends Cell Biol , vol.20 , pp. 257-268
    • Schmitt, H.D.1
  • 79
    • 0037468865 scopus 로고    scopus 로고
    • The neuroblastoma amplified gene, NAG: genomic structure and characterisation of the 7.3 kb transcript predominantly expressed in neuroblastoma
    • Scott, D. K., Board, J. R., Lu, X., Pearson, A. D., Kenyon, R. M., and Lunec, J. (2003). The neuroblastoma amplified gene, NAG: genomic structure and characterisation of the 7.3 kb transcript predominantly expressed in neuroblastoma. Gene 307, 1-11. doi: 10.1016/S0378-1119(03)00459-1
    • (2003) Gene , vol.307 , pp. 1-11
    • Scott, D.K.1    Board, J.R.2    Lu, X.3    Pearson, A.D.4    Kenyon, R.M.5    Lunec, J.6
  • 80
    • 84862241805 scopus 로고    scopus 로고
    • The DSL1 complex: the smallest but not the least CATCHR
    • Spang, A. (2012). The DSL1 complex: the smallest but not the least CATCHR. Traffic 13, 908-913. doi: 10.1111/j.1600-0854.2012.01362.x
    • (2012) Traffic , vol.13 , pp. 908-913
    • Spang, A.1
  • 81
    • 0034121266 scopus 로고    scopus 로고
    • HZwint-1, a novel human kinetochore component that interacts with HZW10
    • Starr, D. A., Saffery, R., Li, Z., Simpson, A. E., Choo, K. H., Yen, T. J., et al. (2000). HZwint-1, a novel human kinetochore component that interacts with HZW10. J. Cell Sci. 113, 1939-1950
    • (2000) J. Cell Sci , vol.113 , pp. 1939-1950
    • Starr, D.A.1    Saffery, R.2    Li, Z.3    Simpson, A.E.4    Choo, K.H.5    Yen, T.J.6
  • 82
    • 0031852650 scopus 로고    scopus 로고
    • ZW10 helps recruit dynactin and dynein to the kinetochore
    • Starr, D. A., Williams, B. C., Hays, T. S., and Goldberg, M. L. (1998). ZW10 helps recruit dynactin and dynein to the kinetochore. J. Cell Biol. 142, 763-774. doi: 10.1083/jcb.142.3.763
    • (1998) J. Cell Biol , vol.142 , pp. 763-774
    • Starr, D.A.1    Williams, B.C.2    Hays, T.S.3    Goldberg, M.L.4
  • 83
    • 34547958546 scopus 로고    scopus 로고
    • NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores
    • Stehman, S. A., Chen, Y., McKenney, R. J., and Vallee, R. B. (2007). NudE and NudEL are required for mitotic progression and are involved in dynein recruitment to kinetochores. J. Cell Biol. 178, 583-594. doi: 10.1083/jcb.200610112
    • (2007) J. Cell Biol , vol.178 , pp. 583-594
    • Stehman, S.A.1    Chen, Y.2    McKenney, R.J.3    Vallee, R.B.4
  • 84
    • 34948888155 scopus 로고    scopus 로고
    • Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis
    • Sun, Y., Shestakova, A., Hunt, L., Sehgal, S., Lupashin, V., and Storrie, B. (2007). Rab6 regulates both ZW10/RINT-1 and conserved oligomeric Golgi complex-dependent Golgi trafficking and homeostasis. Mol. Biol. Cell 18, 4129-4142. doi: 10.1091/mbc.E07-01-0080
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4129-4142
    • Sun, Y.1    Shestakova, A.2    Hunt, L.3    Sehgal, S.4    Lupashin, V.5    Storrie, B.6
  • 85
    • 0037013167 scopus 로고    scopus 로고
    • Fragmentation and dispersal of the pericentriolar Golgi complex is required for entry into mitosis in mammalian cells
    • Sütterlin, 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. doi: 10.1016/S0092-8674(02)00720-1
    • (2002) Cell , vol.109 , pp. 359-369
    • Sütterlin, C.1    Hsu, P.2    Mallabiabarrena, A.3    Malhotra, V.4
  • 86
    • 0027294075 scopus 로고
    • The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p
    • Sweet, D. J., and Pelham, H. R. (1993). The TIP1 gene of Saccharomyces cerevisiae encodes an 80 kDa cytoplasmic protein that interacts with the cytoplasmic domain of Sec20p. EMBO J. 12, 2831-2840
    • (1993) EMBO J , vol.12 , pp. 2831-2840
    • Sweet, D.J.1    Pelham, H.R.2
  • 87
    • 59649120867 scopus 로고    scopus 로고
    • Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
    • Tripathi, A., Ren, Y., Jeffrey, P. D., and Hughson, F. M. (2009). Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nat. Struct. Mol. Biol. 16, 114-123. doi: 10.1038/nsmb.1548
    • (2009) Nat. Struct. Mol. Biol , vol.16 , pp. 114-123
    • Tripathi, A.1    Ren, Y.2    Jeffrey, P.D.3    Hughson, F.M.4
  • 88
    • 63049134520 scopus 로고    scopus 로고
    • p31 deficiency influences endoplasmic reticulum tubular morphology and cell survival
    • Uemura, T., Sato, T., Aoki, T., Yamamoto, A., Okada, T., Hirai, R., et al. (2009). p31 deficiency influences endoplasmic reticulum tubular morphology and cell survival. Mol. Cell. Biol. 29, 1869-1881. doi: 10.1128/MCB.01089-08
    • (2009) Mol. Cell. Biol , vol.29 , pp. 1869-1881
    • Uemura, T.1    Sato, T.2    Aoki, T.3    Yamamoto, A.4    Okada, T.5    Hirai, R.6
  • 89
    • 0034628508 scopus 로고    scopus 로고
    • A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae
    • Uetz, P., Giot, L., Cagney, G., Mansfield, T. A., Judson, R. S., Knight, J. R., et al. (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature 403, 623-627. doi: 10.1038/35001009
    • (2000) Nature , vol.403 , pp. 623-627
    • Uetz, P.1    Giot, L.2    Cagney, G.3    Mansfield, T.A.4    Judson, R.S.5    Knight, J.R.6
  • 90
    • 25444486756 scopus 로고    scopus 로고
    • Subunit map of the conserved oligomeric Golgi complex
    • Ungar, D., Oka, T., Vasile, E., Krieger, M., and Hughson, F. M. (2005). Subunit map of the conserved oligomeric Golgi complex. J. Biol. Chem. 280, 32729-32735. doi: 10.1074/jbc.M504590200
    • (2005) J. Biol. Chem , vol.280 , pp. 32729-32735
    • Ungar, D.1    Oka, T.2    Vasile, E.3    Krieger, M.4    Hughson, F.M.5
  • 91
    • 0035016821 scopus 로고    scopus 로고
    • Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast
    • VanRheenen, S. M., Reilly, B. A., Chamberlain, S. J., and Waters, M. G. (2001). Dsl1p, an essential protein required for membrane traffic at the endoplasmic reticulum/Golgi interface in yeast. Traffic 2, 212-231. doi: 10.1034/j.1600-0854.2001.020307.x
    • (2001) Traffic , vol.2 , pp. 212-231
    • VanRheenen, S.M.1    Reilly, B.A.2    Chamberlain, S.J.3    Waters, M.G.4
  • 92
    • 48749102970 scopus 로고    scopus 로고
    • A unique residue in rab3c determines the interaction with novel binding protein Zwint-1
    • van Vlijmen, T., Vleugel, M., Evers, M., Mohammed, S., Wulf, P. S., Heck, A. J., et al. (2008). A unique residue in rab3c determines the interaction with novel binding protein Zwint-1. FEBS Lett. 582, 2838-2842. doi: 10.1016/j.febslet.2008.07.012
    • (2008) FEBS Lett , vol.582 , pp. 2838-2842
    • van Vlijmen, T.1    Vleugel, M.2    Evers, M.3    Mohammed, S.4    Wulf, P.S.5    Heck, A.J.6
  • 93
    • 33644517564 scopus 로고    scopus 로고
    • Role of the kinetochore/cell cycle checkpoint protein ZW10 in interphase cytoplasmic dynein function
    • Varma, D., Dujardin, D. L., Stehman, S. A., and Vallee, R. B. (2006). Role of the kinetochore/cell cycle checkpoint protein ZW10 in interphase cytoplasmic dynein function. J. Cell Biol. 172, 655-662. doi: 10.1083/jcb.200510120
    • (2006) J. Cell Biol , vol.172 , pp. 655-662
    • Varma, D.1    Dujardin, D.L.2    Stehman, S.A.3    Vallee, R.B.4
  • 94
    • 84865072109 scopus 로고    scopus 로고
    • Evolution and function of the mitotic checkpoint
    • Vleugel, M., Hoogendoorn, E., Snel, B., and Kops, G. J. (2012). Evolution and function of the mitotic checkpoint. Dev. Cell 23, 239-250. doi: 10.1016/j.devcel.2012.06.013
    • (2012) Dev. Cell , vol.23 , pp. 239-250
    • Vleugel, M.1    Hoogendoorn, E.2    Snel, B.3    Kops, G.J.4
  • 95
    • 84869112077 scopus 로고    scopus 로고
    • The Drosophila RZZ complex-roles in membrane trafficking and cytokinesis
    • Wainman, A., Giansanti, M. G., Goldberg, M. L., and Gatti, M. (2012). The Drosophila RZZ complex-roles in membrane trafficking and cytokinesis. J. Cell Sci. 125, 4014-4025. doi: 10.1242/jcs.099820
    • (2012) J. Cell Sci , vol.125 , pp. 4014-4025
    • Wainman, A.1    Giansanti, M.G.2    Goldberg, M.L.3    Gatti, M.4
  • 96
    • 19944427982 scopus 로고    scopus 로고
    • Human Zwint-1 specifies localization of Zeste White 10 to kinetochores and is essential for mitotic checkpoint signaling
    • Wang, H., Hu, X., Ding, X., Dou, Z., Yang, Z., Shaw, A. W., et al. (2004). Human Zwint-1 specifies localization of Zeste White 10 to kinetochores and is essential for mitotic checkpoint signaling. J. Biol. Chem. 279, 54590-54598. doi: 10.1074/jbc.M407588200
    • (2004) J. Biol. Chem , vol.279 , pp. 54590-54598
    • Wang, H.1    Hu, X.2    Ding, X.3    Dou, Z.4    Yang, Z.5    Shaw, A.W.6
  • 97
    • 4344654349 scopus 로고    scopus 로고
    • Coamplification of DDX1 correlates with an improved survival probability in children with MYCN-amplified human neuroblastoma
    • Weber, A., Imisch, P., Bergmann, E., and Christiansen, H. (2004). Coamplification of DDX1 correlates with an improved survival probability in children with MYCN-amplified human neuroblastoma. J. Clin. Oncol. 22, 2681-2690. doi: 10.1200/JCO.2004.07.192
    • (2004) J. Clin. Oncol , vol.22 , pp. 2681-2690
    • Weber, A.1    Imisch, P.2    Bergmann, E.3    Christiansen, H.4
  • 98
    • 84875886094 scopus 로고    scopus 로고
    • COG complexes form spatial landmarks for distinct SNARE complexes
    • Willett, R., Kudlyk, T., Pokrovskaya, I., Schönherr, R., Ungar, D., Duden, R., et al. (2013). COG complexes form spatial landmarks for distinct SNARE complexes. Nat. Commun. 4, 1553. doi: 10.1038/ncomms2535
    • (2013) Nat. Commun , vol.4 , pp. 1553
    • Willett, R.1    Kudlyk, T.2    Pokrovskaya, I.3    Schönherr, R.4    Ungar, D.5    Duden, R.6
  • 99
    • 0026757402 scopus 로고
    • The Drosophila l(1) zw10 gene product, required for accurate mitotic chromosome segregation, is redistributed at anaphase onset
    • Williams, B. C., Karr, T. L., Montgomery, J. M., and Goldberg, M. L. (1992). The Drosophila l(1) zw10 gene product, required for accurate mitotic chromosome segregation, is redistributed at anaphase onset. J. Cell Biol. 118, 759-773. doi: 10.1083/jcb.118.4.759
    • (1992) J. Cell Biol , vol.118 , pp. 759-773
    • Williams, B.C.1    Karr, T.L.2    Montgomery, J.M.3    Goldberg, M.L.4
  • 100
    • 0037694976 scopus 로고    scopus 로고
    • Zwilch, a new component of the ZW10/ROD complex required for kinetochore functions
    • Williams, B. C., Li, Z., Liu, S., Williams, E. V., Leung, G., Yen, T. J., et al. (2003). Zwilch, a new component of the ZW10/ROD complex required for kinetochore functions. Mol. Biol. Cell 14, 1379-1391. doi: 10.1091/mbc.E02-09-0624
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1379-1391
    • Williams, B.C.1    Li, Z.2    Liu, S.3    Williams, E.V.4    Leung, G.5    Yen, T.J.6
  • 101
    • 0033531259 scopus 로고    scopus 로고
    • Co-amplification of a novel gene, NAG, with the N-myc gene in neuroblastoma
    • Wimmer, K., Zhu, X. X., Lamb, B. J., Kuick, R., Ambros, P. F., Kovar, H., et al. (1999). Co-amplification of a novel gene, NAG, with the N-myc gene in neuroblastoma. Oncogene 18, 233-238. doi: 10.1038/sj.onc.1202287
    • (1999) Oncogene , vol.18 , pp. 233-238
    • Wimmer, K.1    Zhu, X.X.2    Lamb, B.J.3    Kuick, R.4    Ambros, P.F.5    Kovar, H.6
  • 102
    • 0035736325 scopus 로고    scopus 로고
    • Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein
    • Wojcik, E., Basto, R., Serr, M., Scaërou, F., Karess, R., and Hays, T. (2001). Kinetochore dynein: its dynamics and role in the transport of the Rough deal checkpoint protein. Nat. Cell Biol. 3, 1001-1007. doi: 10.1038/ncb1101-1001
    • (2001) Nat. Cell Biol , vol.3 , pp. 1001-1007
    • Wojcik, E.1    Basto, R.2    Serr, M.3    Scaërou, F.4    Karess, R.5    Hays, T.6
  • 103
    • 0035794203 scopus 로고    scopus 로고
    • RINT-1, a novel rad50-interacting protein, participates in radiation induced G2/M checkpoint control
    • Xiao, J., Liu, C.-C., Chen, P.-L., and Lee, W.-H. (2001). RINT-1, a novel rad50-interacting protein, participates in radiation induced G2/M checkpoint control. J. Biol. Chem. 276, 6105-6111. doi: 10.1074/jbc.M008893200
    • (2001) J. Biol. Chem , vol.276 , pp. 6105-6111
    • Xiao, J.1    Liu, C.-C.2    Chen, P.-L.3    Lee, W.-H.4
  • 104
    • 0036193747 scopus 로고    scopus 로고
    • Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif
    • Yamaguchi, T., Dulubova, I., Min, S. W., Chen, X., Rizo, J., and Südhof, T. C. (2002). Sly1 binds to Golgi and ER syntaxins via a conserved N-terminal peptide motif. Dev. Cell 2, 295-305. doi: 10.1016/S1534-5807(02)00125-9
    • (2002) Dev. Cell , vol.2 , pp. 295-305
    • Yamaguchi, T.1    Dulubova, I.2    Min, S.W.3    Chen, X.4    Rizo, J.5    Südhof, T.C.6
  • 105
    • 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. doi: 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
  • 106
    • 70349782801 scopus 로고    scopus 로고
    • Role of SIP30 in the development and maintenance of peripheral nerve injury-induced neuropathic pain
    • Zhang, Y. Q., Guo, N., Peng, G., Wang, X., Han, M., Raincrow, J., et al. (2009). Role of SIP30 in the development and maintenance of peripheral nerve injury-induced neuropathic pain. Pain 146, 130-140. doi: 10.1016/j.pain.2009.07.011
    • (2009) Pain , vol.146 , pp. 130-140
    • Zhang, Y.Q.1    Guo, N.2    Peng, G.3    Wang, X.4    Han, M.5    Raincrow, J.6
  • 107
    • 84875590198 scopus 로고    scopus 로고
    • MAIGO2 is involved in abscisic acid-mediated response to abiotic stresses and Golgi-to-ER retrograde transport
    • Zhao, P., Liu, F., Zhang, B., Liu, X., Wang, B., Gong, J., et al. (2013). MAIGO2 is involved in abscisic acid-mediated response to abiotic stresses and Golgi-to-ER retrograde transport. Physiol. Plant 148, 246-260. doi: 10.1111/j.1399-3054.2012.01704.x
    • (2013) Physiol. Plant , vol.148 , pp. 246-260
    • Zhao, P.1    Liu, F.2    Zhang, B.3    Liu, X.4    Wang, B.5    Gong, J.6
  • 108
    • 69949175597 scopus 로고    scopus 로고
    • A link between ER tethering and COP-I vesicle uncoating
    • Zink, S., Wenzel, D., Wurm, C. A., and Schmitt, H. D. (2009). A link between ER tethering and COP-I vesicle uncoating. Dev. Cell 17, 403-416. doi: 10.1016/j.devcel.2009.07.012
    • (2009) Dev. Cell , vol.17 , pp. 403-416
    • Zink, S.1    Wenzel, D.2    Wurm, C.A.3    Schmitt, H.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.