메뉴 건너뛰기




Volumn 289, Issue 21, 2014, Pages 14968-14980

Two dipolar α-helices within hormone-encoding regions of proglucagon are sorting signals to the regulated secretory pathway

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDES;

EID: 84901457013     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.563684     Document Type: Article
Times cited : (16)

References (64)
  • 2
    • 84870596168 scopus 로고    scopus 로고
    • Ghrelin, the proglucagon-derived peptides and peptide YY in nutrient homeostasis
    • Dong, C. X., and Brubaker, P. L. (2012) Ghrelin, the proglucagon-derived peptides and peptide YY in nutrient homeostasis. Nat. Rev. Gastroenterol. Hepatol. 9, 705-715 .
    • (2012) Nat. Rev. Gastroenterol. Hepatol. , vol.9 , pp. 705-715
    • Dong, C.X.1    Brubaker, P.L.2
  • 5
    • 12344302029 scopus 로고    scopus 로고
    • Significance of prohormone convertase 2, PC2, mediated initial cleavage at the proglucagon interdomain site, Lys70-Arg71, to generate glucagon
    • DOI 10.1210/en.2004-1118
    • Dey, A., Lipkind, G. M., Rouillé, Y., Norrbom, C., Stein, J., Zhang, C., Carroll, R., and Steiner, D. F. (2005) Significance of prohormone convertase 2, PC2, mediated initial cleavage at the proglucagon interdomain site, Lys70-Arg71, to generate glucagon. Endocrinology 146, 713-727 . (Pubitemid 40129827)
    • (2005) Endocrinology , vol.146 , Issue.2 , pp. 713-727
    • Dey, A.1    Lipkind, G.M.2    Rouille, Y.3    Norrbom, C.4    Stein, J.5    Zhang, C.6    Carroll, R.7    Steiner, D.F.8
  • 6
    • 0035920170 scopus 로고    scopus 로고
    • Severe defect in proglucagon processing in islet Acells of prohormone convertase 2 null mice
    • Furuta, M., Zhou, A., Webb, G., Carroll, R., Ravazzola, M., Orci, L., and Steiner, D. F. (2001) Severe defect in proglucagon processing in islet Acells of prohormone convertase 2 null mice. J. Biol. Chem. 276, 27197-27202 .
    • (2001) J. Biol. Chem. , vol.276 , pp. 27197-27202
    • Furuta, M.1    Zhou, A.2    Webb, G.3    Carroll, R.4    Ravazzola, M.5    Orci, L.6    Steiner, D.F.7
  • 7
    • 0033305618 scopus 로고    scopus 로고
    • Proglucagon processing profile in canine L cells expressing endogenous prohormone convertase 1/3 and prohormone convertase 2
    • Damholt, A. B., Buchan, A. M., Holst, J. J., and Kofod, H. (1999) Proglucagon processing profile in canine L cells expressing endogenous prohormone convertase 1/3 and prohormone convertase 2. Endocrinology 140, 4800-4808 . (Pubitemid 30666150)
    • (1999) Endocrinology , vol.140 , Issue.10 , pp. 4800-4808
    • Damholt, A.B.1    Buchan, A.M.J.2    Holst, J.J.3    Kofod, H.4
  • 8
    • 0031765121 scopus 로고    scopus 로고
    • Proglucagon processing in an islet cell line: Effects of PC1 overexpression and PC2 depletion
    • Dhanvantari, S., and Brubaker, P. L. (1998) Proglucagon processing in an islet cell line: effects of PC1 overexpression and PC2 depletion. Endocrinology 139, 1630-1637 . (Pubitemid 28513818)
    • (1998) Endocrinology , vol.139 , Issue.4 , pp. 1630-1637
    • Dhanvantari, S.1    Brubaker, P.L.2
  • 9
    • 0030012124 scopus 로고    scopus 로고
    • Role of prohormone convertases in the tissue-specific processing of proglucagon
    • DOI 10.1210/me.10.4.342
    • Dhanvantari, S., Seidah, N. G., and Brubaker, P. L. (1996) Role of prohormone convertases in the tissue-specific processing of proglucagon. Mol. Endocrinol. 10, 342-355. (Pubitemid 26112399)
    • (1996) Molecular Endocrinology , vol.10 , Issue.4 , pp. 342-355
    • Dhanvantari, S.1    Seidah, N.G.2    Brubaker, P.L.3
  • 10
    • 84901399050 scopus 로고    scopus 로고
    • Progressive change of intra-islet GLP-1 production during diabetes development
    • 10.1002/dmrr.2534
    • O'Malley, T. J., Fava, G. E., Zhang, Y., Fonseca, V. A., and Wu, H. (2014) Progressive change of intra-islet GLP-1 production during diabetes development. Diabetes. Metab. Res. Rev. 10.1002/dmrr.2534 .
    • (2014) Diabetes. Metab. Res. Rev.
    • O'malley, T.J.1    Fava, G.E.2    Zhang, Y.3    Fonseca, V.A.4    Wu, H.5
  • 11
    • 0021288365 scopus 로고
    • Immnocytochemical characterization of secretory granule maturation in pancreatic A-cells
    • Ravazzola, M., Perrelet, A., Unger, R. H., and Orci, L. (1984) Immunocytochemical characterization of secretory granule maturation in pancreatic A-cells. Endocrinology 114, 481-485 . (Pubitemid 14183248)
    • (1984) Endocrinology , vol.114 , Issue.2 , pp. 481-485
    • Ravazzola, M.1    Perrelet, A.2    Unger, R.H.3    Orci, L.4
  • 12
    • 0017621891 scopus 로고
    • Studies on proinsulin and proglucagon biosynthesis and conversion at the subcellular level. II. Distribution of radioactive peptide hormones and hormone precursors in subcellular fractions after pulse and pulse-chase incubation of islet tissue
    • DOI 10.1083/jcb.74.2.589
    • Noe, B. D., Baste, C. A., and Bauer, G. E. (1977) Studies on proinsulin and proglucagon biosynthesis and conversion at the subcellular level. II. Distribution of radioactive peptide hormones and hormone precursors in subcellular fractions after pulse and pulse-chase incubation of islet tissue. J. Cell Biol. 74, 589-604 . (Pubitemid 8153991)
    • (1977) Journal of Cell Biology , vol.74 , Issue.2 , pp. 589-604
    • Noe, B.D.1    Baste, C.A.2    Bauer, G.E.3
  • 13
    • 0029133141 scopus 로고
    • Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility
    • Huang, X. F., and Arvan, P. (1995) Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility. J. Biol. Chem. 270, 20417-20423 .
    • (1995) J. Biol. Chem. , vol.270 , pp. 20417-20423
    • Huang, X.F.1    Arvan, P.2
  • 14
    • 0042835761 scopus 로고    scopus 로고
    • Disruption of a receptor-mediated mechanism for intracellular sorting of proinsulin in familial hyperproinsulinemia
    • DOI 10.1210/me.2002-0380
    • Dhanvantari, S., Shen, F.-S., Adams, T., Snell, C. R., Zhang, C., Mackin, R. B., Morris, S. J., and Loh, Y. P. (2003) Disruption of a receptor-mediated mechanism for intracellular sorting of proinsulin in familial hyperproinsulinemia. Mol. Endocrinol. 17, 1856-1867 . (Pubitemid 37072300)
    • (2003) Molecular Endocrinology , vol.17 , Issue.9 , pp. 1856-1867
    • Dhanvantari, S.1    Shen, F.-S.2    Adams, T.3    Snell, C.R.4    Zhang, C.5    Mackin, R.B.6    Morris, S.J.7    Loh, Y.P.8
  • 15
    • 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, D. R., Normant, E., Shen, F., Chen, H. C., Pannell, L., Zhang, Y., and Loh, Y. P. (1997) Carboxypeptidase E is a regulated secretory pathway sorting receptor: genetic obliteration leads to endocrine disorders in Cpe-(fat) mice. Cell 88, 73-83 . (Pubitemid 27180332)
    • (1997) Cell , vol.88 , Issue.1 , pp. 73-83
    • Cool, D.R.1    Normant, E.2    Shen, F.-S.3    Chen, H.-C.4    Pannell, L.5    Zhang, Y.6    Loh, Y.P.7
  • 16
    • 0033330659 scopus 로고    scopus 로고
    • Identification of a novel prohormone sorting signal-binding site on carboxypeptidase E, a regulated secretory pathway-sorting receptor
    • Zhang, C. F., Snell, C. R., and Loh, Y. P. (1999) Identification of a novel prohormone sorting signal-binding site on carboxypeptidase E, a regulated secretory pathway-sorting receptor. Mol. Endocrinol. 13, 527-536 . (Pubitemid 30636420)
    • (1999) Molecular Endocrinology , vol.13 , Issue.4 , pp. 527-536
    • Zhang, C.-F.1    Snell, C.R.2    Loh, Y.P.3
  • 17
    • 0037024565 scopus 로고    scopus 로고
    • Mechanism of sorting proopiomelanocortin and proenkephalin to the regulated secretory pathway of neuroendocrine cells
    • Loh, Y. P., Maldonado, A., Zhang, C., Tam, W. H., and Cawley, N. (2002) Mechanism of sorting proopiomelanocortin and proenkephalin to the regulated secretory pathway of neuroendocrine cells. Ann. N.Y. Acad. Sci. 971, 416-425 . (Pubitemid 35305334)
    • (2002) Annals of the New York Academy of Sciences , vol.971 , pp. 416-425
    • Loh, Y.P.1    Maldonado, A.2    Zhang, C.3    Tam, W.H.4    Cawley, N.5
  • 18
    • 12344328770 scopus 로고    scopus 로고
    • Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase E
    • DOI 10.1016/j.neuron.2004.12.037, PII S0896627304008554
    • Lou, H., Kim, S.-K., Zaitsev, E., Snell, C. R., Lu, B., and Loh, Y. P. (2005) Sorting and activity-dependent secretion of BDNF require interaction of a specific motif with the sorting receptor carboxypeptidase e. Neuron 45, 245-255 . (Pubitemid 40128118)
    • (2005) Neuron , vol.45 , Issue.2 , pp. 245-255
    • Lou, H.1    Kim, S.-K.2    Zaitsev, E.3    Snell, C.R.4    Lu, B.5    Loh, Y.P.6
  • 19
    • 0036316744 scopus 로고    scopus 로고
    • Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro- and neuropeptide Y
    • DOI 10.1046/j.1471-4159.2002.00919.x
    • Brakch, N., Allemandou, F., Cavadas, C., Grouzmann, E., and Brunner, H. R. (2002) Dibasic cleavage site is required for sorting to the regulated secretory pathway for both pro-and neuropeptide Y. J. Neurochem. 81, 1166-1175 . (Pubitemid 34809251)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.6 , pp. 1166-1175
    • Brakch, N.1    Allemandou, F.2    Cavadas, C.3    Grouzmann, E.4    Brunner, H.R.5
  • 20
    • 0029787008 scopus 로고    scopus 로고
    • A protease processing site is essential for prorenin sorting to the regulated secretory pathway
    • DOI 10.1074/jbc.271.34.20636
    • Brechler, V., Chu, W. N., Baxter, J. D., Thibault, G., and Reudelhuber, T. L. (1996) A protease processing site is essential for prorenin sorting to the regulated secretory pathway. J. Biol. Chem. 271, 20636-20640 . (Pubitemid 26281843)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20636-20640
    • Brechler, V.1    Chu, W.N.2    Baxter, J.D.3    Thibault, G.4    Reudelhuber, T.L.5
  • 21
    • 1242272053 scopus 로고    scopus 로고
    • Progastrin Is Directed to the Regulated Secretory Pathway by Synergistically Acting Basic and Acidic Motifs
    • DOI 10.1074/jbc.M310547200
    • Bundgaard, J. R., Birkedal, H., and Rehfeld, J. F. (2004) Progastrin is directed to the regulated secretory pathway by synergistically acting basic and acidic motifs. J. Biol. Chem. 279, 5488-5493 . (Pubitemid 38220573)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.7 , pp. 5488-5493
    • Bundgaard, J.R.1    Birkedal, H.2    Rehfeld, J.F.3
  • 22
    • 0035794132 scopus 로고    scopus 로고
    • The role of dibasic residues in prohormone sorting to the regulated secretory pathway. A study with proneurotensin
    • Feliciangeli, S., Kitabgi, P., and Bidard, J. N. (2001) The role of dibasic residues in prohormone sorting to the regulated secretory pathway. A study with proneurotensin. J. Biol. Chem. 276, 6140-6150 .
    • (2001) J. Biol. Chem. , vol.276 , pp. 6140-6150
    • Feliciangeli, S.1    Kitabgi, P.2    Bidard, J.N.3
  • 23
    • 29244470261 scopus 로고    scopus 로고
    • A prohormone convertase cleavage site within a predicted α-helix mediates sorting of the neuronal and endocrine polypeptide VGF into the regulated secretory pathway
    • DOI 10.1074/jbc.M509122200
    • Garcia, A. L., Han, S.-K., Janssen, W. G., Khaing, Z. Z., Ito, T., Glucksman, M. J., Benson, D. L., and Salton, S. R. (2005) A prohormone convertase cleavage site within a predicted α -helix mediates sorting of the neuronal and endocrine polypeptide VGF into the regulated secretory pathway. J. Biol. Chem. 280, 41595-41608 . (Pubitemid 41832222)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.50 , pp. 41595-41608
    • Garcia, A.L.1    Han, S.-K.2    Janssen, W.G.3    Khaing, Z.Z.4    Ito, T.5    Glucksman, M.J.6    Benson, D.L.7    Salton, S.R.J.8
  • 24
    • 0035854755 scopus 로고    scopus 로고
    • A conserved α -helix at the amino terminus of prosomatostatin serves as a sorting signal for the regulated secretory pathway
    • Mouchantaf, R., Kumar, U., Sulea, T., and Patel, Y. C. (2001) A conserved α -helix at the amino terminus of prosomatostatin serves as a sorting signal for the regulated secretory pathway. J. Biol. Chem. 276, 26308-26316 .
    • (2001) J. Biol. Chem. , vol.276 , pp. 26308-26316
    • Mouchantaf, R.1    Kumar, U.2    Sulea, T.3    Patel, Y.C.4
  • 25
    • 84875115035 scopus 로고    scopus 로고
    • An amphipathic α -helix in the prodomain of cocaine and amphetamine regulated transcript peptide precursor serves as its sorting signal to the regulated secretory pathway
    • Blanco, E. H., Lagos, C. F., Andrés, M. E., and Gysling, K. (2013) An amphipathic α -helix in the prodomain of cocaine and amphetamine regulated transcript peptide precursor serves as its sorting signal to the regulated secretory pathway. PLoS One 8, e59695 .
    • (2013) PLoS One , vol.8
    • Blanco, E.H.1    Lagos, C.F.2    Andrés, M.E.3    Gysling, K.4
  • 26
    • 14244255720 scopus 로고    scopus 로고
    • Modulation of secretory granule-targeting efficiency by cis and trans compounding of sorting signals
    • DOI 10.1074/jbc.M408658200
    • Lacombe, M.-J., Mercure, C., Dikeakos, J. D., and Reudelhuber, T. L. (2005) Modulation of secretory granule-targeting efficiency by cis and trans compounding of sorting signals. J. Biol. Chem. 280, 4803-4807 . (Pubitemid 40288652)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.6 , pp. 4803-4807
    • Lacombe, M.-J.1    Mercure, C.2    Dikeakos, J.D.3    Reudelhuber, T.L.4
  • 27
    • 33847765866 scopus 로고    scopus 로고
    • A hydrophobic patch in a charged α-helix is sufficient to target proteins to dense core secretory granules
    • DOI 10.1074/jbc.M605718200
    • Dikeakos, J. D., Lacombe, M.-J., Mercure, C., Mireuta, M., and Reudelhuber, T. L. (2007) A hydrophobic patch in a charged α -helix is sufficient to target proteins to dense core secretory granules. J. Biol. Chem. 282, 1136-1143 . (Pubitemid 47076583)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2 , pp. 1136-1143
    • Dikeakos, J.D.1    Lacombe, M.-J.2    Mercure, C.3    Mireuta, M.4    Reudelhuber, T.L.5
  • 28
    • 0016709043 scopus 로고
    • X-ray analysis of glucagon and its relationship to receptor binding
    • Sasaki, K., Dockerill, S., Adamiak, D. A., Tickle, I. J., and Blundell, T. (1975) X-ray analysis of glucagon and its relationship to receptor binding. Nature 257, 751-757 .
    • (1975) Nature , vol.257 , pp. 751-757
    • Sasaki, K.1    Dockerill, S.2    Adamiak, D.A.3    Tickle, I.J.4    Blundell, T.5
  • 29
    • 73649107900 scopus 로고    scopus 로고
    • Crystal structure of glucagonlike peptide-1 in complex with the extracellular domain of the glucagonlike peptide-1 receptor
    • Underwood, C. R., Garibay, P., Knudsen, L. B., Hastrup, S., Peters, G. H., Rudolph, R., and Reedtz-Runge, S. (2010) Crystal structure of glucagonlike peptide-1 in complex with the extracellular domain of the glucagonlike peptide-1 receptor. J. Biol. Chem. 285, 723-730 .
    • (2010) J. Biol. Chem. , vol.285 , pp. 723-730
    • Underwood, C.R.1    Garibay, P.2    Knudsen, L.B.3    Hastrup, S.4    Peters, G.H.5    Rudolph, R.6    Reedtz-Runge, S.7
  • 30
    • 78651358892 scopus 로고    scopus 로고
    • Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain
    • Venneti, K. C., and Hewage, C. M. (2011) Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain. FEBS Lett. 585, 346-352 .
    • (2011) FEBS Lett. , vol.585 , pp. 346-352
    • Venneti, K.C.1    Hewage, C.M.2
  • 31
    • 84877886048 scopus 로고    scopus 로고
    • The α -helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum
    • Dirndorfer, D., Seidel, R. P., Nimrod, G., Miesbauer, M., Ben-Tal, N., Engelhard, M., Zimmermann, R., Winklhofer, K. F., and Tatzelt, J. (2013) The α -helical structure of prodomains promotes translocation of intrinsically disordered neuropeptide hormones into the endoplasmic reticulum. J. Biol. Chem. 288, 13961-13973 .
    • (2013) J. Biol. Chem. , vol.288 , pp. 13961-13973
    • Dirndorfer, D.1    Seidel, R.P.2    Nimrod, G.3    Miesbauer, M.4    Ben-Tal, N.5    Engelhard, M.6    Zimmermann, R.7    Winklhofer, K.F.8    Tatzelt, J.9
  • 32
    • 0035795227 scopus 로고    scopus 로고
    • Molecular evolution of proglucagon
    • DOI 10.1016/S0167-0115(00)00232-9, PII S0167011500002329
    • Irwin, D. M. (2001) Molecular evolution of proglucagon. Regul. Pept. 98, 1-12 . (Pubitemid 32155486)
    • (2001) Regulatory Peptides , vol.98 , Issue.1-2 , pp. 1-12
    • Irwin, D.M.1
  • 33
    • 84877344380 scopus 로고    scopus 로고
    • The sorting of proglucagon to secretory granules is mediated by carboxypeptidase e and intrinsic sorting signals
    • McGirr, R., Guizzetti, L., and Dhanvantari, S. (2013) The sorting of proglucagon to secretory granules is mediated by carboxypeptidase E and intrinsic sorting signals. J. Endocrinol. 217, 229-240 .
    • (2013) J. Endocrinol. , vol.217 , pp. 229-240
    • McGirr, R.1    Guizzetti, L.2    Dhanvantari, S.3
  • 34
    • 24944438228 scopus 로고    scopus 로고
    • Glucose dependence of the regulated secretory pathway in αTC1-6 cells
    • DOI 10.1210/en.2005-0402
    • McGirr, R., Ejbick, C. E., Carter, D. E., Andrews, J. D., Nie, Y., Friedman, T. C., and Dhanvantari, S. (2005) Glucose dependence of the regulated secretory pathway in αTC1-6 cells. Endocrinology 146, 4514-4523 . (Pubitemid 41324050)
    • (2005) Endocrinology , vol.146 , Issue.10 , pp. 4514-4523
    • McGirr, R.1    Ejbick, C.E.2    Carter, D.E.3    Andrews, J.D.4    Nie, Y.5    Friedman, T.C.6    Dhanvantari, S.7
  • 35
    • 41149129237 scopus 로고    scopus 로고
    • Analysis of regulated secretion using PC12 cells
    • Chapter 15, Unit 15.12
    • Taupenot, L. (2007) Analysis of regulated secretion using PC12 cells. Curr. Protoc. Cell Biol. Chapter 15, Unit 15.12 .
    • (2007) Curr. Protoc. Cell Biol.
    • Taupenot, L.1
  • 37
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server. Bioinformatics 16, 404-405 . (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 39
    • 0021691817 scopus 로고
    • Analysis of membrane and surface protein sequences with the hydrophobic moment plot
    • DOI 10.1016/0022-2836(84)90309-7
    • Eisenberg, D., Schwarz, E., Komaromy, M., and Wall, R. (1984) Analysis of membrane and surface protein sequences with the hydrophobic moment plot. J. Mol. Biol. 179, 125-142 . (Pubitemid 16223392)
    • (1984) Journal of Molecular Biology , vol.179 , Issue.1 , pp. 125-142
    • Eisenberg, D.1    Schwarz, E.2    Komaromy, M.3    Wall, R.4
  • 40
    • 0023657949 scopus 로고
    • Hydrophobic cluster analysis: An efficient new way to compare and analyse amino acid sequences
    • Gaboriaud, C., Bissery, V., Benchetrit, T., and Mornon, J. P. (1987) Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 224, 149-155 .
    • (1987) FEBS Lett. , vol.224 , pp. 149-155
    • Gaboriaud, C.1    Bissery, V.2    Benchetrit, T.3    Mornon, J.P.4
  • 41
    • 0031764282 scopus 로고    scopus 로고
    • Depletion of carboxypeptidase E, a regulated secretory pathway sorting receptor, causes misrouting and constitutive secretion of proinsulin and proenkephalin, but not chromogranin A
    • Normant, E., and Loh, Y. P. (1998) Depletion of carboxypeptidase E, a regulated secretory pathway sorting receptor, causes misrouting and constitutive secretion of proinsulin and proenkephalin, but not chromogranin A. Endocrinology 139, 2137-2145 . (Pubitemid 28513878)
    • (1998) Endocrinology , vol.139 , Issue.4 , pp. 2137-2145
    • Normant, E.1    Loh, Y.P.2
  • 42
    • 2642683228 scopus 로고    scopus 로고
    • Subcellular localization of epitope-tagged neurotrophins in neuroendocrine cells
    • DOI 10.1002/(SICI)1097-4547(19980215)51:4<463::AID-JNR6>3.0.CO;2-A
    • Möller, J. C., Krüttgen, A., Heymach, J. V., Jr., Ghori, N., and Shooter, E. M. (1998) Subcellular localization of epitope-tagged neurotrophins in neuroendocrine cells. J. Neurosci. Res. 51, 463-472 . (Pubitemid 28106707)
    • (1998) Journal of Neuroscience Research , vol.51 , Issue.4 , pp. 463-472
    • Moller, J.C.1    Kruttgen, A.2    Heymach Jr., J.V.3    Ghori, N.4    Shooter, E.M.5
  • 43
    • 0036291394 scopus 로고    scopus 로고
    • Insertion of dibasic residues directs a constitutive protein to the regulated secretory pathway
    • DOI 10.1006/bbrc.2001.6137
    • Féliciangéli, S., and Kitabgi, P. (2002) Insertion of dibasic residues directs a constitutive protein to the regulated secretory pathway. Biochem. Biophys. Res. Commun. 290, 191-196 . (Pubitemid 34694482)
    • (2002) Biochemical and Biophysical Research Communications , vol.290 , Issue.1 , pp. 191-196
    • Feliciangeli, S.1    Kitabgi, P.2
  • 44
    • 0025303611 scopus 로고
    • Renin is sorted to the regulated secretory pathway in transfected PC12 cells by a mechanism which does not require expression of the pro-peptide
    • DOI 10.1111/j.1432-1033.1990.tb15556.x
    • Chidgey, M. A., and Harrison, T. M. (1990) Renin is sorted to the regulated secretory pathway in transfected PC12 cells by a mechanism which does not require expression of the pro-peptide. Eur. J. Biochem. 190, 139-144 . (Pubitemid 20183975)
    • (1990) European Journal of Biochemistry , vol.190 , Issue.1 , pp. 139-144
    • Chidgey, M.A.J.1    Harrison, T.M.2
  • 45
    • 40149096514 scopus 로고    scopus 로고
    • Immunohistochemical staining of human islet cells with region-specific antibodies against secretogranins II and III
    • DOI 10.1111/j.1469-7580.2008.00857.x
    • Stridsberg, M., Grimelius, L., and Portela-Gomes, G. M. (2008) Immunohistochemical staining of human islet cells with region-specific antibodies against secretogranins II and III. J. Anat. 212, 229-234 . (Pubitemid 351325479)
    • (2008) Journal of Anatomy , vol.212 , Issue.3 , pp. 229-234
    • Stridsberg, M.1    Grimelius, L.2    Portela-Gomes, G.M.3
  • 46
    • 77953646073 scopus 로고    scopus 로고
    • Secretogranin III: A bridge between core hormone aggregates and the secretory granule membrane
    • Hosaka, M., and Watanabe, T. (2010) Secretogranin III: a bridge between core hormone aggregates and the secretory granule membrane. Endocr. J. 57, 275-286 .
    • (2010) Endocr. J. , vol.57 , pp. 275-286
    • Hosaka, M.1    Watanabe, T.2
  • 48
    • 84866444859 scopus 로고    scopus 로고
    • All three components of the neuronal SNARE complex contribute to secretory vesicle docking
    • Wu, Y., Gu, Y., Morphew, M. K., Yao, J., Yeh, F. L., Dong, M., and Chapman, E. R. (2012) All three components of the neuronal SNARE complex contribute to secretory vesicle docking. J. Cell Biol. 198, 323-330 .
    • (2012) J. Cell Biol. , vol.198 , pp. 323-330
    • Wu, Y.1    Gu, Y.2    Morphew, M.K.3    Yao, J.4    Yeh, F.L.5    Dong, M.6    Chapman, E.R.7
  • 49
    • 34249778678 scopus 로고    scopus 로고
    • 2+ channels and soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins to cholesterol-rich lipid rafts in pancreatic α-cells: Effects on glucagon stimulus-secretion coupling
    • DOI 10.1210/en.2006-1296
    • 2+ channels and soluble N-ethylmaleimide-sensitive factor attachment protein receptor proteins to cholesterol-rich lipid rafts in pancreatic alpha-cells: effects on glucagon stimulus-secretion coupling. Endocrinology 148, 2157-2167 . (Pubitemid 46997050)
    • (2007) Endocrinology , vol.148 , Issue.5 , pp. 2157-2167
    • Xia, F.1    Leung, Y.M.2    Gaisano, G.3    Gao, X.4    Chen, Y.5    Fox, J.E.M.6    Bhattacharjee, A.7    Wheeler, M.B.8    Gaisano, H.Y.9    Tsushima, R.G.10
  • 51
    • 84884686335 scopus 로고    scopus 로고
    • Widespread dysregulation of peptide hormone release in mice lacking adaptor protein AP-3
    • Sirkis, D. W., Edwards, R. H., and Asensio, C. S. (2013) Widespread dysregulation of peptide hormone release in mice lacking adaptor protein AP-3. PLoS Genet. 9, e1003812 .
    • (2013) PLoS Genet. , vol.9
    • Sirkis, D.W.1    Edwards, R.H.2    Asensio, C.S.3
  • 52
    • 84896094444 scopus 로고    scopus 로고
    • Role of vesicleassociated membrane protein 2 in exocytosis of glucagon-like peptide-1 from the murine intestinal L cell
    • Li, S. K., Zhu, D., Gaisano, H. Y., and Brubaker, P. L. (2014) Role of vesicleassociated membrane protein 2 in exocytosis of glucagon-like peptide-1 from the murine intestinal L cell. Diabetologia 54, 809-818 .
    • (2014) Diabetologia , vol.54 , pp. 809-818
    • Li, S.K.1    Zhu, D.2    Gaisano, H.Y.3    Brubaker, P.L.4
  • 53
    • 0034704108 scopus 로고    scopus 로고
    • A predicted α-helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway
    • DOI 10.1074/jbc.M004757200
    • Jutras, I., Seidah, N. G., and Reudelhuber, T. L. (2000) A predicted α -helix mediates targeting of the proprotein convertase PC1 to the regulated secretory pathway. J. Biol. Chem. 275, 40337-40343 . (Pubitemid 32064667)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 40337-40343
    • Jutras, I.1    Seidah, N.G.2    Reudelhuber, T.L.3
  • 54
    • 0022512255 scopus 로고
    • Mutations in the guinea pig preproglucagon gene are restricted to a specific portion of the prohormone sequence
    • DOI 10.1016/0014-5793(86)81429-6
    • Seino, S., Welsh, M., Bell, G. I., Chan, S. J., and Steiner, D. F. (1986) Mutations in the guinea pig preproglucagon gene are restricted to a specific portion of the prohormone sequence. FEBS Lett. 203, 25-30 . (Pubitemid 16043485)
    • (1986) FEBS Letters , vol.203 , Issue.1 , pp. 25-30
    • Seino, S.1    Welsh, M.2    Bell, G.I.3
  • 56
    • 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
    • DOI 10.1021/bi036331g
    • Assadi, M., Sharpe, J. C., Snell, C., and Loh, Y. P. (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 . (Pubitemid 38787687)
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7798-7807
    • Assadi, M.1    Sharpe, J.C.2    Snell, C.3    Loh, Y.P.4
  • 57
    • 0037039349 scopus 로고    scopus 로고
    • Carboxypeptidase E, a prohormone sorting receptor, is anchored to secretory granules via a C-terminal transmembrane insertion
    • DOI 10.1021/bi015698n
    • Dhanvantari, S., Arnaoutova, I., Snell, C. R., Steinbach, P. J., Hammond, K., Caputo, G. A., London, E., and Loh, Y. P. (2002) Carboxypeptidase E, a prohormone sorting receptor, is anchored to secretory granules via a Cterminal transmembrane insertion. Biochemistry 41, 52-60 . (Pubitemid 34049380)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 52-60
    • Dhanvantari, S.1    Arnaoutova, I.2    Snell, C.R.3    Steinbach, P.J.4    Hammond, K.5    Caputo, G.A.6    London, E.7    Loh, Y.P.8
  • 58
    • 0029070171 scopus 로고
    • Omega loops: Nonregular secondary structures significant in protein function and stability
    • Fetrow, J. S. (1995) Omega loops: nonregular secondary structures significant in protein function and stability. FASEB J. 9, 708-717 .
    • (1995) FASEB J. , vol.9 , pp. 708-717
    • Fetrow, J.S.1
  • 59
    • 33846100727 scopus 로고    scopus 로고
    • Self-masking in an Intact ERM-merlin Protein: An Active Role for the Central α-Helical Domain
    • DOI 10.1016/j.jmb.2006.10.075, PII S0022283606014550
    • Li, Q., Nance, M. R., Kulikauskas, R., Nyberg, K., Fehon, R., Karplus, P. A., Bretscher, A., and Tesmer, J. J. (2007) Self-masking in an intact ERMmerlin protein: an active role for the central α -helical domain. J. Mol. Biol. 365, 1446-1459 . (Pubitemid 46055267)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.5 , pp. 1446-1459
    • Li, Q.1    Nance, M.R.2    Kulikauskas, R.3    Nyberg, K.4    Fehon, R.5    Karplus, P.A.6    Bretscher, A.7    Tesmer, J.J.G.8
  • 60
    • 56149106018 scopus 로고    scopus 로고
    • Short elements with charged amino acids form clusters to sort protachykinin into large dense-core vesicles
    • Ma, G.-Q., Wang, B., Wang, H.-B., Wang, Q., and Bao, L. (2008) Short elements with charged amino acids form clusters to sort protachykinin into large dense-core vesicles. Traffic 9, 2165-2179 .
    • (2008) Traffic , vol.9 , pp. 2165-2179
    • Ma, G.-Q.1    Wang, B.2    Wang, H.-B.3    Wang, Q.4    Bao, L.5
  • 61
    • 28844478947 scopus 로고    scopus 로고
    • Prohormone-convertase 1 processing enhances post-golgi sorting of prothyrotropin-releasing hormone-derived peptides
    • DOI 10.1074/jbc.M507193200
    • Mulcahy, L. R., Vaslet, C. A., and Nillni, E. A. (2005) Prohormone-convertase 1 processing enhances post-Golgi sorting of prothyrotropin-releasing hormone-derived peptides. J. Biol. Chem. 280, 39818-39826 . (Pubitemid 41779115)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39818-39826
    • Mulcahy, L.R.1    Vaslet, C.A.2    Nillni, E.A.3
  • 62
    • 50649106484 scopus 로고    scopus 로고
    • Prothyrotropin-releasing hormone targets its processing products to different vesicles of the secretory pathway
    • Perello, M., Stuart, R., and Nillni, E. A. (2008) Prothyrotropin- releasing hormone targets its processing products to different vesicles of the secretory pathway. J. Biol. Chem. 283, 19936-19947 .
    • (2008) J. Biol. Chem. , vol.283 , pp. 19936-19947
    • Perello, M.1    Stuart, R.2    Nillni, E.A.3
  • 63
    • 34247543907 scopus 로고    scopus 로고
    • Sending proteins to dense core secretory granules: Still a lot to sort out
    • DOI 10.1083/jcb.200701024
    • Dikeakos, J. D., and Reudelhuber, T. L. (2007) Sending proteins to dense core secretory granules: still a lot to sort out. J. Cell Biol. 177, 191-196 . (Pubitemid 46658630)
    • (2007) Journal of Cell Biology , vol.177 , Issue.2 , pp. 191-196
    • Dikeakos, J.D.1    Reudelhuber, T.L.2
  • 64
    • 84872021191 scopus 로고    scopus 로고
    • Multiple sorting systems for secretory granules ensure the regulated secretion of peptide hormones
    • Sun, M., Watanabe, T., Bochimoto, H., Sakai, Y., Torii, S., Takeuchi, T., and Hosaka, M. (2013) Multiple sorting systems for secretory granules ensure the regulated secretion of peptide hormones. Traffic 14, 205-218 .
    • (2013) Traffic , vol.14 , pp. 205-218
    • Sun, M.1    Watanabe, T.2    Bochimoto, H.3    Sakai, Y.4    Torii, S.5    Takeuchi, T.6    Hosaka, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.