메뉴 건너뛰기




Volumn 8, Issue 3, 2013, Pages

Rab3D Is Critical for Secretory Granule Maturation in PC12 Cells

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; F ACTIN; FURIN; ISOPROTEIN; RAB PROTEIN; RAB3A PROTEIN; RAB3D PROTEIN; SECRETOGRANIN II; UNCLASSIFIED DRUG;

EID: 84875087422     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0057321     Document Type: Article
Times cited : (17)

References (47)
  • 1
    • 0024414397 scopus 로고
    • Biosynthetic protein transport in the secretory pathway
    • Huttner WB, Tooze SA, (1989) Biosynthetic protein transport in the secretory pathway. Curr Opin Cell Biol 1: 648-654.
    • (1989) Curr Opin Cell Biol , vol.1 , pp. 648-654
    • Huttner, W.B.1    Tooze, S.A.2
  • 2
    • 0034762729 scopus 로고    scopus 로고
    • Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction and F-actin-dependent tethering
    • Rudolf R, Salm T, Rustom A, Gerdes H-H, (2001) Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction and F-actin-dependent tethering. Mol Biol Cell 12: 1353-1365.
    • (2001) Mol Biol Cell , vol.12 , pp. 1353-1365
    • Rudolf, R.1    Salm, T.2    Rustom, A.3    Gerdes, H.-H.4
  • 3
    • 0037383440 scopus 로고    scopus 로고
    • Myosin Va facilitates the distribution of secretory granules in the F-actin rich cortex of PC12 cells
    • Rudolf R, Kogel T, Kuznetsov SA, Salm T, Schlicker O, et al. (2003) Myosin Va facilitates the distribution of secretory granules in the F-actin rich cortex of PC12 cells. J Cell Sci 116: 1339-1348.
    • (2003) J Cell Sci , vol.116 , pp. 1339-1348
    • Rudolf, R.1    Kogel, T.2    Kuznetsov, S.A.3    Salm, T.4    Schlicker, O.5
  • 4
    • 0026332190 scopus 로고
    • Characterization of the immature secretory granule, an intermediate in granule biogenesis
    • Tooze SA, Flatmark T, Tooze J, Huttner WB, (1991) Characterization of the immature secretory granule, an intermediate in granule biogenesis. J Cell Biol 115: 1491-1503.
    • (1991) J Cell Biol , vol.115 , pp. 1491-1503
    • Tooze, S.A.1    Flatmark, T.2    Tooze, J.3    Huttner, W.B.4
  • 5
    • 0032576576 scopus 로고    scopus 로고
    • Homotypic fusion of immature secretory granules during maturation in a cell-free assay
    • Urbe S, Page LJ, Tooze SA, (1998) Homotypic fusion of immature secretory granules during maturation in a cell-free assay. J Cell Biol 143: 1831-1844.
    • (1998) J Cell Biol , vol.143 , pp. 1831-1844
    • Urbe, S.1    Page, L.J.2    Tooze, S.A.3
  • 6
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
    • Gerdes HH, Rosa P, Phillips E, Baeuerle PA, Frank R, et al. (1989) The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation. J Biol Chem 264: 12009-12015.
    • (1989) J Biol Chem , vol.264 , pp. 12009-12015
    • Gerdes, H.H.1    Rosa, P.2    Phillips, E.3    Baeuerle, P.A.4    Frank, R.5
  • 7
    • 0031033158 scopus 로고    scopus 로고
    • pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules
    • Urbe S, Dittie AS, Tooze SA, (1997) pH-dependent processing of secretogranin II by the endopeptidase PC2 in isolated immature secretory granules. Biochem J 321: 65-74.
    • (1997) Biochem J , vol.321 , pp. 65-74
    • Urbe, S.1    Dittie, A.S.2    Tooze, S.A.3
  • 9
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittie AS, Hajibagheri N, Tooze SA, (1996) The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J Cell Biol 132: 523-536.
    • (1996) J Cell Biol , vol.132 , pp. 523-536
    • Dittie, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 10
    • 0030792177 scopus 로고    scopus 로고
    • Furin is sorted into the regulated secretory pathway in neuroendocrine cells, interacts with the AP-1 complex, and is removed during granule maturation by a casein kinase II dependent mechanism
    • Dittie AS, Thomas L, Thomas G, Tooze SA, (1997) Furin is sorted into the regulated secretory pathway in neuroendocrine cells, interacts with the AP-1 complex, and is removed during granule maturation by a casein kinase II dependent mechanism. EMBO J 16: 4859-4870.
    • (1997) EMBO J , vol.16 , pp. 4859-4870
    • Dittie, A.S.1    Thomas, L.2    Thomas, G.3    Tooze, S.A.4
  • 11
    • 0032550222 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles
    • Klumperman J, Kuliawat R, Griffith JM, Geuze HJ, Arvan P, (1998) Mannose 6-phosphate receptors are sorted from immature secretory granules via adaptor protein AP-1, clathrin, and syntaxin 6-positive vesicles. J Cell Biol 141: 359-371.
    • (1998) J Cell Biol , vol.141 , pp. 359-371
    • Klumperman, J.1    Kuliawat, R.2    Griffith, J.M.3    Geuze, H.J.4    Arvan, P.5
  • 12
    • 0033492232 scopus 로고    scopus 로고
    • Differential distribution of mannose-6-phosphate receptors and furin in immature secretory granules
    • Dittie AS, Klumperman J, Tooze SA, (1999) Differential distribution of mannose-6-phosphate receptors and furin in immature secretory granules. J Cell Sci 112: 3955-3966.
    • (1999) J Cell Sci , vol.112 , pp. 3955-3966
    • Dittie, A.S.1    Klumperman, J.2    Tooze, S.A.3
  • 13
    • 0034307475 scopus 로고    scopus 로고
    • Biogenesis of regulated exocytotic carriers in neuroendocrine cells
    • Eaton BA, Haugwitz M, Lau D, Moore HP, (2000) Biogenesis of regulated exocytotic carriers in neuroendocrine cells. J Neurosci 20: 7334-7344.
    • (2000) J Neurosci , vol.20 , pp. 7334-7344
    • Eaton, B.A.1    Haugwitz, M.2    Lau, D.3    Moore, H.P.4
  • 14
    • 77953149779 scopus 로고    scopus 로고
    • Distinct roles of myosin Va in membrane remodeling and exocytosis of secretory granules
    • Kogel T, Rudolf R, Hodneland E, Hellwig A, Kuznetsov SA, et al. (2010) Distinct roles of myosin Va in membrane remodeling and exocytosis of secretory granules. Traffic 11: 637-650.
    • (2010) Traffic , vol.11 , pp. 637-650
    • Kogel, T.1    Rudolf, R.2    Hodneland, E.3    Hellwig, A.4    Kuznetsov, S.A.5
  • 15
    • 0034723263 scopus 로고    scopus 로고
    • Characterization of myosin V binding to brain vesicles
    • Miller KE, Sheetz MP, (2000) Characterization of myosin V binding to brain vesicles. J Biol Chem 275: 2598-2606.
    • (2000) J Biol Chem , vol.275 , pp. 2598-2606
    • Miller, K.E.1    Sheetz, M.P.2
  • 16
    • 0037067673 scopus 로고    scopus 로고
    • A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport
    • Strom M, Hume AN, Tarafder AK, Barkagianni E, Seabra MC, (2002) A family of Rab27-binding proteins. Melanophilin links Rab27a and myosin Va function in melanosome transport. J Biol Chem 277: 25423-25430.
    • (2002) J Biol Chem , vol.277 , pp. 25423-25430
    • Strom, M.1    Hume, A.N.2    Tarafder, A.K.3    Barkagianni, E.4    Seabra, M.C.5
  • 17
    • 0037165662 scopus 로고    scopus 로고
    • Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions
    • Nagashima K, Torii S, Yi Z, Igarashi M, Okamoto K, et al. (2002) Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions. FEBS Lett 517: 233-238.
    • (2002) FEBS Lett , vol.517 , pp. 233-238
    • Nagashima, K.1    Torii, S.2    Yi, Z.3    Igarashi, M.4    Okamoto, K.5
  • 18
    • 0037044819 scopus 로고    scopus 로고
    • Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin
    • Fukuda M, Kuroda TS, (2002) Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin. J Biol Chem 277: 43096-43103.
    • (2002) J Biol Chem , vol.277 , pp. 43096-43103
    • Fukuda, M.1    Kuroda, T.S.2
  • 19
    • 83255167070 scopus 로고    scopus 로고
    • Molecular mechanism of myosin Va recruitment to dense core secretory granules
    • Brozzi F, Diraison F, Lajus S, Rajatileka S, Philips T, et al. (2012) Molecular mechanism of myosin Va recruitment to dense core secretory granules. Traffic 13: 54-69.
    • (2012) Traffic , vol.13 , pp. 54-69
    • Brozzi, F.1    Diraison, F.2    Lajus, S.3    Rajatileka, S.4    Philips, T.5
  • 20
    • 0034624037 scopus 로고    scopus 로고
    • Crystal structures of a Rab protein in its inactive and active conformations
    • Stroupe C, Brunger AT, (2000) Crystal structures of a Rab protein in its inactive and active conformations. J Mol Biol 304: 585-598.
    • (2000) J Mol Biol , vol.304 , pp. 585-598
    • Stroupe, C.1    Brunger, A.T.2
  • 21
    • 0025787279 scopus 로고
    • rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif
    • Kinsella BT, Maltese WA, (1991) rab GTP-binding proteins implicated in vesicular transport are isoprenylated in vitro at cysteines within a novel carboxyl-terminal motif. J Biol Chem 266: 8540-8544.
    • (1991) J Biol Chem , vol.266 , pp. 8540-8544
    • Kinsella, B.T.1    Maltese, W.A.2
  • 22
    • 33745508887 scopus 로고    scopus 로고
    • Rab3A and Rab27A cooperatively regulate the docking step of dense-core vesicle exocytosis in PC12 cells
    • Tsuboi T, Fukuda M, (2006) Rab3A and Rab27A cooperatively regulate the docking step of dense-core vesicle exocytosis in PC12 cells. J Cell Sci 119: 2196-2203.
    • (2006) J Cell Sci , vol.119 , pp. 2196-2203
    • Tsuboi, T.1    Fukuda, M.2
  • 23
    • 0033581022 scopus 로고    scopus 로고
    • Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3
    • Chung SH, Joberty G, Gelino EA, Macara IG, Holz RW, (1999) Comparison of the effects on secretion in chromaffin and PC12 cells of Rab3 family members and mutants. Evidence that inhibitory effects are independent of direct interaction with Rabphilin3. J Biol Chem 274: 18113-18120.
    • (1999) J Biol Chem , vol.274 , pp. 18113-18120
    • Chung, S.H.1    Joberty, G.2    Gelino, E.A.3    Macara, I.G.4    Holz, R.W.5
  • 24
    • 0037175049 scopus 로고    scopus 로고
    • Localization versus function of Rab3 proteins. Evidence for a common regulatory role in controlling fusion
    • Schluter OM, Khvotchev M, Jahn R, Sudhof TC, (2002) Localization versus function of Rab3 proteins. Evidence for a common regulatory role in controlling fusion. J Biol Chem 277: 40919-40929.
    • (2002) J Biol Chem , vol.277 , pp. 40919-40929
    • Schluter, O.M.1    Khvotchev, M.2    Jahn, R.3    Sudhof, T.C.4
  • 25
    • 0142074731 scopus 로고    scopus 로고
    • Weibel-Palade bodies recruit Rab27 by a content-driven, maturation-dependent mechanism that is independent of cell type
    • Hannah MJ, Hume AN, Arribas M, Williams R, Hewlett LJ, et al. (2003) Weibel-Palade bodies recruit Rab27 by a content-driven, maturation-dependent mechanism that is independent of cell type. J Cell Sci 116: 3939-3948.
    • (2003) J Cell Sci , vol.116 , pp. 3939-3948
    • Hannah, M.J.1    Hume, A.N.2    Arribas, M.3    Williams, R.4    Hewlett, L.J.5
  • 26
    • 56649111420 scopus 로고    scopus 로고
    • Kinetics of Rab27a-dependent actions on vesicle docking and priming in pancreatic beta-cells
    • Merrins MJ, Stuenkel EL, (2008) Kinetics of Rab27a-dependent actions on vesicle docking and priming in pancreatic beta-cells. J Physiol 586: 5367-5381.
    • (2008) J Physiol , vol.586 , pp. 5367-5381
    • Merrins, M.J.1    Stuenkel, E.L.2
  • 27
    • 2142695916 scopus 로고    scopus 로고
    • Subcellular distribution and function of Rab3A, B, C, and D isoforms in insulin-secreting cells
    • Iezzi M, Escher G, Meda P, Charollais A, Baldini G, et al. (1999) Subcellular distribution and function of Rab3A, B, C, and D isoforms in insulin-secreting cells. Mol Endocrinol 13: 202-212.
    • (1999) Mol Endocrinol , vol.13 , pp. 202-212
    • Iezzi, M.1    Escher, G.2    Meda, P.3    Charollais, A.4    Baldini, G.5
  • 28
    • 0030964893 scopus 로고    scopus 로고
    • Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor
    • Wu X, Bowers B, Wei Q, Kocher B, Hammer JA III, (1997) Myosin V associates with melanosomes in mouse melanocytes: evidence that myosin V is an organelle motor. J Cell Sci 110: 847-859.
    • (1997) J Cell Sci , vol.110 , pp. 847-859
    • Wu, X.1    Bowers, B.2    Wei, Q.3    Kocher, B.4    Hammer III, J.A.5
  • 29
    • 0031748734 scopus 로고    scopus 로고
    • Myosin Va associates with microtubule-rich domains in both interphase and dividing cells
    • Wu X, Kocher B, Wei Q, Hammer JA III, (1998) Myosin Va associates with microtubule-rich domains in both interphase and dividing cells. Cell Motil Cytoskeleton 40: 286-303.
    • (1998) Cell Motil Cytoskeleton , vol.40 , pp. 286-303
    • Wu, X.1    Kocher, B.2    Wei, Q.3    Hammer III, J.A.4
  • 30
    • 0030696255 scopus 로고    scopus 로고
    • Targeting of green fluorescent protein to neuroendocrine secretory granules: a new tool for real time studies of regulated protein secretion
    • Kaether C, Salm T, Glombik M, Almers W, Gerdes H-H, (1997) Targeting of green fluorescent protein to neuroendocrine secretory granules: a new tool for real time studies of regulated protein secretion. Eur J Cell Biol 74: 133-142.
    • (1997) Eur J Cell Biol , vol.74 , pp. 133-142
    • Kaether, C.1    Salm, T.2    Glombik, M.3    Almers, W.4    Gerdes, H.-H.5
  • 31
    • 0020578970 scopus 로고
    • Relationship between NGF-mediated volume increase and "priming effect" in fast and slow reacting clones of PC12 pheochromocytoma cells
    • Heumann R, Kachel V, Thoenen H, (1983) Relationship between NGF-mediated volume increase and "priming effect" in fast and slow reacting clones of PC12 pheochromocytoma cells. Exp Cell Res 145: 179-190.
    • (1983) Exp Cell Res , vol.145 , pp. 179-190
    • Heumann, R.1    Kachel, V.2    Thoenen, H.3
  • 32
    • 0028033742 scopus 로고
    • An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network
    • Ohashi M, Huttner WB, (1994) An elevation of cytosolic protein phosphorylation modulates trimeric G-protein regulation of secretory vesicle formation from the trans-Golgi network. J Biol Chem 269: 24897-24905.
    • (1994) J Biol Chem , vol.269 , pp. 24897-24905
    • Ohashi, M.1    Huttner, W.B.2
  • 33
    • 0034568261 scopus 로고    scopus 로고
    • Rab3A and Rab3D control the total granule number and the fraction of granules docked at the plasma membrane in PC12 cells
    • Martelli AM, Baldini G, Tabellini G, Koticha D, Bareggi R, (2000) Rab3A and Rab3D control the total granule number and the fraction of granules docked at the plasma membrane in PC12 cells. Traffic 1: 976-986.
    • (2000) Traffic , vol.1 , pp. 976-986
    • Martelli, A.M.1    Baldini, G.2    Tabellini, G.3    Koticha, D.4    Bareggi, R.5
  • 34
    • 0348010367 scopus 로고    scopus 로고
    • Dominant negative Rab3D mutants reduce GTP-bound endogenous Rab3D in pancreatic acini
    • Chen X, Ernst SA, Williams JA, (2003) Dominant negative Rab3D mutants reduce GTP-bound endogenous Rab3D in pancreatic acini. J Biol Chem 278: 50053-50060.
    • (2003) J Biol Chem , vol.278 , pp. 50053-50060
    • Chen, X.1    Ernst, S.A.2    Williams, J.A.3
  • 36
    • 77953149779 scopus 로고    scopus 로고
    • Distinct Roles of Myosin Va in Membrane Remodeling and Exocytosis of Secretory Granules
    • Kogel T, Rudolf R, Hodneland E, Hellwig A, Kuznetsov SA, et al. (2010) Distinct Roles of Myosin Va in Membrane Remodeling and Exocytosis of Secretory Granules. Traffic.
    • (2010) Traffic
    • Kogel, T.1    Rudolf, R.2    Hodneland, E.3    Hellwig, A.4    Kuznetsov, S.A.5
  • 37
    • 0033773259 scopus 로고    scopus 로고
    • Expression and localization of rab escort protein isoforms in parotid acinar cells from rat
    • Chan D, Lin J, Raffaniello RD, (2000) Expression and localization of rab escort protein isoforms in parotid acinar cells from rat. J Cell Physiol 185: 339-347.
    • (2000) J Cell Physiol , vol.185 , pp. 339-347
    • Chan, D.1    Lin, J.2    Raffaniello, R.D.3
  • 38
    • 0036724568 scopus 로고    scopus 로고
    • RaB3D Is Not Required for Exocrine Exocytosis but for Maintenance of Normally Sized Secretory Granules
    • Riedel D, Antonin W, Fernandez-Chacon R, Alvarez de Toledo G, Jo T, et al. (2002) RaB3D Is Not Required for Exocrine Exocytosis but for Maintenance of Normally Sized Secretory Granules. Mol Cell Biol 22: 6487-6497.
    • (2002) Mol Cell Biol , vol.22 , pp. 6487-6497
    • Riedel, D.1    Antonin, W.2    Fernandez-Chacon, R.3    Alvarez de Toledo, G.4    Jo, T.5
  • 39
    • 0021051920 scopus 로고
    • Increase in zymogen granule volume accounts for increase in volume density during prenatal development of pancreas
    • Ermak TH, Rothman SS, (1983) Increase in zymogen granule volume accounts for increase in volume density during prenatal development of pancreas. Anat Rec 207: 487-501.
    • (1983) Anat Rec , vol.207 , pp. 487-501
    • Ermak, T.H.1    Rothman, S.S.2
  • 40
    • 0032567763 scopus 로고    scopus 로고
    • Expression of Rab3D N135I inhibits regulated secretion of ACTH in AtT-20 cells
    • Baldini G, Wang G, Weber M, Zweyer M, Bareggi R, et al. (1998) Expression of Rab3D N135I inhibits regulated secretion of ACTH in AtT-20 cells. J Cell Biol 140: 305-313.
    • (1998) J Cell Biol , vol.140 , pp. 305-313
    • Baldini, G.1    Wang, G.2    Weber, M.3    Zweyer, M.4    Bareggi, R.5
  • 41
    • 33646112380 scopus 로고    scopus 로고
    • Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells
    • Ahras M, Otto GP, Tooze SA, (2006) Synaptotagmin IV is necessary for the maturation of secretory granules in PC12 cells. J Cell Biol 173: 241-251.
    • (2006) J Cell Biol , vol.173 , pp. 241-251
    • Ahras, M.1    Otto, G.P.2    Tooze, S.A.3
  • 42
    • 33646151413 scopus 로고    scopus 로고
    • GGA function is required for maturation of neuroendocrine secretory granules
    • Kakhlon O, Sakya P, Larijani B, Watson R, Tooze SA, (2006) GGA function is required for maturation of neuroendocrine secretory granules. Embo J 25: 1590-1602.
    • (2006) Embo J , vol.25 , pp. 1590-1602
    • Kakhlon, O.1    Sakya, P.2    Larijani, B.3    Watson, R.4    Tooze, S.A.5
  • 43
    • 0030856189 scopus 로고    scopus 로고
    • Distinct molecular events during secretory granule biogenesis revealed by sensitivities to brefeldin A
    • Fernandez CJ, Haugwitz M, Eaton B, Moore HP, (1997) Distinct molecular events during secretory granule biogenesis revealed by sensitivities to brefeldin A. Mol Biol Cell 8: 2171-2185.
    • (1997) Mol Biol Cell , vol.8 , pp. 2171-2185
    • Fernandez, C.J.1    Haugwitz, M.2    Eaton, B.3    Moore, H.P.4
  • 45
    • 16644377748 scopus 로고    scopus 로고
    • Role of synaptotagmin and its related molecules in regulated secretion
    • Fukuda M, (2004) Role of synaptotagmin and its related molecules in regulated secretion. Tanpakushitsu Kakusan Koso 49: 2186-2197.
    • (2004) Tanpakushitsu Kakusan Koso , vol.49 , pp. 2186-2197
    • Fukuda, M.1
  • 46
  • 47
    • 1542289732 scopus 로고    scopus 로고
    • Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis
    • Shibasaki T, Sunaga Y, Fujimoto K, Kashima Y, Seino S, (2004) Interaction of ATP sensor, cAMP sensor, Ca2+ sensor, and voltage-dependent Ca2+ channel in insulin granule exocytosis. J Biol Chem 279: 7956-7961.
    • (2004) J Biol Chem , vol.279 , pp. 7956-7961
    • Shibasaki, T.1    Sunaga, Y.2    Fujimoto, K.3    Kashima, Y.4    Seino, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.