메뉴 건너뛰기




Volumn 22, Issue 12, 2008, Pages 2583-2595

How peptide hormone vesicles are transported to the secretion site for exocytosis

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; CLATHRIN; DOCKING PROTEIN; F ACTIN; GUANOSINE TRIPHOSPHATE; KINESIN 1; KINESIN 2; MEMBRANE LIPID; MEMBRANE PROTEIN; MOLECULAR MOTOR; PEPTIDE HORMONE; RAB27A PROTEIN;

EID: 56749175040     PISSN: 08888809     EISSN: None     Source Type: Journal    
DOI: 10.1210/me.2008-0209     Document Type: Short Survey
Times cited : (58)

References (148)
  • 4
    • 0034589372 scopus 로고    scopus 로고
    • Neurotrophins and activity-dependent plasticity
    • Thoenen H 2000 Neurotrophins and activity-dependent plasticity. Prog Brain Res 128:183-191
    • (2000) Prog Brain Res , vol.128 , pp. 183-191
    • Thoenen, H.1
  • 5
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly RB 1985 Pathways of protein secretion in eukaryotes. Science 230:25-32
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 6
    • 0028969528 scopus 로고
    • Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface
    • Futter CE, Connolly CN, Cutler DF, Hopkins CR 1995 Newly synthesized transferrin receptors can be detected in the endosome before they appear on the cell surface. J Biol Chem 270:10999-11003
    • (1995) J Biol Chem , vol.270 , pp. 10999-11003
    • Futter, C.E.1    Connolly, C.N.2    Cutler, D.F.3    Hopkins, C.R.4
  • 7
    • 0038603127 scopus 로고    scopus 로고
    • Constitutive protein secretion from the trans-Golgi network to the plasma membrane
    • Ponnambalam S, Baldwin SA 2003 Constitutive protein secretion from the trans-Golgi network to the plasma membrane. Mol Membr Biol 20:129-139
    • (2003) Mol Membr Biol , vol.20 , pp. 129-139
    • Ponnambalam, S.1    Baldwin, S.A.2
  • 8
    • 0023658351 scopus 로고
    • The rate of bulk flow from the endoplasmic reticulum to the cell surface
    • Wieland FT, Gleason ML, Serafini TA, Rothman JE 1987 The rate of bulk flow from the endoplasmic reticulum to the cell surface. Cell 50:289-300
    • (1987) Cell , vol.50 , pp. 289-300
    • Wieland, F.T.1    Gleason, M.L.2    Serafini, T.A.3    Rothman, J.E.4
  • 9
    • 0027396746 scopus 로고
    • Subtype-specific differences in the intracellular sorting of G protein-coupled receptors
    • von Zastrow M, Link R, Daunt D, Barsh G, Kobilka B 1993 Subtype-specific differences in the intracellular sorting of G protein-coupled receptors. J Biol Chem 268:763-766
    • (1993) J Biol Chem , vol.268 , pp. 763-766
    • von Zastrow, M.1    Link, R.2    Daunt, D.3    Barsh, G.4    Kobilka, B.5
  • 10
    • 0021267181 scopus 로고
    • Somatostatin discriminates between the intracellular pathways of secretory and membrane proteins
    • Green R, Shields D 1984 Somatostatin discriminates between the intracellular pathways of secretory and membrane proteins. J Cell Biol 99:97-104
    • (1984) J Cell Biol , vol.99 , pp. 97-104
    • Green, R.1    Shields, D.2
  • 12
    • 0033851201 scopus 로고    scopus 로고
    • Basic mechanisms of secretion: Sorting into the regulated secretory pathway
    • Blazquez M, Shennan KI 2000 Basic mechanisms of secretion: sorting into the regulated secretory pathway. Biochem Cell Biol 78:181-191
    • (2000) Biochem Cell Biol , vol.78 , pp. 181-191
    • Blazquez, M.1    Shennan, K.I.2
  • 13
    • 34247543907 scopus 로고    scopus 로고
    • Sending proteins to dense core secretory granules: Still a lot to sort out
    • Dikeakos JD, Reudelhuber TL 2007 Sending proteins to dense core secretory granules: still a lot to sort out. J Cell Biol 177:191-196
    • (2007) J Cell Biol , vol.177 , pp. 191-196
    • Dikeakos, J.D.1    Reudelhuber, T.L.2
  • 14
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles
    • Bauerfeind R, Huttner WB 1993 Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles. Curr Opin Cell Biol 5:628-635
    • (1993) Curr Opin Cell Biol , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 15
    • 9544255798 scopus 로고    scopus 로고
    • Secretory granule targeting of atrial natriuretic peptide correlates with its calcium-mediated aggregation
    • Canaff L, Brechler V, Reudelhuber TL, Thibault G 1996 Secretory granule targeting of atrial natriuretic peptide correlates with its calcium-mediated aggregation. Proc Natl Acad Sci USA 93:9483-9487
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9483-9487
    • Canaff, L.1    Brechler, V.2    Reudelhuber, T.L.3    Thibault, G.4
  • 16
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E, Huttner WB 1991 Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol 115:1505-1519
    • (1991) J Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 17
    • 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, Argos P, Huttner WB 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    Argos, P.6    Huttner, W.B.7
  • 18
    • 0030976604 scopus 로고    scopus 로고
    • Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpe(fat) mice
    • Cool DR, Normant E, Shen F, Chen HC, Pannell L, Zhang Y, Loh YP 1997 Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe(fat) mice. Cell 88:73-83
    • (1997) Cell , vol.88 , pp. 73-83
    • Cool, D.R.1    Normant, E.2    Shen, F.3    Chen, H.C.4    Pannell, L.5    Zhang, Y.6    Loh, Y.P.7
  • 19
    • 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, Kim SK, Zaitsev E, Snell CR, Lu B, Loh YP 2005 Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase E. Neuron 45:245-255
    • (2005) Neuron , vol.45 , pp. 245-255
    • Lou, H.1    Kim, S.K.2    Zaitsev, E.3    Snell, C.R.4    Lu, B.5    Loh, Y.P.6
  • 20
    • 0036800341 scopus 로고    scopus 로고
    • Identification of a chromogranin A domain that mediates binding to secretogranin III and targeting to secretory granules in pituitary cells and pancreatic β-cells
    • Hosaka M, Watanabe T, Sakai Y, Uchiyama Y, Takeuchi T 2002 Identification of a chromogranin A domain that mediates binding to secretogranin III and targeting to secretory granules in pituitary cells and pancreatic β-cells. Mol Biol Cell 13:3388-3399
    • (2002) Mol Biol Cell , vol.13 , pp. 3388-3399
    • Hosaka, M.1    Watanabe, T.2    Sakai, Y.3    Uchiyama, Y.4    Takeuchi, T.5
  • 21
    • 27844494185 scopus 로고    scopus 로고
    • Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules
    • Hosaka M, Watanabe T, Sakai Y, Kato T, Takeuchi T 2005 Interaction between secretogranin III and carboxypeptidase E facilitates prohormone sorting within secretory granules. J Cell Sci 118:4785-4795
    • (2005) J Cell Sci , vol.118 , pp. 4785-4795
    • Hosaka, M.1    Watanabe, T.2    Sakai, Y.3    Kato, T.4    Takeuchi, T.5
  • 22
    • 0030035227 scopus 로고    scopus 로고
    • Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein
    • Milgram SL, Mains RE, Eipper BA 1996 Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein. J Biol Chem 271:17526-17535
    • (1996) J Biol Chem , vol.271 , pp. 17526-17535
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 24
    • 2942720796 scopus 로고    scopus 로고
    • The C-terminus of prohormone convertase 2 is sufficient and necessary for Raft association and sorting to the regulated secretory pathway
    • Assadi M, Sharpe JC, Snell C, Loh YP 2004 The C-terminus of prohormone convertase 2 is sufficient and necessary for Raft association and sorting to the regulated secretory pathway. Biochemistry 43:7798-7807
    • (2004) Biochemistry , vol.43 , pp. 7798-7807
    • Assadi, M.1    Sharpe, J.C.2    Snell, C.3    Loh, Y.P.4
  • 25
    • 0034703034 scopus 로고    scopus 로고
    • Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor
    • Dhanvantari S, Loh YP 2000 Lipid raft association of carboxypeptidase E is necessary for its function as a regulated secretory pathway sorting receptor. J Biol Chem 275:29887-29893
    • (2000) J Biol Chem , vol.275 , pp. 29887-29893
    • Dhanvantari, S.1    Loh, Y.P.2
  • 26
    • 0037325451 scopus 로고    scopus 로고
    • Sorting of carboxypeptidase E to the regulated secretory pathway requires interaction of its transmembrane domain with lipid rafts
    • Zhang CF, Dhanvantari S, Lou H, Loh YP 2003 Sorting of carboxypeptidase E to the regulated secretory pathway requires interaction of its transmembrane domain with lipid rafts. Biochem J 369:453-460
    • (2003) Biochem J , vol.369 , pp. 453-460
    • Zhang, C.F.1    Dhanvantari, S.2    Lou, H.3    Loh, Y.P.4
  • 27
    • 0345687330 scopus 로고    scopus 로고
    • Recycling of Raft-associated prohormone sorting receptor carboxypeptidase E requires interaction with ARF6
    • Arnaoutova I, Jackson CL, Al-Awar OS, Donaldson JG, Loh YP 2003 Recycling of Raft-associated prohormone sorting receptor carboxypeptidase E requires interaction with ARF6. Mol Biol Cell 14:4448-4457
    • (2003) Mol Biol Cell , vol.14 , pp. 4448-4457
    • Arnaoutova, I.1    Jackson, C.L.2    Al-Awar, O.S.3    Donaldson, J.G.4    Loh, Y.P.5
  • 28
    • 4744357518 scopus 로고    scopus 로고
    • Membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells
    • Wu CM, Chang HT, Chang MD 2004 Membrane-bound carboxypeptidase E facilitates the entry of eosinophil cationic protein into neuroendocrine cells. Biochem J 382:841-848
    • (2004) Biochem J , vol.382 , pp. 841-848
    • Wu, C.M.1    Chang, H.T.2    Chang, M.D.3
  • 29
    • 0036701575 scopus 로고    scopus 로고
    • Lumenal protein multimerization in the distal secretory pathway/secretory granules
    • Arvan P, Zhang BY, Feng L, Liu M, Kuliawat R 2002 Lumenal protein multimerization in the distal secretory pathway/secretory granules. Curr Opin Cell Biol 14:448-453
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 448-453
    • Arvan, P.1    Zhang, B.Y.2    Feng, L.3    Liu, M.4    Kuliawat, R.5
  • 30
    • 0034043450 scopus 로고    scopus 로고
    • Signal-mediated sorting of neuropeptides and prohormones: Secretory granule biogenesis revisited
    • Glombik MM, Gerdes HH 2000 Signal-mediated sorting of neuropeptides and prohormones: secretory granule biogenesis revisited. Biochimie 82:315-326
    • (2000) Biochimie , vol.82 , pp. 315-326
    • Glombik, M.M.1    Gerdes, H.H.2
  • 31
    • 0029589423 scopus 로고
    • The granin family - its role in sorting and secretory granule formation
    • Ozawa H, Takata K 1995 The granin family - its role in sorting and secretory granule formation. Cell Struct Funct 20:415-420
    • (1995) Cell Struct Funct , vol.20 , pp. 415-420
    • Ozawa, H.1    Takata, K.2
  • 32
    • 0032177313 scopus 로고    scopus 로고
    • Protein and lipid sorting from the trans-Golgi network to secretory granules-recent developments
    • Thiele C, Huttner WB 1998 Protein and lipid sorting from the trans-Golgi network to secretory granules-recent developments. Semin Cell Dev Biol 9:511-516
    • (1998) Semin Cell Dev Biol , vol.9 , pp. 511-516
    • Thiele, C.1    Huttner, W.B.2
  • 33
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • Arvan P, Castle D 1998 Sorting and storage during secretory granule biogenesis: looking backward and looking forward. Biochem J 332:593-610
    • (1998) Biochem J , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 35
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban PA, Irminger JC 1994 Sorting and processing of secretory proteins. Biochem J 299:1-18
    • (1994) Biochem J , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.C.2
  • 36
    • 0033062601 scopus 로고    scopus 로고
    • Protein hormone storage in secretory granules: Mechanisms for concentration and sorting
    • Dannies PS 1999 Protein hormone storage in secretory granules: mechanisms for concentration and sorting. Endocr Rev 20:3-21
    • (1999) Endocr Rev , vol.20 , pp. 3-21
    • Dannies, P.S.1
  • 37
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells
    • Kuliawat R, Klumperman J, Ludwig T, Arvan P 1997 Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells. J Cell Biol 137:595-608
    • (1997) J Cell Biol , vol.137 , pp. 595-608
    • Kuliawat, R.1    Klumperman, J.2    Ludwig, T.3    Arvan, P.4
  • 38
    • 0030792177 scopus 로고    scopus 로고
    • Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation
    • Dittie AS, Thomas L, Thomas G, Tooze SA 1997 Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation. 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
  • 39
    • 0035341464 scopus 로고    scopus 로고
    • PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic
    • Crump CM, Xiang Y, Thomas L, Gu F, Austin C, Tooze SA, Thomas G 2001 PACS-1 binding to adaptors is required for acidic cluster motif-mediated protein traffic. EMBO J 20:2191-2201
    • (2001) EMBO J , vol.20 , pp. 2191-2201
    • Crump, C.M.1    Xiang, Y.2    Thomas, L.3    Gu, F.4    Austin, C.5    Tooze, S.A.6    Thomas, G.7
  • 40
    • 1342289620 scopus 로고    scopus 로고
    • The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads
    • Nakayama K, Wakatsuki S 2003 The structure and function of GGAs, the traffic controllers at the TGN sorting crossroads. Cell Struct Funct 28:431-442
    • (2003) Cell Struct Funct , vol.28 , pp. 431-442
    • Nakayama, K.1    Wakatsuki, S.2
  • 41
    • 0023194305 scopus 로고
    • Use of a synthetic peptide antigen to generate antisera reactive with a proteolytic processing site in native human proinsulin: Demonstration of cleavage within clathrin-coated (pro)secretory vesicles
    • Steiner DF, Michael J, Houghten R, Mathieu M, Gardner PR, Ravazzola M, Orci L 1987 Use of a synthetic peptide antigen to generate antisera reactive with a proteolytic processing site in native human proinsulin: demonstration of cleavage within clathrin-coated (pro)secretory vesicles. Proc Natl Acad Sci USA 84:6184-6188
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 6184-6188
    • Steiner, D.F.1    Michael, J.2    Houghten, R.3    Mathieu, M.4    Gardner, P.R.5    Ravazzola, M.6    Orci, L.7
  • 42
    • 0040142226 scopus 로고    scopus 로고
    • Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins
    • Teuchert M, Schafer W, Berghofer S, Hoflack B, Klenk HD, Garten W 1999 Sorting of furin at the trans-Golgi network. Interaction of the cytoplasmic tail sorting signals with AP-1 Golgi-specific assembly proteins. J Biol Chem 274:8199-8207
    • (1999) J Biol Chem , vol.274 , pp. 8199-8207
    • Teuchert, M.1    Schafer, W.2    Berghofer, S.3    Hoflack, B.4    Klenk, H.D.5    Garten, W.6
  • 43
    • 0023008920 scopus 로고
    • Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells
    • Tooze J, Tooze SA 1986 Clathrin-coated vesicular transport of secretory proteins during the formation of ACTH-containing secretory granules in AtT20 cells. J Cell Biol 103:839-850
    • (1986) J Cell Biol , vol.103 , pp. 839-850
    • Tooze, J.1    Tooze, S.A.2
  • 44
    • 0035021147 scopus 로고    scopus 로고
    • Trafficking of yellow-fluorescent-protein-tagged mu1 subunit of clathrin adaptor AP-1 complex in living cells
    • Huang F, Nesterov A, Carter RE, Sorkin A 2001 Trafficking of yellow-fluorescent-protein-tagged mu1 subunit of clathrin adaptor AP-1 complex in living cells. Traffic 2:345-357
    • (2001) Traffic , vol.2 , pp. 345-357
    • Huang, F.1    Nesterov, A.2    Carter, R.E.3    Sorkin, A.4
  • 45
    • 0347762565 scopus 로고    scopus 로고
    • The GGA proteins: Adaptors on the move
    • Bonifacino JS 2004 The GGA proteins: adaptors on the move. Nat Rev Mol Cell Biol 5:23-32
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 23-32
    • Bonifacino, J.S.1
  • 46
    • 0037031658 scopus 로고    scopus 로고
    • Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network
    • Doray B, Ghosh P, Griffith J, Geuze HJ, Kornfeld S 2002 Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network. Science 297:1700-1703
    • (2002) Science , vol.297 , pp. 1700-1703
    • Doray, B.1    Ghosh, P.2    Griffith, J.3    Geuze, H.J.4    Kornfeld, S.5
  • 47
    • 0036791359 scopus 로고    scopus 로고
    • Furin at the cutting edge: From protein traffic to embryogenesis and disease
    • Thomas G 2002 Furin at the cutting edge: from protein traffic to embryogenesis and disease. Nat Rev Mol Cell Biol 3:753-766
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 753-766
    • Thomas, G.1
  • 48
    • 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
  • 49
    • 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
  • 50
    • 0033491889 scopus 로고    scopus 로고
    • The majority of clathrin coated vesicles from lactating rabbit mammary gland arises from the secretory pathway
    • Pauloin A, Tooze SA, Michelutti I, Delpal S, Ollivier-Bousquet M 1999 The majority of clathrin coated vesicles from lactating rabbit mammary gland arises from the secretory pathway. J Cell Sci 112:4089-4100
    • (1999) J Cell Sci , vol.112 , pp. 4089-4100
    • Pauloin, A.1    Tooze, S.A.2    Michelutti, I.3    Delpal, S.4    Ollivier-Bousquet, M.5
  • 52
    • 0032845769 scopus 로고    scopus 로고
    • γ-Synergin: An EH domain-containing protein that interacts with γ-adaptin
    • Page LJ, Sowerby PJ, Lui WW, Robinson MS 1999 γ-Synergin: an EH domain-containing protein that interacts with γ-adaptin. J Cell Biol 146:993-1004
    • (1999) J Cell Biol , vol.146 , pp. 993-1004
    • Page, L.J.1    Sowerby, P.J.2    Lui, W.W.3    Robinson, M.S.4
  • 55
    • 23944455380 scopus 로고    scopus 로고
    • Colchicine treatment differently affects releasable thyrotropin-releasing hormone (TRH) pools in the hypothalamic paraventricular nucleus (PVN) and the median eminence (ME)
    • Alexander K, Nikodemova M, Kucerova J, Strbak V 2005 Colchicine treatment differently affects releasable thyrotropin-releasing hormone (TRH) pools in the hypothalamic paraventricular nucleus (PVN) and the median eminence (ME). Cell Mol Neurobiol 25:681-695
    • (2005) Cell Mol Neurobiol , vol.25 , pp. 681-695
    • Alexander, K.1    Nikodemova, M.2    Kucerova, J.3    Strbak, V.4
  • 56
    • 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 HH 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
  • 57
    • 0034078008 scopus 로고    scopus 로고
    • Microtubule-based transport systems in neurons: The roles of kinesins and dyneins
    • Goldstein LS, Yang Z 2000 Microtubule-based transport systems in neurons: the roles of kinesins and dyneins. Annu Rev Neurosci 23:39-71
    • (2000) Annu Rev Neurosci , vol.23 , pp. 39-71
    • Goldstein, L.S.1    Yang, Z.2
  • 59
    • 0023292982 scopus 로고
    • Characterization of an islet carboxypeptidase B involved in prohormone processing
    • Mackin RB, Noe BD 1987 Characterization of an islet carboxypeptidase B involved in prohormone processing. Endocrinology 120:457-468
    • (1987) Endocrinology , vol.120 , pp. 457-468
    • Mackin, R.B.1    Noe, B.D.2
  • 60
    • 0023655547 scopus 로고
    • The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing
    • Davidson HW, Hutton JC 1987 The insulin-secretory-granule carboxypeptidase H. Purification and demonstration of involvement in proinsulin processing. Biochem J 245:575-582
    • (1987) Biochem J , vol.245 , pp. 575-582
    • Davidson, H.W.1    Hutton, J.C.2
  • 61
    • 0025049062 scopus 로고
    • 2-terminal sequences
    • 2-terminal sequences. J Biol Chem 265:17101-17105
    • (1990) J Biol Chem , vol.265 , pp. 17101-17105
    • Parkinson, D.1
  • 62
    • 0025327208 scopus 로고
    • Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10)
    • Fricker LD, Das B, Angeletti RH 1990 Identification of the pH-dependent membrane anchor of carboxypeptidase E (EC 3.4.17.10). J Biol Chem 265:2476-2482
    • (1990) J Biol Chem , vol.265 , pp. 2476-2482
    • Fricker, L.D.1    Das, B.2    Angeletti, R.H.3
  • 63
    • 0027929948 scopus 로고
    • The C-terminal region of carboxypeptidase E is involved in membrane binding and intracellular routing in AtT-20 cells
    • Mitra A, Song L, Fricker LD 1994 The C-terminal region of carboxypeptidase E is involved in membrane binding and intracellular routing in AtT-20 cells. J Biol Chem 269:19876-19881
    • (1994) J Biol Chem , vol.269 , pp. 19876-19881
    • Mitra, A.1    Song, L.2    Fricker, L.D.3
  • 64
    • 41649089832 scopus 로고    scopus 로고
    • Carboxypeptidase E cytoplasmic tail-driven vesicle transport is key for activity-dependent secretion of peptide hormones
    • Park JJ, Cawley NX, Loh YP 2008 Carboxypeptidase E cytoplasmic tail-driven vesicle transport is key for activity-dependent secretion of peptide hormones. Mol Endocrinol 22:989-1005
    • (2008) Mol Endocrinol , vol.22 , pp. 989-1005
    • Park, J.J.1    Cawley, N.X.2    Loh, Y.P.3
  • 65
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata H, Nakamura Y, Hayakawa A, Takata H, Suzuki T, Miyazawa K, Kitamura N 2003 A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J Biol Chem 278:22946-22955
    • (2003) J Biol Chem , vol.278 , pp. 22946-22955
    • Inomata, H.1    Nakamura, Y.2    Hayakawa, A.3    Takata, H.4    Suzuki, T.5    Miyazawa, K.6    Kitamura, N.7
  • 66
    • 0037205493 scopus 로고    scopus 로고
    • Interaction of Alzheimer's β-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade
    • Taru H, Iijima K, Hase M, Kirino Y, Yagi Y, Suzuki T 2002 Interaction of Alzheimer's β-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J Biol Chem 277:20070-20078
    • (2002) J Biol Chem , vol.277 , pp. 20070-20078
    • Taru, H.1    Iijima, K.2    Hase, M.3    Kirino, Y.4    Yagi, Y.5    Suzuki, T.6
  • 67
    • 0031079682 scopus 로고    scopus 로고
    • Cholinergic stimulation of lacrimal acinar cells promotes redistribution of membrane-associated kinesin and the secretory protein, β-hexosaminidase, and increases kinesin motor activity
    • Hamm-Alvarez SF, Da Costa S, Yang T, Wei X, Gierow JP, Mircheff AK 1997 Cholinergic stimulation of lacrimal acinar cells promotes redistribution of membrane-associated kinesin and the secretory protein, β-hexosaminidase, and increases kinesin motor activity. Exp Eye Res 64:141-156
    • (1997) Exp Eye Res , vol.64 , pp. 141-156
    • Hamm-Alvarez, S.F.1    Da Costa, S.2    Yang, T.3    Wei, X.4    Gierow, J.P.5    Mircheff, A.K.6
  • 68
    • 0033605213 scopus 로고    scopus 로고
    • Kinesin cross-bridges between neurosecretory granules and microtubules in the mouse neurohypophysis
    • Senda T, Yu W 1999 Kinesin cross-bridges between neurosecretory granules and microtubules in the mouse neurohypophysis. Neurosci Lett 262:69-71
    • (1999) Neurosci Lett , vol.262 , pp. 69-71
    • Senda, T.1    Yu, W.2
  • 69
    • 0242362834 scopus 로고    scopus 로고
    • Kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 β-cells
    • Varadi A, Tsuboi T, Johnson-Cadwell LI, Allan VJ, Rutter GA 2003 Kinesin I and cytoplasmic dynein orchestrate glucose-stimulated insulin-containing vesicle movements in clonal MIN6 β-cells. Biochem Biophys Res Commun 311:272-282
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 272-282
    • Varadi, A.1    Tsuboi, T.2    Johnson-Cadwell, L.I.3    Allan, V.J.4    Rutter, G.A.5
  • 70
    • 0025844789 scopus 로고
    • Kinesin-related gene unc-104 is required for axonal transport of synaptic vesicles in C. elegans
    • Hall DH, Hedgecock EM 1991 Kinesin-related gene unc-104 is required for axonal transport of synaptic vesicles in C. elegans. Cell 65:837-847
    • (1991) Cell , vol.65 , pp. 837-847
    • Hall, D.H.1    Hedgecock, E.M.2
  • 72
    • 0035819072 scopus 로고    scopus 로고
    • UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans
    • Byrd DT, Kawasaki M, Walcoff M, Hisamoto N, Matsumoto K, Jin Y 2001 UNC-16, a JNK-signaling scaffold protein, regulates vesicle transport in C. elegans. Neuron 32:787-800
    • (2001) Neuron , vol.32 , pp. 787-800
    • Byrd, D.T.1    Kawasaki, M.2    Walcoff, M.3    Hisamoto, N.4    Matsumoto, K.5    Jin, Y.6
  • 74
    • 0031951523 scopus 로고    scopus 로고
    • Changes in kinesin distribution and phosphorylation occur during regulated secretion in pancreatic acinar cells
    • Marlowe KJ, Farshori P, Torgerson RR, Anderson KL, Miller LJ, McNiven MA 1998 Changes in kinesin distribution and phosphorylation occur during regulated secretion in pancreatic acinar cells. Eur J Cell Biol 75:140-152
    • (1998) Eur J Cell Biol , vol.75 , pp. 140-152
    • Marlowe, K.J.1    Farshori, P.2    Torgerson, R.R.3    Anderson, K.L.4    Miller, L.J.5    McNiven, M.A.6
  • 77
    • 0036469290 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility
    • Morfini G, Szebenyi G, Elluru R, Ratner N, Brady ST 2002 Glycogen synthase kinase 3 phosphorylates kinesin light chains and negatively regulates kinesin-based motility. EMBO J 21:281-293
    • (2002) EMBO J , vol.21 , pp. 281-293
    • Morfini, G.1    Szebenyi, G.2    Elluru, R.3    Ratner, N.4    Brady, S.T.5
  • 79
    • 0036776122 scopus 로고    scopus 로고
    • Globular tail fragment of myosin-V displaces vesicle-associated motor and blocks vesicle transport in squid nerve cell extracts
    • Brown JR, Peacock-Villada EM, Langford GM 2002 Globular tail fragment of myosin-V displaces vesicle-associated motor and blocks vesicle transport in squid nerve cell extracts. Biol Bull 203:210-211
    • (2002) Biol Bull , vol.203 , pp. 210-211
    • Brown, J.R.1    Peacock-Villada, E.M.2    Langford, G.M.3
  • 80
    • 0034752888 scopus 로고    scopus 로고
    • Recombinant globular tail fragment of myosin-V blocks vesicle transport in squid nerve cell extracts
    • Brown JR, Simonetta KR, Sandberg LA, Stafford P, Langford GM 2001 Recombinant globular tail fragment of myosin-V blocks vesicle transport in squid nerve cell extracts. Biol Bull 201:240-241
    • (2001) Biol Bull , vol.201 , pp. 240-241
    • Brown, J.R.1    Simonetta, K.R.2    Sandberg, L.A.3    Stafford, P.4    Langford, G.M.5
  • 82
    • 0033960789 scopus 로고    scopus 로고
    • Membrane trafficking, organelle transport, and the cytoskeleton
    • Rogers SL, Gelfand VI 2000 Membrane trafficking, organelle transport, and the cytoskeleton. Curr Opin Cell Biol 12:57-62
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 57-62
    • Rogers, S.L.1    Gelfand, V.I.2
  • 83
    • 0032576569 scopus 로고    scopus 로고
    • Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast
    • Pruyne DW, Schott DH, Bretscher A 1998 Tropomyosin-containing actin cables direct the Myo2p-dependent polarized delivery of secretory vesicles in budding yeast. J Cell Biol 143:1931-1945
    • (1998) J Cell Biol , vol.143 , pp. 1931-1945
    • Pruyne, D.W.1    Schott, D.H.2    Bretscher, A.3
  • 85
    • 0037387771 scopus 로고    scopus 로고
    • Myosins II and V in chromaffin cells: Myosin V is a chromaffin vesicle molecular motor involved in secretion
    • Rose SD, Lejen T, Casaletti L, Larson RE, Pene TD, Trifaro JM 2003 Myosins II and V in chromaffin cells: myosin V is a chromaffin vesicle molecular motor involved in secretion. J Neurochem 85:287-298
    • (2003) J Neurochem , vol.85 , pp. 287-298
    • Rose, S.D.1    Lejen, T.2    Casaletti, L.3    Larson, R.E.4    Pene, T.D.5    Trifaro, J.M.6
  • 87
    • 25644458576 scopus 로고    scopus 로고
    • Constitutive secretion of protease nexin-1 by glial cells and its regulation by G-protein-coupled receptors
    • Giau R, Carrette J, Bockaert J, Homburger V 2005 Constitutive secretion of protease nexin-1 by glial cells and its regulation by G-protein-coupled receptors. J Neurosci 25:8995-9004
    • (2005) J Neurosci , vol.25 , pp. 8995-9004
    • Giau, R.1    Carrette, J.2    Bockaert, J.3    Homburger, V.4
  • 89
    • 26944465715 scopus 로고    scopus 로고
    • Myosin 5a controls insulin granule recruitment during late-phase secretion
    • Ivarsson R, Jing X, Waselle L, Regazzi R, Renstrom E 2005 Myosin 5a controls insulin granule recruitment during late-phase secretion. Traffic 6:1027-1035
    • (2005) Traffic , vol.6 , pp. 1027-1035
    • Ivarsson, R.1    Jing, X.2    Waselle, L.3    Regazzi, R.4    Renstrom, E.5
  • 90
    • 19644364331 scopus 로고    scopus 로고
    • Myosin Va transports dense core secretory vesicles in pancreatic MIN6 β-cells
    • Varadi A, Tsuboi T, Rutter GA 2005 Myosin Va transports dense core secretory vesicles in pancreatic MIN6 β-cells. Mol Biol Cell 16:2670-2680
    • (2005) Mol Biol Cell , vol.16 , pp. 2670-2680
    • Varadi, A.1    Tsuboi, T.2    Rutter, G.A.3
  • 91
    • 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
  • 93
    • 10344242949 scopus 로고    scopus 로고
    • Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme
    • Alam MR, Caldwell BD, Johnson RC, Darlington DN, Mains RE, Eipper BA 1996 Novel proteins that interact with the COOH-terminal cytosolic routing determinants of an integral membrane peptide-processing enzyme. J Biol Chem 271:28636-28640
    • (1996) J Biol Chem , vol.271 , pp. 28636-28640
    • Alam, M.R.1    Caldwell, B.D.2    Johnson, R.C.3    Darlington, D.N.4    Mains, R.E.5    Eipper, B.A.6
  • 94
    • 0033521020 scopus 로고    scopus 로고
    • The novel kinase peptidylglycine α-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine α-amidating monooxygenase
    • Caldwell BD, Darlington DN, Penzes P, Johnson RC, Eipper BA, Mains RE 1999 The novel kinase peptidylglycine α-amidating monooxygenase cytosolic interactor protein 2 interacts with the cytosolic routing determinants of the peptide processing enzyme peptidylglycine α-amidating monooxygenase. J Biol Chem 274:34646-34656
    • (1999) J Biol Chem , vol.274 , pp. 34646-34656
    • Caldwell, B.D.1    Darlington, D.N.2    Penzes, P.3    Johnson, R.C.4    Eipper, B.A.5    Mains, R.E.6
  • 95
    • 0033613833 scopus 로고    scopus 로고
    • Kalirin, a multifunctional PAM COOH-terminal domain interactor protein, affects cytoskeletal organization and ACTH secretion from AtT-20 cells
    • Mains RE, Alam MR, Johnson RC, Darlington DN, Back N, Hand TA, Eipper BA 1999 Kalirin, a multifunctional PAM COOH-terminal domain interactor protein, affects cytoskeletal organization and ACTH secretion from AtT-20 cells. J Biol Chem 274:2929-2937
    • (1999) J Biol Chem , vol.274 , pp. 2929-2937
    • Mains, R.E.1    Alam, M.R.2    Johnson, R.C.3    Darlington, D.N.4    Back, N.5    Hand, T.A.6    Eipper, B.A.7
  • 98
    • 0029843493 scopus 로고    scopus 로고
    • The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush DR, Maurice T, Roth D, Novick P 1996 The exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J 15:6483-6494
    • (1996) EMBO J , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 100
    • 33745746188 scopus 로고    scopus 로고
    • Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering
    • Inoue M, Chiang SH, Chang L, Chen XW, Saltiel AR 2006 Compartmentalization of the exocyst complex in lipid rafts controls Glut4 vesicle tethering. Mol Biol Cell 17:2303-2311
    • (2006) Mol Biol Cell , vol.17 , pp. 2303-2311
    • Inoue, M.1    Chiang, S.H.2    Chang, L.3    Chen, X.W.4    Saltiel, A.R.5
  • 101
    • 0038376537 scopus 로고    scopus 로고
    • Insulin signaling: GLUT4 vesicles exit via the exocyst
    • Kanzaki M, Pessin JE 2003 Insulin signaling: GLUT4 vesicles exit via the exocyst. Curr Biol 13:R574-R576
    • (2003) Curr Biol , vol.13
    • Kanzaki, M.1    Pessin, J.E.2
  • 102
    • 33646123087 scopus 로고    scopus 로고
    • Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane
    • Gerges NZ, Backos DS, Rupasinghe CN, Spaller MR, Esteban JA 2006 Dual role of the exocyst in AMPA receptor targeting and insertion into the postsynaptic membrane. EMBO J 25:1623-1634
    • (2006) EMBO J , vol.25 , pp. 1623-1634
    • Gerges, N.Z.1    Backos, D.S.2    Rupasinghe, C.N.3    Spaller, M.R.4    Esteban, J.A.5
  • 104
    • 0242266915 scopus 로고    scopus 로고
    • The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains
    • Folsch H, Pypaert M, Maday S, Pelletier L, Mellman I 2003 The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains. J Cell Biol 163:351-362
    • (2003) J Cell Biol , vol.163 , pp. 351-362
    • Folsch, H.1    Pypaert, M.2    Maday, S.3    Pelletier, L.4    Mellman, I.5
  • 105
    • 34548188298 scopus 로고    scopus 로고
    • Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c
    • Chen XW, Leto D, Chiang SH, Wang Q, Saltiel AR 2007 Activation of RalA is required for insulin-stimulated Glut4 trafficking to the plasma membrane via the exocyst and the motor protein Myo1c. Dev Cell 13:391-404
    • (2007) Dev Cell , vol.13 , pp. 391-404
    • Chen, X.W.1    Leto, D.2    Chiang, S.H.3    Wang, Q.4    Saltiel, A.R.5
  • 106
    • 49649090688 scopus 로고    scopus 로고
    • The RalA GTPase is a central regulator of insulin exocytosis from pancreatic islet β-cells
    • Lopez JA, Kwan EP, Xie L, He Y, James DE, Gaisano HY 2008 The RalA GTPase is a central regulator of insulin exocytosis from pancreatic islet β-cells. J Biol Chem 283:17939-17945
    • (2008) J Biol Chem , vol.283 , pp. 17939-17945
    • Lopez, J.A.1    Kwan, E.P.2    Xie, L.3    He, Y.4    James, D.E.5    Gaisano, H.Y.6
  • 109
    • 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
  • 110
    • 34247333875 scopus 로고    scopus 로고
    • Differential dynamics of Rab3A and Rab27A on secretory granules
    • Handley MT, Haynes LP, Burgoyne RD 2007 Differential dynamics of Rab3A and Rab27A on secretory granules. J Cell Sci 120:973-984
    • (2007) J Cell Sci , vol.120 , pp. 973-984
    • Handley, M.T.1    Haynes, L.P.2    Burgoyne, R.D.3
  • 111
    • 0031454368 scopus 로고    scopus 로고
    • Overexpression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice
    • Ohnishi H, Samuelson LC, Yule DI, Ernst SA, Williams JA 1997 Overexpression of Rab3D enhances regulated amylase secretion from pancreatic acini of transgenic mice. J Clin Invest 100:3044-3052
    • (1997) J Clin Invest , vol.100 , pp. 3044-3052
    • Ohnishi, H.1    Samuelson, L.C.2    Yule, D.I.3    Ernst, S.A.4    Williams, J.A.5
  • 114
    • 0032702830 scopus 로고    scopus 로고
    • High affinity Rab3 binding is dispensable for Rabphilin-dependent potentiation of stimulated secretion
    • Joberty G, Stabila PF, Coppola T, Macara IG, Regazzi R 1999 High affinity Rab3 binding is dispensable for Rabphilin-dependent potentiation of stimulated secretion. J Cell Sci 112:3579-3587
    • (1999) J Cell Sci , vol.112 , pp. 3579-3587
    • Joberty, G.1    Stabila, P.F.2    Coppola, T.3    Macara, I.G.4    Regazzi, R.5
  • 115
    • 0029077932 scopus 로고
    • Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells
    • Chung SH, Takai Y, Holz RW 1995 Evidence that the Rab3a-binding protein, rabphilin3a, enhances regulated secretion. Studies in adrenal chromaffin cells. J Biol Chem 270:16714-16718
    • (1995) J Biol Chem , vol.270 , pp. 16714-16718
    • Chung, S.H.1    Takai, Y.2    Holz, R.W.3
  • 116
    • 0030877243 scopus 로고    scopus 로고
    • Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion
    • Wang Y, Okamoto M, Schmitz F, Hofmann K, Sudhof TC 1997 Rim is a putative Rab3 effector in regulating synaptic-vesicle fusion. Nature 388:593-598
    • (1997) Nature , vol.388 , pp. 593-598
    • Wang, Y.1    Okamoto, M.2    Schmitz, F.3    Hofmann, K.4    Sudhof, T.C.5
  • 117
    • 0027370160 scopus 로고
    • Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein
    • Kishida S, Shirataki H, Sasaki T, Kato M, Kaibuchi K, Takai Y 1993 Rab3A GTPase-activating protein-inhibiting activity of Rabphilin-3A, a putative Rab3A target protein. J Biol Chem 268:22259-22261
    • (1993) J Biol Chem , vol.268 , pp. 22259-22261
    • Kishida, S.1    Shirataki, H.2    Sasaki, T.3    Kato, M.4    Kaibuchi, K.5    Takai, Y.6
  • 120
    • 0037171801 scopus 로고    scopus 로고
    • RIM binding proteins (RBPs) couple Rab3-interacting molecules (RIMs) to voltage-gated Ca(2+) channels
    • Hibino H, Pironkova R, Onwumere O, Vologodskaia M, Hudspeth AJ, Lesage F 2002 RIM binding proteins (RBPs) couple Rab3-interacting molecules (RIMs) to voltage-gated Ca(2+) channels. Neuron 34:411-423
    • (2002) Neuron , vol.34 , pp. 411-423
    • Hibino, H.1    Pironkova, R.2    Onwumere, O.3    Vologodskaia, M.4    Hudspeth, A.J.5    Lesage, F.6
  • 121
    • 0037187643 scopus 로고    scopus 로고
    • Drosophila liprin-α and the receptor phosphatase Dlar control synapse morphogenesis
    • Kaufmann N, DeProto J, Ranjan R, Wan H, Van Vactor D 2002 Drosophila liprin-α and the receptor phosphatase Dlar control synapse morphogenesis. Neuron 34:27-38
    • (2002) Neuron , vol.34 , pp. 27-38
    • Kaufmann, N.1    DeProto, J.2    Ranjan, R.3    Wan, H.4    Van Vactor, D.5
  • 122
    • 0037195108 scopus 로고    scopus 로고
    • A family of RIM-binding proteins regulated by alternative splicing: Implications for the genesis of synaptic active zones
    • Wang Y, Liu X, Biederer T, Sudhof TC 2002 A family of RIM-binding proteins regulated by alternative splicing: implications for the genesis of synaptic active zones. Proc Natl Acad Sci USA 99:14464-14469
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14464-14469
    • Wang, Y.1    Liu, X.2    Biederer, T.3    Sudhof, T.C.4
  • 123
    • 0035971104 scopus 로고    scopus 로고
    • A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells
    • Haynes LP, Evans GJ, Morgan A, Burgoyne RD 2001 A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells. J Biol Chem 276:9726-9732
    • (2001) J Biol Chem , vol.276 , pp. 9726-9732
    • Haynes, L.P.1    Evans, G.J.2    Morgan, A.3    Burgoyne, R.D.4
  • 124
    • 0037131362 scopus 로고    scopus 로고
    • Slp4-a/granuphilin-a regulates dense-core vesicle exocytosis in PC12 cells
    • Fukuda M, Kanno E, Saegusa C, Ogata Y, Kuroda TS 2002 Slp4-a/granuphilin-a regulates dense-core vesicle exocytosis in PC12 cells. J Biol Chem 277:39673-39678
    • (2002) J Biol Chem , vol.277 , pp. 39673-39678
    • Fukuda, M.1    Kanno, E.2    Saegusa, C.3    Ogata, Y.4    Kuroda, T.S.5
  • 126
    • 2542463861 scopus 로고    scopus 로고
    • Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a
    • Torii S, Takeuchi T, Nagamatsu S, Izumi T 2004 Rab27 effector granuphilin promotes the plasma membrane targeting of insulin granules via interaction with syntaxin 1a. J Biol Chem 279:22532-22538
    • (2004) J Biol Chem , vol.279 , pp. 22532-22538
    • Torii, S.1    Takeuchi, T.2    Nagamatsu, S.3    Izumi, T.4
  • 127
    • 1342310841 scopus 로고    scopus 로고
    • The roles of Rab27 and its effectors in the regulated secretory pathways
    • Izumi T, Gomi H, Kasai K, Mizutani S, Torii S 2003 The roles of Rab27 and its effectors in the regulated secretory pathways. Cell Struct Funct 28:465-474
    • (2003) Cell Struct Funct , vol.28 , pp. 465-474
    • Izumi, T.1    Gomi, H.2    Kasai, K.3    Mizutani, S.4    Torii, S.5
  • 130
    • 33845933426 scopus 로고    scopus 로고
    • Illuminating membrane fusion
    • Rizo J 2006 Illuminating membrane fusion. Proc Natl Acad Sci USA 103:19611-19612
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 19611-19612
    • Rizo, J.1
  • 131
    • 23944501982 scopus 로고    scopus 로고
    • SNARE complexes prepare for membrane fusion
    • Sorensen JB 2005 SNARE complexes prepare for membrane fusion. Trends Neurosci 28:453-455
    • (2005) Trends Neurosci , vol.28 , pp. 453-455
    • Sorensen, J.B.1
  • 132
    • 15944374827 scopus 로고    scopus 로고
    • Ca2+-regulated exocytosis and SNARE function
    • Stojilkovic SS 2005 Ca2+-regulated exocytosis and SNARE function. Trends Endocrinol Metab 16:81-83
    • (2005) Trends Endocrinol Metab , vol.16 , pp. 81-83
    • Stojilkovic, S.S.1
  • 133
    • 15544382560 scopus 로고    scopus 로고
    • Synaptic vesicle docking: A putative role for the Munc18/Sec1 protein family
    • Weimer RM, Richmond JE 2005 Synaptic vesicle docking: a putative role for the Munc18/Sec1 protein family. Curr Top Dev Biol 65:83-113
    • (2005) Curr Top Dev Biol , vol.65 , pp. 83-113
    • Weimer, R.M.1    Richmond, J.E.2
  • 134
    • 0037672843 scopus 로고    scopus 로고
    • The molecular machinery of synaptic vesicle exocytosis
    • Li L, Chin LS 2003 The molecular machinery of synaptic vesicle exocytosis. Cell Mol Life Sci 60:942-960
    • (2003) Cell Mol Life Sci , vol.60 , pp. 942-960
    • Li, L.1    Chin, L.S.2
  • 136
    • 33746102907 scopus 로고    scopus 로고
    • Back on track - on the role of the microtubule for kinesin motility and cellular function
    • Lakamper S, Meyhofer E 2006 Back on track - on the role of the microtubule for kinesin motility and cellular function. J Muscle Res Cell Motil 27:161-171
    • (2006) J Muscle Res Cell Motil , vol.27 , pp. 161-171
    • Lakamper, S.1    Meyhofer, E.2
  • 137
    • 0033558093 scopus 로고    scopus 로고
    • The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis
    • Guo W, Roth D, Walch-Solimena C, Novick P 1999 The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J 18:1071-1080
    • (1999) EMBO J , vol.18 , pp. 1071-1080
    • Guo, W.1    Roth, D.2    Walch-Solimena, C.3    Novick, P.4
  • 141
    • 9244243320 scopus 로고    scopus 로고
    • Hither and yon: A review of bi-directional microtubule-based transport
    • Gross SP 2004 Hither and yon: a review of bi-directional microtubule-based transport. Phys Biol 1:R1-R11
    • (2004) Phys Biol , vol.1
    • Gross, S.P.1
  • 142
    • 20344382542 scopus 로고    scopus 로고
    • Kinesin and dynein move a peroxisome in vivo: A tug-of-war or coordinated movement?
    • Kural C, Kim H, Syed S, Goshima G, Gelfand VI, Selvin PR 2005 Kinesin and dynein move a peroxisome in vivo: a tug-of-war or coordinated movement? Science 308:1469-1472
    • (2005) Science , vol.308 , pp. 1469-1472
    • Kural, C.1    Kim, H.2    Syed, S.3    Goshima, G.4    Gelfand, V.I.5    Selvin, P.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.