메뉴 건너뛰기




Volumn 14, Issue 4, 2002, Pages 448-453

Lumenal protein multimerization in the distal secretory pathway/secretory granules

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN LUMENAL; SECRETORY PROTEIN; UNCLASSIFIED DRUG; CARRIER PROTEIN; PROTEIN; PROTEIN PRECURSOR;

EID: 0036701575     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(02)00344-7     Document Type: Review
Times cited : (43)

References (67)
  • 1
    • 0035147424 scopus 로고    scopus 로고
    • Multicolour imaging of post-Golgi sorting and trafficking in live cells
    • Keller P., Toomre D., Diaz E., White J., Simons K. Multicolour imaging of post-Golgi sorting and trafficking in live cells. Nat Cell Biol. 3:2001;140-149.
    • (2001) Nat Cell Biol , vol.3 , pp. 140-149
    • Keller, P.1    Toomre, D.2    Diaz, E.3    White, J.4    Simons, K.5
  • 2
    • 0028920154 scopus 로고
    • The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack
    • Miesenbock G., Rothman J.E. The capacity to retrieve escaped ER proteins extends to the trans-most cisterna of the Golgi stack. J Cell Biol. 129:1995;309-319.
    • (1995) J Cell Biol , vol.129 , pp. 309-319
    • Miesenbock, G.1    Rothman, J.E.2
  • 4
    • 0035369692 scopus 로고    scopus 로고
    • Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor
    • Zhu Y., Doray B., Poussu A., Lehto V.P., Kornfeld S. Binding of GGA2 to the lysosomal enzyme sorting motif of the mannose 6-phosphate receptor. Science. 292:2001;1716-1718.
    • (2001) Science , vol.292 , pp. 1716-1718
    • Zhu, Y.1    Doray, B.2    Poussu, A.3    Lehto, V.P.4    Kornfeld, S.5
  • 5
    • 0037059451 scopus 로고    scopus 로고
    • Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane
    • Baron C.L., Malhotra V. Role of diacylglycerol in PKD recruitment to the TGN and protein transport to the plasma membrane. Science. 295:2002;325-328.
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 6
    • 0035013167 scopus 로고    scopus 로고
    • The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers
    • Brown D.L., Heimann K., Lock J., Kjer-Nielsen L., van Vliet C., Stow J.L., Gleeson P.A. The GRIP domain is a specific targeting sequence for a population of trans-Golgi network derived tubulo-vesicular carriers. Traffic. 2:2001;336-344.
    • (2001) Traffic , vol.2 , pp. 336-344
    • Brown, D.L.1    Heimann, K.2    Lock, J.3    Kjer-Nielsen, L.4    Van Vliet, C.5    Stow, J.L.6    Gleeson, P.A.7
  • 7
    • 0037148787 scopus 로고    scopus 로고
    • Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains
    • Misra S., Puertollano R., Kato Y., Bonifacino J.S., Hurley J.H. Structural basis for acidic-cluster-dileucine sorting-signal recognition by VHS domains. Nature. 415:2002;933-937.
    • (2002) Nature , vol.415 , pp. 933-937
    • Misra, S.1    Puertollano, R.2    Kato, Y.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 8
    • 0037088675 scopus 로고    scopus 로고
    • Overexpression of an ARF-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced AP-1 coat dissociation and membrane tubulation
    • Shinotsuka C., Yoshida Y., Kawamoto K., Takatsu H., Nakayama K. Overexpression of an ARF-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced AP-1 coat dissociation and membrane tubulation. J Biol Chem. 277:2002;9468-9573.
    • (2002) J Biol Chem , vol.277 , pp. 9468-9573
    • Shinotsuka, C.1    Yoshida, Y.2    Kawamoto, K.3    Takatsu, H.4    Nakayama, K.5
  • 9
    • 0036151274 scopus 로고    scopus 로고
    • Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: Evidence for distinct functions in protein traffic
    • Zhao X., Lasell T.K., Melanon P. Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol Biol Cell. 13:2002;119-133.
    • (2002) Mol Biol Cell , vol.13 , pp. 119-133
    • Zhao, X.1    Lasell, T.K.2    Melanon, P.3
  • 10
    • 0035830496 scopus 로고    scopus 로고
    • Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network
    • Liljedahl M., Maeda Y., Colanzi A., Ayala I., Van Lint J., Malhotra V. Protein kinase D regulates the fission of cell surface destined transport carriers from the trans-Golgi network. Cell. 104:2001;409-420.
    • (2001) Cell , vol.104 , pp. 409-420
    • Liljedahl, M.1    Maeda, Y.2    Colanzi, A.3    Ayala, I.4    Van Lint, J.5    Malhotra, V.6
  • 12
    • 0035900480 scopus 로고    scopus 로고
    • Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles
    • Belden W.J., Barlowe C. Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles. Science. 294:2001;1528-1531.
    • (2001) Science , vol.294 , pp. 1528-1531
    • Belden, W.J.1    Barlowe, C.2
  • 13
    • 0034893765 scopus 로고    scopus 로고
    • Association of prohormone convertase 3 with membrane lipid rafts
    • Blazquez M., Docherty K., Shennan K.I. Association of prohormone convertase 3 with membrane lipid rafts. J Mol Endocrinol. 27:2001;107-116.
    • (2001) J Mol Endocrinol , vol.27 , pp. 107-116
    • Blazquez, M.1    Docherty, K.2    Shennan, K.I.3
  • 14
    • 0942295656 scopus 로고    scopus 로고
    • Involvement of the membrane lipid bilayer in sorting prohormone convertase 2 into the regulated secretory pathway
    • Blazquez M., Thiele C., Huttner W.B., Docherty K., Shennan K.I. Involvement of the membrane lipid bilayer in sorting prohormone convertase 2 into the regulated secretory pathway. Biochem J. 349:2000;843-852.
    • (2000) Biochem J , vol.349 , pp. 843-852
    • Blazquez, M.1    Thiele, C.2    Huttner, W.B.3    Docherty, K.4    Shennan, K.I.5
  • 15
    • 0034703034 scopus 로고    scopus 로고
    • Lipid raft association of carboxypeptidaseE is necessary for its function as a regulated secretory pathway sorting receptor
    • Dhanvantari S., Loh Y.P. Lipid raft association of carboxypeptidaseE is necessary for its function as a regulated secretory pathway sorting receptor. J Biol Chem. 275:2000;29887-29893. Until recently, it was considered that lumenal proteins lacking a glycosylphosphatidylinositol anchor would not have a sufficiently strong interaction with secretory pathway membranes to be recovered in a Triton X-100-insoluble lipid raft fraction. These authors were the first to demonstrate that a lumenal, membrane-associated secretory protein could indeed be recovered in the lipid raft fraction. It is important to note that because the starting material used for the analysis was purified secretory granule membranes, most of the lumenal carboxypeptidase E of the granule is likely to have already been removed during the preparation of the starting material. Thus, it remains unclear what fraction of total granule carboxypeptidase E is actually associated with lipid rafts. Nevertheless, of the subfraction purified with secretory granule membranes, a major portion appears to be associated with lipid rafts. These points are similarly applicable to Blazquez et al. [13,14] .
    • (2000) J Biol Chem , vol.275 , pp. 29887-29893
    • Dhanvantari, S.1    Loh, Y.P.2
  • 17
    • 0034731433 scopus 로고    scopus 로고
    • Thyroglobulin is selected as luminal protein cargo for apical transport via detergent-resistant membranes in epithelial cells
    • Martin-Belmonte F., Alonso M.A., Zhang X., Arvan P. Thyroglobulin is selected as luminal protein cargo for apical transport via detergent-resistant membranes in epithelial cells. J Biol Chem. 275:2000;41074-41081.
    • (2000) J Biol Chem , vol.275 , pp. 41074-41081
    • Martin-Belmonte, F.1    Alonso, M.A.2    Zhang, X.3    Arvan, P.4
  • 18
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz M., Nuoffer C., Hauri H.P., Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol. 148:2000;925-930.
    • (2000) J Cell Biol , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.P.3    Riezman, H.4
  • 19
    • 0035957985 scopus 로고    scopus 로고
    • Regulated apical secretion of zymogens in rat pancreas. Involvement of the glycosylphosphatidylinositol-anchored glycoprotein GP-2, the lectin ZG16p, and cholesterol-glycosphingolipid-enriched microdomains
    • Schmidt K., Schrader M., Kern H.F., Kleene R. Regulated apical secretion of zymogens in rat pancreas. Involvement of the glycosylphosphatidylinositol-anchored glycoprotein GP-2, the lectin ZG16p, and cholesterol-glycosphingolipid-enriched microdomains. J Biol Chem. 276:2001;14315-14323.
    • (2001) J Biol Chem , vol.276 , pp. 14315-14323
    • Schmidt, K.1    Schrader, M.2    Kern, H.F.3    Kleene, R.4
  • 21
    • 0035280141 scopus 로고    scopus 로고
    • Secretory granule biogenesis: Rafting to the SNARE
    • Tooze S.A., Martens G.J., Huttner W.B. Secretory granule biogenesis: rafting to the SNARE. Trends Cell Biol. 11:2001;116-122.
    • (2001) Trends Cell Biol , vol.11 , pp. 116-122
    • Tooze, S.A.1    Martens, G.J.2    Huttner, W.B.3
  • 22
    • 0034088234 scopus 로고    scopus 로고
    • Proinsulin endoproteolysis confers enhanced targeting of processed insulin to the regulated secretory pathway
    • Kuliawat R., Prabakaran D., Arvan P. Proinsulin endoproteolysis confers enhanced targeting of processed insulin to the regulated secretory pathway. Mol Biol Cell. 11:2000;1959-1972. Regulated secretory proteins exhibit conditionally dependent protein multimerization. In the case of proinsulin, endoproteolytic cleavage to insulin is required to make a protein species that efficiently polymerizes. This study shows a strong correlation between the conversion to insulin from proinsulin and the efficiency of its storage in the secretory granules of a heterologous cell line.
    • (2000) Mol Biol Cell , vol.11 , pp. 1959-1972
    • Kuliawat, R.1    Prabakaran, D.2    Arvan, P.3
  • 23
    • 0035808327 scopus 로고    scopus 로고
    • Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells
    • Lee M.S., Zhu Y.L., Chang J.E., Dannies P.S. Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells. J Biol Chem. 276:2001;715-721. Lubrol insolubility of intragranule prolactin-dense cores has been known for decades. However, in light of recent findings indicating that some regulated secretory proteins may also associate with the lumenal leaflet of the granule membrane (see Dhanvantari and Loh [2000] [15••] ), it remains open whether lubrol insolubility, as used in this study, reflects only protein-protein interactions involving proteins of the granule dense core. It may, in part, reflect protein interactions with granule membrane remnants after extraction with the non-ionic detergent.
    • (2001) J Biol Chem , vol.276 , pp. 715-721
    • Lee, M.S.1    Zhu, Y.L.2    Chang, J.E.3    Dannies, P.S.4
  • 24
    • 0035844876 scopus 로고    scopus 로고
    • Intracellular retention of newly-synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex
    • Zhang B.-Y., Chang A., Kjeldsen T.B., Arvan P. Intracellular retention of newly-synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex. J Cell Biol. 153:2001;1187-1197.
    • (2001) J Cell Biol , vol.153 , pp. 1187-1197
    • Zhang, B.-Y.1    Chang, A.2    Kjeldsen, T.B.3    Arvan, P.4
  • 25
    • 0034683662 scopus 로고    scopus 로고
    • Exclusion of Golgi residents from transport vesicles budding from Golgi cisternae in intact cells
    • Orci L., Amherdt M., Ravazzola M., Perrelet A., Rothman J.E. Exclusion of Golgi residents from transport vesicles budding from Golgi cisternae in intact cells. J Cell Biol. 150:2000;1263-1270.
    • (2000) J Cell Biol , vol.150 , pp. 1263-1270
    • Orci, L.1    Amherdt, M.2    Ravazzola, M.3    Perrelet, A.4    Rothman, J.E.5
  • 28
    • 0034604330 scopus 로고    scopus 로고
    • Megavesicles implicated in the rapid transport of intracisternal aggregates across the Golgi stack
    • Volchuk A., Amherdt M., Ravazzola M., Brugger B., Rivera V.M., Clackson T., Perrelet A., Sollner T.H., Rothman J.E., Orci L. Megavesicles implicated in the rapid transport of intracisternal aggregates across the Golgi stack. Cell. 102:2000;335-348. When conjoined to repeats of an oligomerization domain that allow for multimerization of a properly folded growth hormone fusion protein within the ER, the multimerized polypeptide hormone is unable to undergo anterograde transport unless the multimers are first dissociated in the presence of a small molecular weight, membrane-permeant ligand that binds specifically to the oligomerization domain (see Rivera et al. [2000] [32] ). A complicated combination of 15°C temperature block in conjunction with brief exposure to the membrane-permeant ligand (to accumulate some growth hormone fusion protein in the intermediate compartment) was carried out. This was followed by washout of the ligand to facilitate re-polymerization, and temperature-block reversal. As a result, some of the fusion protein advanced through the secretory pathway. An interesting electron microscopic analysis reportedly recovers 15-20% of protein aggregates, assessed by morphological criteria, in 'megavesicles'. However, the actual fraction of secretory protein that might be conveyed anterograde by megavesicles is difficult to say with precision from these studies. Additional co-localization of a range of Golgi-resident proteins with megavesicles might also shed further light on the origin and fate of these unusual compartments.
    • (2000) Cell , vol.102 , pp. 335-348
    • Volchuk, A.1    Amherdt, M.2    Ravazzola, M.3    Brugger, B.4    Rivera, V.M.5    Clackson, T.6    Perrelet, A.7    Sollner, T.H.8    Rothman, J.E.9    Orci, L.10
  • 29
    • 0035945347 scopus 로고    scopus 로고
    • Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: A role for ArfGAP1
    • Lanoix J., Ouwendijk J., Stark A., Szafer E., Cassel D., Dejgaard K., Weiss M., Nilsson T. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J Cell Biol. 155:2001;1199-1212.
    • (2001) J Cell Biol , vol.155 , pp. 1199-1212
    • Lanoix, J.1    Ouwendijk, J.2    Stark, A.3    Szafer, E.4    Cassel, D.5    Dejgaard, K.6    Weiss, M.7    Nilsson, T.8
  • 30
    • 0035945348 scopus 로고    scopus 로고
    • Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport
    • Martinez-Menárguez J.A., Prekeris R., Oorschot V.M.J., Scheller R., Slot J.W., Geuze H.J., Klumperman J. Peri-Golgi vesicles contain retrograde but not anterograde proteins consistent with the cisternal progression model of intra-Golgi transport. J Cell Biol. 155:2001;1213.
    • (2001) J Cell Biol , vol.155 , pp. 1213
    • Martinez-Menárguez, J.A.1    Prekeris, R.2    Oorschot, V.M.J.3    Scheller, R.4    Slot, J.W.5    Geuze, H.J.6    Klumperman, J.7
  • 31
    • 0035945357 scopus 로고    scopus 로고
    • Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae
    • Mironov A.A., Beznoussenko G.V., Nicoziani P., Martella O., Trucco A., Kweon H.-S., di Giandomenico D., Polishchuk R.S., Fusella A., Lupetti P., et al. Small cargo proteins and large aggregates can traverse the Golgi by a common mechanism without leaving the lumen of cisternae. J Cell Biol. 155:2001;1225-1238. This paper seemingly refutes the notion that megavesicles are required for rapid transit of unusually large lumenal cargo through the Golgi stack (see Volchuk et al. 2000 [28••] ). Given that some regulated secretory proteins begin to polymerize at sites before arrival in immature secretory granules (reviewed in Arvan and Castle 1998 [36] ), the finding that Golgi cistermae can readily accommodate large lumenal cargo speaks to a process of continuous maturation of the secretory containers throughout their advance from Golgi to secretory granule (see Clermont et al. [1992] [47] ).
    • (2001) J Cell Biol , vol.155 , pp. 1225-1238
    • Mironov, A.A.1    Beznoussenko, G.V.2    Nicoziani, P.3    Martella, O.4    Trucco, A.5    Kweon, H.-S.6    Di Giandomenico, D.7    Polishchuk, R.S.8    Fusella, A.9    Lupetti, P.10
  • 33
    • 0035900570 scopus 로고    scopus 로고
    • Immature granules are not major sites for segregation of constitutively secreted granule content proteins in NIT-1 insulinoma cells
    • Rindler M.J., Colomer V., Jin Y. Immature granules are not major sites for segregation of constitutively secreted granule content proteins in NIT-1 insulinoma cells. Biochem Biophys Res Commun. 288:2001;1071-1077.
    • (2001) Biochem Biophys Res Commun , vol.288 , pp. 1071-1077
    • Rindler, M.J.1    Colomer, V.2    Jin, Y.3
  • 34
    • 0034307475 scopus 로고    scopus 로고
    • Biogenesis of regulated exocytotic carriers in neuroendocrine cells
    • Eaton B.A., Haugwitz M., Lau D., Moore H.P. Biogenesis of regulated exocytotic carriers in neuroendocrine cells. J Neurosci. 20:2000;7334-7344.
    • (2000) J Neurosci , vol.20 , pp. 7334-7344
    • Eaton, B.A.1    Haugwitz, M.2    Lau, D.3    Moore, H.P.4
  • 35
    • 0034640306 scopus 로고    scopus 로고
    • Protein traffic from the secretory pathway to the endosomal system in pancreatic β-cells
    • Turner M., Arvan P. Protein traffic from the secretory pathway to the endosomal system in pancreatic β-cells. J Biol Chem. 275:2000;14025-14030. Several previous studies had suggested biosynthetic trafficking of membrane proteins to the cell surface only after initial delivery to endosomes, but this is the first report providing evidence to support an immature secretory granule-to-endosome-to-surface route for some lumenal proteins.
    • (2000) J Biol Chem , vol.275 , pp. 14025-14030
    • Turner, M.1    Arvan, P.2
  • 36
    • 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. 332:1998;593-610.
    • (1998) Biochem J , vol.332 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 37
    • 0032516858 scopus 로고    scopus 로고
    • Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells
    • Tooze S.A. Biogenesis of secretory granules in the trans-Golgi network of neuroendocrine and endocrine cells. Biochim Biophys Acta. 1404:1998;231-244.
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 231-244
    • Tooze, S.A.1
  • 38
    • 0032517767 scopus 로고    scopus 로고
    • Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells
    • Hirschberg K., Miller C.M., Ellenberg J., Presley J.F., Siggia E.D., Phair R.D., Lippincott-Schwartz J. Kinetic analysis of secretory protein traffic and characterization of Golgi to plasma membrane transport intermediates in living cells. J Cell Biol. 143:1998;1485-1503.
    • (1998) J Cell Biol , vol.143 , pp. 1485-1503
    • Hirschberg, K.1    Miller, C.M.2    Ellenberg, J.3    Presley, J.F.4    Siggia, E.D.5    Phair, R.D.6    Lippincott-Schwartz, J.7
  • 39
    • 0033594080 scopus 로고    scopus 로고
    • Golgi structure in three dimensions: Functional insights from the normal rat kidney cell
    • Ladinsky M.S., Mastronarde D.N., McIntosh J.R., Howell K.E., Staehelin L.A. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J Cell Biol. 144:1999;1135-1149.
    • (1999) J Cell Biol , vol.144 , pp. 1135-1149
    • Ladinsky, M.S.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4    Staehelin, L.A.5
  • 40
    • 0034627793 scopus 로고    scopus 로고
    • Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane
    • Polishchuk R.S., Polishchuk E.V., Marra P., Alberti S., Buccione R., Luini A., Mironov A.A. Correlative light-electron microscopy reveals the tubular-saccular ultrastructure of carriers operating between Golgi apparatus and plasma membrane. J Cell Biol. 148:2000;45-58.
    • (2000) J Cell Biol , vol.148 , pp. 45-58
    • Polishchuk, R.S.1    Polishchuk, E.V.2    Marra, P.3    Alberti, S.4    Buccione, R.5    Luini, A.6    Mironov, A.A.7
  • 41
    • 0024588990 scopus 로고
    • Formation of secretion granules in the Golgi apparatus of plasma cells in the rat
    • Rambourg A., Clermont Y., Hermo L., Chretien M. Formation of secretion granules in the Golgi apparatus of plasma cells in the rat. Am J Anat. 184:1989;52-61.
    • (1989) Am J Anat , vol.184 , pp. 52-61
    • Rambourg, A.1    Clermont, Y.2    Hermo, L.3    Chretien, M.4
  • 42
    • 0034599767 scopus 로고    scopus 로고
    • Imaging constitutive exocytosis with total internal reflection fluorescence microscopy
    • Schmoranzer J., Goulian M., Axelrod D., Simon S.M. Imaging constitutive exocytosis with total internal reflection fluorescence microscopy. J Cell Biol. 149:2000;23-32.
    • (2000) J Cell Biol , vol.149 , pp. 23-32
    • Schmoranzer, J.1    Goulian, M.2    Axelrod, D.3    Simon, S.M.4
  • 43
    • 0034599547 scopus 로고    scopus 로고
    • Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy
    • Toomre D., Steyer J.A., Keller P., Almers W., Simons K. Fusion of constitutive membrane traffic with the cell surface observed by evanescent wave microscopy. J Cell Biol. 149:2000;33-40.
    • (2000) J Cell Biol , vol.149 , pp. 33-40
    • Toomre, D.1    Steyer, J.A.2    Keller, P.3    Almers, W.4    Simons, K.5
  • 44
    • 0034930079 scopus 로고    scopus 로고
    • Three dimensional configuration of the secretory pathway and segregation of secretion granules in the yeast Saccharomyces cerevisiae
    • Rambourg A., Jackson C.L., Clermont Y. Three dimensional configuration of the secretory pathway and segregation of secretion granules in the yeast Saccharomyces cerevisiae. J Cell Sci. 114:2001;2231-2239.
    • (2001) J Cell Sci , vol.114 , pp. 2231-2239
    • Rambourg, A.1    Jackson, C.L.2    Clermont, Y.3
  • 45
    • 0034872373 scopus 로고    scopus 로고
    • Structural evidence for multiple transport mechanisms through the Golgi in the pancreatic beta-cell line, HIT-T15
    • Marsh B.J., Mastronarde D.N., McIntosh J.R., Howell K.E. Structural evidence for multiple transport mechanisms through the Golgi in the pancreatic beta-cell line, HIT-T15. Biochem Soc Trans. 29:2001;461-467. These elegant high-voltage electron microscopy studies provide independent support for several conclusions described earlier by Rambourg and colleagues in their morphological analyses of regulated secretory cells. Unfortunately, the HIT-T15 cell line does not produce large numbers of insulin secretory granules. High-voltage analyses of islet β cells are therefore still needed.
    • (2001) Biochem Soc Trans , vol.29 , pp. 461-467
    • Marsh, B.J.1    Mastronarde, D.N.2    McIntosh, J.R.3    Howell, K.E.4
  • 46
    • 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. Dynamics of immature secretory granules: role of cytoskeletal elements during transport, cortical restriction, and F-actin-dependent tethering. Mol Biol Cell. 12:2001;1353-1365. These authors find that fluorescent immature secretory granules (ISGs) newly formed in the Golgi region rapidly relocate along microtubule tracks to the subplasmalemmal cortex of PC12 cells (which normally have a very high fraction of granules pre-docked at the plasmalemma). Here, the ISGs mature, as measured by progressive loss of furin signal. It is important to note that other endocrine cells such as insulin-secreting pancreatic β cells tend to have a considerably smaller fraction of docked granules, and during ongoing secretory stimulation such cells continuously recruit granules from the cell interior to the surface for docking and exocytotic fusion.
    • (2001) Mol Biol Cell , vol.12 , pp. 1353-1365
    • Rudolf, R.1    Salm, T.2    Rustom, A.3    Gerdes, H.H.4
  • 47
    • 0026506801 scopus 로고
    • Segregation of secretory material in all elements of the Golgi apparatus in principal epithelial cells of the rat seminal vesicle
    • Clermont Y., Rambourg A., Hermo L. Segregation of secretory material in all elements of the Golgi apparatus in principal epithelial cells of the rat seminal vesicle. Anat Rec. 232:1992;349-358.
    • (1992) Anat Rec , vol.232 , pp. 349-358
    • Clermont, Y.1    Rambourg, A.2    Hermo, L.3
  • 48
    • 0017838948 scopus 로고
    • Intracellular transport and packaging of prolactin: A quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries
    • Farquhar M.G., Reid J.J., Daniell L.W. Intracellular transport and packaging of prolactin: a quantitative electron microscope autoradiographic study of mammotrophs dissociated from rat pituitaries. Endocrinology. 102:1978;296-311.
    • (1978) Endocrinology , vol.102 , pp. 296-311
    • Farquhar, M.G.1    Reid, J.J.2    Daniell, L.W.3
  • 49
    • 0026332190 scopus 로고
    • Characterization of the immature secretory granule, an intermediate in granule biogenesis
    • Tooze S.A., Flatmark T., Tooze J., Huttner W.B. Characterization of the immature secretory granule, an intermediate in granule biogenesis. J Cell Biol. 115:1991;1491-1504.
    • (1991) J Cell Biol , vol.115 , pp. 1491-1504
    • Tooze, S.A.1    Flatmark, T.2    Tooze, J.3    Huttner, W.B.4
  • 50
    • 0035158011 scopus 로고    scopus 로고
    • Homotypic fusion of immature secretory granules during maturation requires syntaxin 6
    • Wendler F., Page L., Urbe S., Tooze S.A. Homotypic fusion of immature secretory granules during maturation requires syntaxin 6. Mol Biol Cell. 12:2001;1699-1709.
    • (2001) Mol Biol Cell , vol.12 , pp. 1699-1709
    • Wendler, F.1    Page, L.2    Urbe, S.3    Tooze, S.A.4
  • 51
    • 0019201355 scopus 로고
    • Freeze-fracture and thin-section study of condensing vacuoles in rat pancreatic acinar cells
    • Sesso A., Assis J.E., Kuwajima V.Y., Kachar B. Freeze-fracture and thin-section study of condensing vacuoles in rat pancreatic acinar cells. Acta Anat. 108:1980;521-539.
    • (1980) Acta Anat , vol.108 , pp. 521-539
    • Sesso, A.1    Assis, J.E.2    Kuwajima, V.Y.3    Kachar, B.4
  • 52
    • 0017225843 scopus 로고
    • Studies on intracellular transport of secretory proteins in the rat exocrine pancreas. IV. Stimulation by in vivo infusion of caerulein
    • Bieger W., Martin-Achard A., Bassler M., Kern H.F. Studies on intracellular transport of secretory proteins in the rat exocrine pancreas. IV. Stimulation by in vivo infusion of caerulein. Cell Tissue Res. 165:1976;435-453.
    • (1976) Cell Tissue Res , vol.165 , pp. 435-453
    • Bieger, W.1    Martin-Achard, A.2    Bassler, M.3    Kern, H.F.4
  • 53
    • 0034766485 scopus 로고    scopus 로고
    • The ER to Golgi interface is the major concentration site of secretory proteins in the exocrine pancreatic cell
    • Oprins A., Rabouille C., Posthuma G., Klumperman J., Geuze H.J., Slot J.W. The ER to Golgi interface is the major concentration site of secretory proteins in the exocrine pancreatic cell. Traffic. 2:2001;831-838.
    • (2001) Traffic , vol.2 , pp. 831-838
    • Oprins, A.1    Rabouille, C.2    Posthuma, G.3    Klumperman, J.4    Geuze, H.J.5    Slot, J.W.6
  • 54
    • 0035105830 scopus 로고    scopus 로고
    • A signal sequence is sufficient for green fluorescent protein to be routed to regulated secretory granules
    • El Meskini R., Jin L., Marx R., Bruzzaniti A., Lee J., Emeson R., Mains R. A signal sequence is sufficient for green fluorescent protein to be routed to regulated secretory granules. Endocrinology. 142:2001;864-873. See annotation Molinete et al. (2000) [55•] .
    • (2001) Endocrinology , vol.142 , pp. 864-873
    • El Meskini, R.1    Jin, L.2    Marx, R.3    Bruzzaniti, A.4    Lee, J.5    Emeson, R.6    Mains, R.7
  • 55
    • 0033817564 scopus 로고    scopus 로고
    • Trafficking of non-regulated secretory proteins in insulin secreting (INS-1) cells
    • Molinete M., Lilla V., Jain R., Joyce P.B.M., Gorr S.-U., Ravazzola M., Halban P.A. Trafficking of non-regulated secretory proteins in insulin secreting (INS-1) cells. Diabetologia. 43:2000;1157-1164. Green fluorescent protein (GFP) and its variants are of great value as reporters for protein localization studies. In this paper, the authors find that one form of GFP not only enters insulin secretory granules, it also appears to be stored and secreted with efficiency that is comparable to that of authentic insulin. In conjunction with similar findings in other regulated secretory cells (see El Meskini et al. [2001] [54•] ), these data raise questions of whether GFP has cryptic sorting for entry signals, or whether there is simply no way to exclude GFP from entry into the lumen of forming granules. The authors observe a similar but less dramatic storage in insulin secretory granules of a glycosylphosphatidylinositol-deficient form of alkaline phosphatase called SEAP, in direct opposition to the results reported in Rindler et al. (2001) [33] . In any event, the findings in this paper raise a note of caution about using protein chimeras with GFP/variants for studies of sorting signals for lumenal protein entry into secretory granules, since such studies may obfuscate the requirement for demonstrating that such a signal is both necessary and sufficient.
    • (2000) Diabetologia , vol.43 , pp. 1157-1164
    • Molinete, M.1    Lilla, V.2    Jain, R.3    Joyce, P.B.M.4    Gorr, S.-U.5    Ravazzola, M.6    Halban, P.A.7
  • 58
    • 0034282635 scopus 로고    scopus 로고
    • Aggregation chaperones enhance aggregation and storage of secretory proteins in endocrine cells
    • Jain R.K., Joyce P.B., Gorr S.U. Aggregation chaperones enhance aggregation and storage of secretory proteins in endocrine cells. J Biol Chem. 275:2000;27032-27036.
    • (2000) J Biol Chem , vol.275 , pp. 27032-27036
    • Jain, R.K.1    Joyce, P.B.2    Gorr, S.U.3
  • 59
    • 0035943417 scopus 로고    scopus 로고
    • Chromogranin A, an 'on/off' switch controlling dense-core secretory granule biogenesis
    • Kim T., Tao-Cheng J.H., Eiden L.E., Loh Y.P. Chromogranin A, an 'on/off' switch controlling dense-core secretory granule biogenesis. Cell. 106:2001;499-509.
    • (2001) Cell , vol.106 , pp. 499-509
    • Kim, T.1    Tao-Cheng, J.H.2    Eiden, L.E.3    Loh, Y.P.4
  • 60
    • 0029981209 scopus 로고    scopus 로고
    • Chromogranin B (secretogranin I) promotes sorting to the regulated secretory pathway of processing intermediates derived from a peptide hormone precursor
    • Natori S., Huttner W.B. Chromogranin B (secretogranin I) promotes sorting to the regulated secretory pathway of processing intermediates derived from a peptide hormone precursor. Proc Natl Acad Sci USA. 93:1996;4431-4436.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4431-4436
    • Natori, S.1    Huttner, W.B.2
  • 61
    • 0034473542 scopus 로고    scopus 로고
    • Signal-mediated sorting of chromogranins to secretory granules
    • Gerdes H.H., Glombik M.M. Signal-mediated sorting of chromogranins to secretory granules. Adv Exp Med Biol. 482:2000;41-54.
    • (2000) Adv Exp Med Biol , vol.482 , pp. 41-54
    • Gerdes, H.H.1    Glombik, M.M.2
  • 62
    • 0036291394 scopus 로고    scopus 로고
    • Insertion of dibasic residues directs a constitutive protein to the regulated secretory pathway
    • Feliciangeli S., Kitabgi P. Insertion of dibasic residues directs a constitutive protein to the regulated secretory pathway. Biochem Biophys Res Commun. 290:2002;191-196. The opinion about the role of dibasic sequences in sorting of regulated secretory proteins presented in this paper provides one end of a spectrum: from the notion that such sequences serve as sorting-signal motifs independently of their recognition by dibasic cleavage enzymes; to the notion that cleavage of such sequences may change the biophysical properties (and consequently, sorting) of the cleavage products; to the notion that such sequences - with or without cleavage - are irrelevant for lumenal-protein targeting to secretory granules.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 191-196
    • Feliciangeli, S.1    Kitabgi, P.2
  • 63
    • 0030976604 scopus 로고    scopus 로고
    • Carboxypeptidase E is a regulated secretory pathway sorting receptor: Genetic obliteration leads to endocrine disorders in Cpefat mice
    • Cool D.R., Normant E., Shen F.S., Chen H.C., Pannel L., Zhang Y., Loh Y.P. Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpefat mice. Cell. 88:1997;73-83.
    • (1997) Cell , vol.88 , pp. 73-83
    • Cool, D.R.1    Normant, E.2    Shen, F.S.3    Chen, H.C.4    Pannel, L.5    Zhang, Y.6    Loh, Y.P.7
  • 64
    • 0035933823 scopus 로고    scopus 로고
    • Resting (basal) secretion of proteins is provided by the minor regulated and constitutive-like pathways and not granule exocytosis in parotid acinar cells
    • Huang A.Y., Castle A.M., Hinton B.T., Castle J.D. Resting (basal) secretion of proteins is provided by the minor regulated and constitutive-like pathways and not granule exocytosis in parotid acinar cells. J Biol Chem. 276:2001;22296-22306.
    • (2001) J Biol Chem , vol.276 , pp. 22296-22306
    • Huang, A.Y.1    Castle, A.M.2    Hinton, B.T.3    Castle, J.D.4
  • 65
    • 0037017395 scopus 로고    scopus 로고
    • Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells
    • Barbero P., Bittova L., Pfeffer S.R. Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells. J Cell Biol. 156:2002;511-518.
    • (2002) J Cell Biol , vol.156 , pp. 511-518
    • Barbero, P.1    Bittova, L.2    Pfeffer, S.R.3
  • 66
    • 0037148531 scopus 로고    scopus 로고
    • A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway
    • Harsay E., Schekman R. A subset of yeast vacuolar protein sorting mutants is blocked in one branch of the exocytic pathway. J Cell Biol. 156:2002;271-286.
    • (2002) J Cell Biol , vol.156 , pp. 271-286
    • Harsay, E.1    Schekman, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.