메뉴 건너뛰기




Volumn 24, Issue 10, 2014, Pages 584-593

Secretory cargo sorting at the trans-Golgi network

Author keywords

Ca2+; Protein sorting; Secretory cargo; TGN

Indexed keywords

ACTIN; CALCIUM ION; COFILIN; MEMBRANE PROTEIN; SECRETORY PROTEIN;

EID: 84908478141     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2014.04.007     Document Type: Review
Times cited : (84)

References (104)
  • 1
    • 79959535759 scopus 로고    scopus 로고
    • Circulating chemokine (CXC motif) ligand (CXCL)9 is increased in aggressive chronic autoimmune thyroiditis, in association with CXCL10
    • Antonelli A., et al. Circulating chemokine (CXC motif) ligand (CXCL)9 is increased in aggressive chronic autoimmune thyroiditis, in association with CXCL10. Cytokine 2011, 55:288-293.
    • (2011) Cytokine , vol.55 , pp. 288-293
    • Antonelli, A.1
  • 2
    • 0037452997 scopus 로고    scopus 로고
    • Large-scale delineation of secreted protein biomarkers overexpressed in cancer tissue and serum
    • Welsh J.B., et al. Large-scale delineation of secreted protein biomarkers overexpressed in cancer tissue and serum. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:3410-3415.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3410-3415
    • Welsh, J.B.1
  • 3
    • 0035890055 scopus 로고    scopus 로고
    • 2+ stabilization
    • 2+ stabilization. EMBO J. 2001, 20:6277-6287.
    • (2001) EMBO J. , vol.20 , pp. 6277-6287
    • Chen, C.D.1
  • 4
    • 0034968330 scopus 로고    scopus 로고
    • -/- mice reveals a role for translational control in secretory cell survival
    • -/- mice reveals a role for translational control in secretory cell survival. Mol. Cell 2001, 7:1153-1163.
    • (2001) Mol. Cell , vol.7 , pp. 1153-1163
    • Harding, H.P.1
  • 5
    • 0030699168 scopus 로고    scopus 로고
    • The fate of cartilage oligomeric matrix protein is determined by the cell type in the case of a novel mutation in pseudoachondroplasia
    • Maddox B.K., et al. The fate of cartilage oligomeric matrix protein is determined by the cell type in the case of a novel mutation in pseudoachondroplasia. J. Biol. Chem. 1997, 272:30993-30997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30993-30997
    • Maddox, B.K.1
  • 6
    • 0018987976 scopus 로고
    • Intracellular protein topogenesis
    • Blobel G. Intracellular protein topogenesis. Proc. Natl. Acad. Sci. U.S.A. 1980, 77:1496-1500.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1496-1500
    • Blobel, G.1
  • 7
    • 0022975133 scopus 로고
    • The trans Golgi network: sorting at the exit site of the Golgi complex
    • Griffiths G., Simons K. The trans Golgi network: sorting at the exit site of the Golgi complex. Science 1986, 234:438-443.
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 8
    • 70350230237 scopus 로고    scopus 로고
    • Membrane traffic within the Golgi apparatus
    • Glick B.S., Nakano A. Membrane traffic within the Golgi apparatus. Annu. Rev. Cell Dev. Biol. 2009, 25:113-132.
    • (2009) Annu. Rev. Cell Dev. Biol. , vol.25 , pp. 113-132
    • Glick, B.S.1    Nakano, A.2
  • 9
    • 84861898727 scopus 로고    scopus 로고
    • Membrane fission: the biogenesis of transport carriers
    • Campelo F., Malhotra V. Membrane fission: the biogenesis of transport carriers. Annu. Rev. Biochem. 2012, 81:407-427.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 407-427
    • Campelo, F.1    Malhotra, V.2
  • 12
    • 0030816038 scopus 로고    scopus 로고
    • The trans-Golgi network: a late secretory sorting station
    • Traub L.M., Kornfeld S. The trans-Golgi network: a late secretory sorting station. Curr. Opin. Cell Biol. 1997, 9:527-533.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 527-533
    • Traub, L.M.1    Kornfeld, S.2
  • 13
    • 54549102285 scopus 로고    scopus 로고
    • Coordinated protein sorting, targeting and distribution in polarized cells
    • Mellman I., Nelson W.J. Coordinated protein sorting, targeting and distribution in polarized cells. Nat. Rev. Mol. Cell Biol. 2008, 9:833-845.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 833-845
    • Mellman, I.1    Nelson, W.J.2
  • 14
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein synthesis
    • Palade G. Intracellular aspects of the process of protein synthesis. Science 1975, 189:867.
    • (1975) Science , vol.189 , pp. 867
    • Palade, G.1
  • 15
    • 0029040979 scopus 로고
    • Trans-Golgi network (TGN) of different cell types: three-dimensional structural characteristics and variability
    • Clermont Y., et al. Trans-Golgi network (TGN) of different cell types: three-dimensional structural characteristics and variability. Anat. Rec. (Hoboken) 1995, 242:289-301.
    • (1995) Anat. Rec. (Hoboken) , vol.242 , pp. 289-301
    • Clermont, Y.1
  • 16
    • 70450225048 scopus 로고    scopus 로고
    • ER exit sites - localization and control of COPII vesicle formation
    • Budnik A., Stephens D.J. ER exit sites - localization and control of COPII vesicle formation. FEBS Lett. 2009, 583:3796-3803.
    • (2009) FEBS Lett. , vol.583 , pp. 3796-3803
    • Budnik, A.1    Stephens, D.J.2
  • 17
    • 0028136433 scopus 로고
    • HVEM tomography of the trans-Golgi network: structural insights and identification of a lace-like vesicle coat
    • Ladinsky M.S., et al. HVEM tomography of the trans-Golgi network: structural insights and identification of a lace-like vesicle coat. J. Cell Biol. 1994, 127:29-38.
    • (1994) J. Cell Biol. , vol.127 , pp. 29-38
    • Ladinsky, M.S.1
  • 18
    • 2442717709 scopus 로고    scopus 로고
    • Domains of the TGN: coats, tethers and G proteins
    • Gleeson P.A., et al. Domains of the TGN: coats, tethers and G proteins. Traffic 2004, 5:315-326.
    • (2004) Traffic , vol.5 , pp. 315-326
    • Gleeson, P.A.1
  • 19
    • 0037459096 scopus 로고    scopus 로고
    • Membrane domains in the secretory and endocytic pathways
    • Pfeffer S. Membrane domains in the secretory and endocytic pathways. Cell 2003, 112:507-517.
    • (2003) Cell , vol.112 , pp. 507-517
    • Pfeffer, S.1
  • 20
    • 0029943503 scopus 로고    scopus 로고
    • Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells
    • Müsch A., et al. Transport of vesicular stomatitis virus G protein to the cell surface is signal mediated in polarized and nonpolarized cells. J. Cell Biol. 1996, 133:543-558.
    • (1996) J. Cell Biol. , vol.133 , pp. 543-558
    • Müsch, A.1
  • 21
    • 0029879919 scopus 로고    scopus 로고
    • Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells
    • Yoshimori T., et al. Different biosynthetic transport routes to the plasma membrane in BHK and CHO cells. J. Cell Biol. 1996, 133:247-256.
    • (1996) J. Cell Biol. , vol.133 , pp. 247-256
    • Yoshimori, T.1
  • 22
    • 0032897432 scopus 로고    scopus 로고
    • Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells
    • Toomre D., et al. Dual-color visualization of trans-Golgi network to plasma membrane traffic along microtubules in living cells. J. Cell Sci. 1999, 112:21-33.
    • (1999) J. Cell Sci. , vol.112 , pp. 21-33
    • Toomre, D.1
  • 23
    • 0345687308 scopus 로고    scopus 로고
    • Mechanism of constitutive export from the Golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-Golgi network tubular domains
    • Polishchuk E.V., et al. Mechanism of constitutive export from the Golgi: bulk flow via the formation, protrusion, and en bloc cleavage of large trans-Golgi network tubular domains. Mol. Biol. Cell 2003, 14:4470-4485.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4470-4485
    • Polishchuk, E.V.1
  • 24
    • 84867571843 scopus 로고    scopus 로고
    • A new class of carriers that transport selective cargo from the trans Golgi network to the cell surface
    • Wakana Y., et al. A new class of carriers that transport selective cargo from the trans Golgi network to the cell surface. EMBO J. 2012, 10.1038/emboj.2012.235.
    • (2012) EMBO J.
    • Wakana, Y.1
  • 26
    • 77950550447 scopus 로고    scopus 로고
    • Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex
    • Burgos P.V., et al. Sorting of the Alzheimer's disease amyloid precursor protein mediated by the AP-4 complex. Dev. Cell 2010, 18:425-436.
    • (2010) Dev. Cell , vol.18 , pp. 425-436
    • Burgos, P.V.1
  • 27
    • 79960716101 scopus 로고    scopus 로고
    • Exit from the trans-Golgi network: from molecules to mechanisms
    • Anitei M., Hoflack B. Exit from the trans-Golgi network: from molecules to mechanisms. Curr. Opin. Cell Biol. 2011, 23:443-451.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 443-451
    • Anitei, M.1    Hoflack, B.2
  • 28
    • 84891894909 scopus 로고    scopus 로고
    • Adaptor proteins involved in polarized sorting
    • Bonifacino J.S. Adaptor proteins involved in polarized sorting. J. Cell Biol. 2014, 204:7-17.
    • (2014) J. Cell Biol. , vol.204 , pp. 7-17
    • Bonifacino, J.S.1
  • 29
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze S.A., Huttner W.B. Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell 1990, 60:837-847.
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2
  • 30
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E., Huttner W.B. Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J. Cell Biol. 1991, 115:1505-1519.
    • (1991) J. Cell Biol. , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 31
    • 33745747908 scopus 로고    scopus 로고
    • Biogenesis of secretory granules
    • Borgonovo B., et al. Biogenesis of secretory granules. Curr. Opin. Cell Biol. 2006, 18:365-370.
    • (2006) Curr. Opin. Cell Biol. , vol.18 , pp. 365-370
    • Borgonovo, B.1
  • 32
    • 34247543907 scopus 로고    scopus 로고
    • Sending proteins to dense core secretory granules: still a lot to sort out
    • Dikeakos J.D., Reudelhuber T.L. Sending proteins to dense core secretory granules: still a lot to sort out. J. Cell Biol. 2007, 177:191-196.
    • (2007) J. Cell Biol. , vol.177 , pp. 191-196
    • Dikeakos, J.D.1    Reudelhuber, T.L.2
  • 33
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: looking backward and looking forward
    • Arvan P., Castle D. Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem. J. 1998, 332:593-610.
    • (1998) Biochem. J. , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 34
    • 0032862770 scopus 로고    scopus 로고
    • Signal-mediated sorting to the regulated pathway of protein secretion
    • Gerdes H.H., Glombik M.M. Signal-mediated sorting to the regulated pathway of protein secretion. Ann. Anat. 1999, 181:447-453.
    • (1999) Ann. Anat. , vol.181 , pp. 447-453
    • Gerdes, H.H.1    Glombik, M.M.2
  • 35
    • 23044488803 scopus 로고    scopus 로고
    • Chromogranin A deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis
    • Kim T., et al. Chromogranin A deficiency in transgenic mice leads to aberrant chromaffin granule biogenesis. J. Neurosci. 2005, 25:6958-6961.
    • (2005) J. Neurosci. , vol.25 , pp. 6958-6961
    • Kim, T.1
  • 36
    • 32944469481 scopus 로고    scopus 로고
    • Requirement for galectin-3 in apical protein sorting
    • Delacour D., et al. Requirement for galectin-3 in apical protein sorting. Curr. Biol. 2006, 16:408-414.
    • (2006) Curr. Biol. , vol.16 , pp. 408-414
    • Delacour, D.1
  • 37
    • 0037039349 scopus 로고    scopus 로고
    • Carboxypeptidase E, a prohormone sorting receptor, is anchored to secretory granules via a C-terminal transmembrane insertion
    • Dhanvantari S., et al. Carboxypeptidase E, a prohormone sorting receptor, is anchored to secretory granules via a C-terminal transmembrane insertion. Biochemistry 2002, 41:52-60.
    • (2002) Biochemistry , vol.41 , pp. 52-60
    • Dhanvantari, S.1
  • 38
    • 0032580247 scopus 로고    scopus 로고
    • Carboxypeptidase E is a sorting receptor for prohormones: binding and kinetic studies
    • Cool D.R., Loh Y.P. Carboxypeptidase E is a sorting receptor for prohormones: binding and kinetic studies. Mol. Cell. Endocrinol. 1998, 139:7-13.
    • (1998) Mol. Cell. Endocrinol. , vol.139 , pp. 7-13
    • Cool, D.R.1    Loh, Y.P.2
  • 39
    • 12344328770 scopus 로고    scopus 로고
    • Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase E
    • Lou H., et al. Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase E. Neuron 2005, 45:245-255.
    • (2005) Neuron , vol.45 , pp. 245-255
    • Lou, H.1
  • 40
    • 0942265534 scopus 로고    scopus 로고
    • Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A
    • Hosaka M., et al. Secretogranin III binds to cholesterol in the secretory granule membrane as an adapter for chromogranin A. J. Biol. Chem. 2004, 279:3627-3634.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3627-3634
    • Hosaka, M.1
  • 41
    • 27844494185 scopus 로고    scopus 로고
    • Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules
    • Hosaka M., et al. Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules. J. Cell Sci. 2005, 118:4785-4795.
    • (2005) J. Cell Sci. , vol.118 , pp. 4785-4795
    • Hosaka, M.1
  • 42
    • 0030836302 scopus 로고    scopus 로고
    • Proinsulin targeting to the regulated pathway is not impaired in carboxypeptidase E-deficient Cpefat/Cpefat mice
    • Irminger J.C., et al. Proinsulin targeting to the regulated pathway is not impaired in carboxypeptidase E-deficient Cpefat/Cpefat mice. J. Biol. Chem. 1997, 272:27532-27534.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27532-27534
    • Irminger, J.C.1
  • 45
    • 0030991809 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN
    • Le Borgne R., Hoflack B. Mannose 6-phosphate receptors regulate the formation of clathrin-coated vesicles in the TGN. J. Cell Biol. 1997, 137:335-345.
    • (1997) J. Cell Biol. , vol.137 , pp. 335-345
    • Le Borgne, R.1    Hoflack, B.2
  • 46
    • 39749200034 scopus 로고    scopus 로고
    • Imaging and imagination: understanding the endo-lysosomal system
    • van Meel E., Klumperman J. Imaging and imagination: understanding the endo-lysosomal system. Histochem. Cell Biol. 2008, 129:253-266.
    • (2008) Histochem. Cell Biol. , vol.129 , pp. 253-266
    • van Meel, E.1    Klumperman, J.2
  • 47
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: new twists in the tale
    • Ghosh P., et al. Mannose 6-phosphate receptors: new twists in the tale. Nat. Rev. Mol. Cell Biol. 2003, 4:202-212.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 202-212
    • Ghosh, P.1
  • 48
    • 0035838461 scopus 로고    scopus 로고
    • A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases
    • Whyte J.R., Munro S. A yeast homolog of the mammalian mannose 6-phosphate receptors contributes to the sorting of vacuolar hydrolases. Curr. Biol. 2001, 11:1074-1078.
    • (2001) Curr. Biol. , vol.11 , pp. 1074-1078
    • Whyte, J.R.1    Munro, S.2
  • 49
    • 0029905298 scopus 로고    scopus 로고
    • Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases
    • Cooper A.A., Stevens T.H. Vps10p cycles between the late-Golgi and prevacuolar compartments in its function as the sorting receptor for multiple yeast vacuolar hydrolases. J. Cell Biol. 1996, 133:529-541.
    • (1996) J. Cell Biol. , vol.133 , pp. 529-541
    • Cooper, A.A.1    Stevens, T.H.2
  • 50
    • 0025370505 scopus 로고
    • Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids
    • Valls L.A., et al. Yeast carboxypeptidase Y vacuolar targeting signal is defined by four propeptide amino acids. J. Cell Biol. 1990, 111:361-368.
    • (1990) J. Cell Biol. , vol.111 , pp. 361-368
    • Valls, L.A.1
  • 51
    • 0029618201 scopus 로고
    • Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins
    • Stack J.H., et al. Receptor-mediated protein sorting to the vacuole in yeast: roles for a protein kinase, a lipid kinase and GTP-binding proteins. Annu. Rev. Cell Dev. Biol. 1995, 11:1-33.
    • (1995) Annu. Rev. Cell Dev. Biol. , vol.11 , pp. 1-33
    • Stack, J.H.1
  • 52
    • 0027443394 scopus 로고
    • Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts
    • Glickman J.N., Kornfeld S. Mannose 6-phosphate-independent targeting of lysosomal enzymes in I-cell disease B lymphoblasts. J. Cell Biol. 1993, 123:99-108.
    • (1993) J. Cell Biol. , vol.123 , pp. 99-108
    • Glickman, J.N.1    Kornfeld, S.2
  • 53
    • 68549128595 scopus 로고    scopus 로고
    • The Vps10p-domain receptor family
    • Hermey G. The Vps10p-domain receptor family. Cell. Mol. Life Sci. 2009, 66:2677-2689.
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 2677-2689
    • Hermey, G.1
  • 54
    • 84890172313 scopus 로고    scopus 로고
    • Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena
    • Briguglio J.S., et al. Lysosomal sorting receptors are essential for secretory granule biogenesis in Tetrahymena. J. Cell Biol. 2013, 203:537-550.
    • (2013) J. Cell Biol. , vol.203 , pp. 537-550
    • Briguglio, J.S.1
  • 55
    • 84861986053 scopus 로고    scopus 로고
    • Wnt/β-catenin signaling and disease
    • Clevers H., Nusse R. Wnt/β-catenin signaling and disease. Cell 2012, 149:1192-1205.
    • (2012) Cell , vol.149 , pp. 1192-1205
    • Clevers, H.1    Nusse, R.2
  • 56
    • 33646134826 scopus 로고    scopus 로고
    • Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells
    • Bänziger C., et al. Wntless, a conserved membrane protein dedicated to the secretion of Wnt proteins from signaling cells. Cell 2006, 125:509-522.
    • (2006) Cell , vol.125 , pp. 509-522
    • Bänziger, C.1
  • 57
    • 84900419345 scopus 로고    scopus 로고
    • Wls retrograde transport to the endoplasmic reticulum during Wnt secretion
    • Yu J., et al. Wls retrograde transport to the endoplasmic reticulum during Wnt secretion. Dev. Cell 2014, 29:1-15.
    • (2014) Dev. Cell , vol.29 , pp. 1-15
    • Yu, J.1
  • 58
    • 84880671888 scopus 로고    scopus 로고
    • The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms
    • Yamamoto H., et al. The apical and basolateral secretion of Wnt11 and Wnt3a in polarized epithelial cells is regulated by different mechanisms. J. Cell Sci. 2013, 126:2931-2943.
    • (2013) J. Cell Sci. , vol.126 , pp. 2931-2943
    • Yamamoto, H.1
  • 59
    • 31844440878 scopus 로고    scopus 로고
    • Functional genomics reveals genes involved in protein secretion and Golgi organization
    • Bard F., et al. Functional genomics reveals genes involved in protein secretion and Golgi organization. Nature 2006, 439:604-607.
    • (2006) Nature , vol.439 , pp. 604-607
    • Bard, F.1
  • 60
    • 79955925696 scopus 로고    scopus 로고
    • 2+ ATPase SPCA1
    • 2+ ATPase SPCA1. Dev. Cell 2011, 20:652-662.
    • (2011) Dev. Cell , vol.20 , pp. 652-662
    • von Blume, J.1
  • 61
    • 76149090527 scopus 로고    scopus 로고
    • Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network
    • von Blume J., et al. Actin remodeling by ADF/cofilin is required for cargo sorting at the trans-Golgi network. J. Cell Biol. 2009, 187:1055-1069.
    • (2009) J. Cell Biol. , vol.187 , pp. 1055-1069
    • von Blume, J.1
  • 62
    • 84872004277 scopus 로고    scopus 로고
    • 2+-dependent secretory cargo sorting at the trans-Golgi network
    • 2+-dependent secretory cargo sorting at the trans-Golgi network. J. Cell Biol. 2012, 199:1057-1066.
    • (2012) J. Cell Biol. , vol.199 , pp. 1057-1066
    • von Blume, J.1
  • 63
    • 84862519850 scopus 로고    scopus 로고
    • Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast
    • Curwin A.J., et al. Cofilin-mediated sorting and export of specific cargo from the Golgi apparatus in yeast. Mol. Biol. Cell 2012, 23:2327-2338.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2327-2338
    • Curwin, A.J.1
  • 64
    • 0027097849 scopus 로고
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution
    • 2+-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution. Mol. Biol. Cell 1992, 3:633-654.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 633-654
    • Antebi, A.1    Fink, G.R.2
  • 65
    • 33947216270 scopus 로고    scopus 로고
    • Calcium in the Golgi apparatus
    • Missiaen L., et al. Calcium in the Golgi apparatus. Cell Calcium 2007, 41:405-416.
    • (2007) Cell Calcium , vol.41 , pp. 405-416
    • Missiaen, L.1
  • 66
    • 0033986288 scopus 로고    scopus 로고
    • Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease
    • Hu Z., et al. Mutations in ATP2C1, encoding a calcium pump, cause Hailey-Hailey disease. Nat. Genet. 2000, 24:61-65.
    • (2000) Nat. Genet. , vol.24 , pp. 61-65
    • Hu, Z.1
  • 67
    • 34548845571 scopus 로고    scopus 로고
    • 2+-ATPase (SPCA1) in mice causes Golgi stress, apoptosis, and midgestational death in homozygous embryos and squamous cell tumors in adult heterozygotes
    • 2+-ATPase (SPCA1) in mice causes Golgi stress, apoptosis, and midgestational death in homozygous embryos and squamous cell tumors in adult heterozygotes. J. Biol. Chem. 2007, 282:26517-26527.
    • (2007) J. Biol. Chem. , vol.282 , pp. 26517-26527
    • Okunade, G.W.1
  • 69
    • 77952710840 scopus 로고    scopus 로고
    • 2+ homeostasis of the trans-Golgi compartment
    • 2+ homeostasis of the trans-Golgi compartment. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:9198-9203.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9198-9203
    • Lissandron, V.1
  • 70
    • 80051473247 scopus 로고    scopus 로고
    • 2+ signalling in the Golgi apparatus
    • 2+ signalling in the Golgi apparatus. Cell Calcium 2011, 50:184-192.
    • (2011) Cell Calcium , vol.50 , pp. 184-192
    • Pizzo, P.1
  • 71
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman S.J., et al. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:15500-15505.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1
  • 72
    • 33845368663 scopus 로고    scopus 로고
    • Actin polymerization serves as a membrane domain switch in model lipid bilayers
    • Liu A.P., Fletcher D.A. Actin polymerization serves as a membrane domain switch in model lipid bilayers. Biophys. J. 2006, 91:4064-4070.
    • (2006) Biophys. J. , vol.91 , pp. 4064-4070
    • Liu, A.P.1    Fletcher, D.A.2
  • 73
    • 77953711502 scopus 로고    scopus 로고
    • The secretory pathway Ca2+-ATPase 1 is associated with cholesterol-rich microdomains of human colon adenocarcinoma cells
    • Baron S., et al. The secretory pathway Ca2+-ATPase 1 is associated with cholesterol-rich microdomains of human colon adenocarcinoma cells. Biochim. Biophys. Acta 2010, 1798:1512-1521.
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 1512-1521
    • Baron, S.1
  • 74
    • 33746189734 scopus 로고    scopus 로고
    • Energetics and kinetics of cooperative cofilin-actin filament interactions
    • Cao W., et al. Energetics and kinetics of cooperative cofilin-actin filament interactions. J. Mol. Biol. 2006, 361:257-267.
    • (2006) J. Mol. Biol. , vol.361 , pp. 257-267
    • Cao, W.1
  • 75
    • 84867628329 scopus 로고    scopus 로고
    • Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness
    • Kang H., et al. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proc. Natl. Acad. Sci. U.S.A. 2012, 109:16923-16927.
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 16923-16927
    • Kang, H.1
  • 76
    • 0029664786 scopus 로고    scopus 로고
    • 2+-binding protein localized to the Golgi lumen
    • 2+-binding protein localized to the Golgi lumen. J. Cell Biol. 1996, 133:257-268.
    • (1996) J. Cell Biol. , vol.133 , pp. 257-268
    • Scherer, P.E.1
  • 77
    • 0024454546 scopus 로고
    • Perturbation of cellular calcium induces secretion of luminal ER proteins
    • Booth C., Koch G.L. Perturbation of cellular calcium induces secretion of luminal ER proteins. Cell 1989, 59:729-737.
    • (1989) Cell , vol.59 , pp. 729-737
    • Booth, C.1    Koch, G.L.2
  • 78
    • 0025361036 scopus 로고
    • The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum
    • Sambrook J.F. The involvement of calcium in transport of secretory proteins from the endoplasmic reticulum. Cell 1990, 61:197-199.
    • (1990) Cell , vol.61 , pp. 197-199
    • Sambrook, J.F.1
  • 79
    • 84861658918 scopus 로고    scopus 로고
    • Secreted kinase phosphorylates extracellular proteins that regulate biomineralization
    • Tagliabracci V.S., et al. Secreted kinase phosphorylates extracellular proteins that regulate biomineralization. Science 2012, 336:1150-1153.
    • (2012) Science , vol.336 , pp. 1150-1153
    • Tagliabracci, V.S.1
  • 80
    • 0023077578 scopus 로고
    • Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi
    • Pfeffer S.R., Rothman J.E. Biosynthetic protein transport and sorting by the endoplasmic reticulum and Golgi. Annu. Rev. Biochem. 1987, 56:829-852.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 829-852
    • Pfeffer, S.R.1    Rothman, J.E.2
  • 81
    • 70649088120 scopus 로고    scopus 로고
    • Bulk flow revisited: transport of a soluble protein in the secretory pathway
    • Thor F., et al. Bulk flow revisited: transport of a soluble protein in the secretory pathway. Traffic 2009, 10:1819-1830.
    • (2009) Traffic , vol.10 , pp. 1819-1830
    • Thor, F.1
  • 82
    • 0022452276 scopus 로고
    • Re-routing of a secretory protein by fusion with human growth hormone sequences
    • Moore H.H., Kelly R.B. Re-routing of a secretory protein by fusion with human growth hormone sequences. Nature 1986, 321:443-446.
    • (1986) Nature , vol.321 , pp. 443-446
    • Moore, H.H.1    Kelly, R.B.2
  • 84
    • 0023652396 scopus 로고
    • A C-terminal signal prevents secretion of luminal ER proteins
    • Munro S., Pelham H.R. A C-terminal signal prevents secretion of luminal ER proteins. Cell 1987, 48:899-907.
    • (1987) Cell , vol.48 , pp. 899-907
    • Munro, S.1    Pelham, H.R.2
  • 85
    • 34548625556 scopus 로고    scopus 로고
    • Unsolved mysteries in membrane traffic
    • Pfeffer S.R. Unsolved mysteries in membrane traffic. Annu. Rev. Biochem. 2007, 76:629-645.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 629-645
    • Pfeffer, S.R.1
  • 87
    • 0032589231 scopus 로고    scopus 로고
    • Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells
    • Ohno H., et al. Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells. FEBS Lett. 1999, 449:215-220.
    • (1999) FEBS Lett. , vol.449 , pp. 215-220
    • Ohno, H.1
  • 89
    • 0042591490 scopus 로고    scopus 로고
    • Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi
    • Wang Y.J., et al. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell 2003, 114:299-310.
    • (2003) Cell , vol.114 , pp. 299-310
    • Wang, Y.J.1
  • 90
    • 67650500688 scopus 로고    scopus 로고
    • Clathrin adaptor AP1B controls adenovirus infectivity of epithelial cells
    • Diaz F., et al. Clathrin adaptor AP1B controls adenovirus infectivity of epithelial cells. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:11143-11148.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 11143-11148
    • Diaz, F.1
  • 91
    • 0035809211 scopus 로고    scopus 로고
    • Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells
    • Fölsch H., et al. Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells. J. Cell Biol. 2001, 152:595-606.
    • (2001) J. Cell Biol. , vol.152 , pp. 595-606
    • Fölsch, H.1
  • 92
    • 51649127294 scopus 로고    scopus 로고
    • Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells
    • Nokes R.L., et al. Rab13 regulates membrane trafficking between TGN and recycling endosomes in polarized epithelial cells. J. Cell Biol. 2008, 182:845-853.
    • (2008) J. Cell Biol. , vol.182 , pp. 845-853
    • Nokes, R.L.1
  • 93
    • 84887564752 scopus 로고    scopus 로고
    • The adaptor protein-1μ1B subunit expands the repertoire of basolateral sorting signal recognition in epithelial cells
    • Guo X., et al. The adaptor protein-1μ1B subunit expands the repertoire of basolateral sorting signal recognition in epithelial cells. Dev. Cell 2013, 27:353-366.
    • (2013) Dev. Cell , vol.27 , pp. 353-366
    • Guo, X.1
  • 94
    • 0038795645 scopus 로고    scopus 로고
    • Signals for sorting of transmembrane proteins to endosomes and lysosomes
    • Bonifacino J.S., Traub L.M. Signals for sorting of transmembrane proteins to endosomes and lysosomes. Annu. Rev. Biochem. 2003, 72:395-447.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 395-447
    • Bonifacino, J.S.1    Traub, L.M.2
  • 95
    • 20544431747 scopus 로고    scopus 로고
    • Protein sorting in the Golgi complex: shifting paradigms
    • Rodriguez-Boulan E., Müsch A. Protein sorting in the Golgi complex: shifting paradigms. Biochim. Biophys. Acta 2005, 1744:455-464.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 455-464
    • Rodriguez-Boulan, E.1    Müsch, A.2
  • 96
    • 84879037961 scopus 로고    scopus 로고
    • A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network
    • Guo Y., et al. A novel GTP-binding protein-adaptor protein complex responsible for export of Vangl2 from the trans Golgi network. Elife 2013, 2:e00160.
    • (2013) Elife , vol.2 , pp. e00160
    • Guo, Y.1
  • 97
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D., Simons K. Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 98
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: new tools and insights
    • Simons K., Gerl M.J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 2010, 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 99
    • 77954299061 scopus 로고    scopus 로고
    • A comprehensive comparison of transmembrane domains reveals organelle-specific properties
    • Sharpe H.J., et al. A comprehensive comparison of transmembrane domains reveals organelle-specific properties. Cell 2010, 142:158-169.
    • (2010) Cell , vol.142 , pp. 158-169
    • Sharpe, H.J.1
  • 100
    • 33749011468 scopus 로고    scopus 로고
    • Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast
    • Wang C-W., et al. Exomer: A coat complex for transport of select membrane proteins from the trans-Golgi network to the plasma membrane in yeast. J. Cell Biol. 2006, 174:973-983.
    • (2006) J. Cell Biol. , vol.174 , pp. 973-983
    • Wang, C.-W.1
  • 101
    • 79953155321 scopus 로고    scopus 로고
    • Transport to the plasma membrane is regulated differently early and late in the cell cycle in Saccharomyces cerevisiae
    • Zanolari B., et al. Transport to the plasma membrane is regulated differently early and late in the cell cycle in Saccharomyces cerevisiae. J. Cell Sci. 2011, 124:1055-1066.
    • (2011) J. Cell Sci. , vol.124 , pp. 1055-1066
    • Zanolari, B.1
  • 102
    • 0035046029 scopus 로고    scopus 로고
    • The oligomeric nature of Na/K-transport ATPase
    • Taniguchi K., et al. The oligomeric nature of Na/K-transport ATPase. J. Biochem. 2001, 129:335-342.
    • (2001) J. Biochem. , vol.129 , pp. 335-342
    • Taniguchi, K.1
  • 104
    • 84876440888 scopus 로고    scopus 로고
    • CRISPR-Cas systems and RNA-guided interference
    • Barrangou R. CRISPR-Cas systems and RNA-guided interference. Wiley Interdiscip. Rev. RNA 2013, 4:267-278.
    • (2013) Wiley Interdiscip. Rev. RNA , vol.4 , pp. 267-278
    • Barrangou, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.