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Volumn 23, Issue 4, 2012, Pages 756-768

The BAR Domain Protein Arfaptin-1 Controls Secretory Granule Biogenesis at the trans-Golgi Network

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR; ARFAPTIN 1; CELL PROTEIN; GLUCOSE; PROTEIN KINASE D; SERINE; SERINE 132; UNCLASSIFIED DRUG;

EID: 84867698481     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2012.07.019     Document Type: Article
Times cited : (77)

References (48)
  • 1
    • 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 2002, 295:325-328.
    • (2002) Science , vol.295 , pp. 325-328
    • Baron, C.L.1    Malhotra, V.2
  • 4
    • 64149121216 scopus 로고    scopus 로고
    • ARF6 regulates the synthesis of fusogenic lipids for calcium-regulated exocytosis in neuroendocrine cells
    • Béglé A., Tryoen-Tóth P., de Barry J., Bader M.F., Vitale N. ARF6 regulates the synthesis of fusogenic lipids for calcium-regulated exocytosis in neuroendocrine cells. J. Biol. Chem. 2009, 284:4836-4845.
    • (2009) J. Biol. Chem. , vol.284 , pp. 4836-4845
    • Béglé, A.1    Tryoen-Tóth, P.2    de Barry, J.3    Bader, M.F.4    Vitale, N.5
  • 5
    • 29144454715 scopus 로고    scopus 로고
    • Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission
    • Bielli A., Haney C.J., Gabreski G., Watkins S.C., Bannykh S.I., Aridor M. Regulation of Sar1 NH2 terminus by GTP binding and hydrolysis promotes membrane deformation to control COPII vesicle fission. J. Cell Biol. 2005, 171:919-924.
    • (2005) J. Cell Biol. , vol.171 , pp. 919-924
    • Bielli, A.1    Haney, C.J.2    Gabreski, G.3    Watkins, S.C.4    Bannykh, S.I.5    Aridor, M.6
  • 6
    • 84859175662 scopus 로고    scopus 로고
    • Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains
    • Boucrot E., Pick A., çamdere G., Liska N., Evergren E., McMahon H.T., Kozlov M.M. Membrane fission is promoted by insertion of amphipathic helices and is restricted by crescent BAR domains. Cell 2012, 149:124-136.
    • (2012) Cell , vol.149 , pp. 124-136
    • Boucrot, E.1    Pick, A.2    çamdere, G.3    Liska, N.4    Evergren, E.5    McMahon, H.T.6    Kozlov, M.M.7
  • 7
    • 84859392762 scopus 로고    scopus 로고
    • The small G protein Arl1 directs the trans-Golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2
    • Christis C., Munro S. The small G protein Arl1 directs the trans-Golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2. J. Cell Biol. 2012, 196:327-335.
    • (2012) J. Cell Biol. , vol.196 , pp. 327-335
    • Christis, C.1    Munro, S.2
  • 8
    • 0036314216 scopus 로고    scopus 로고
    • Phasic insulin release and metabolic regulation in type 2 diabetes
    • Del Prato S., Marchetti P., Bonadonna R.C. Phasic insulin release and metabolic regulation in type 2 diabetes. Diabetes 2002, 51(Suppl 1):S109-S116.
    • (2002) Diabetes , vol.51 , Issue.SUPPL. 1
    • Del Prato, S.1    Marchetti, P.2    Bonadonna, R.C.3
  • 9
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators: roles in membrane transport, development and disease
    • Donaldson J.G., Jackson C.L. ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nature Rev. 2011, 12:362-375.
    • (2011) Nature Rev. , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 11
    • 79961026124 scopus 로고    scopus 로고
    • Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology
    • Fu Y., Rubin C.S. Protein kinase D: coupling extracellular stimuli to the regulation of cell physiology. EMBO Rep. 2011, 12:785-796.
    • (2011) EMBO Rep. , vol.12 , pp. 785-796
    • Fu, Y.1    Rubin, C.S.2
  • 12
    • 34347379940 scopus 로고    scopus 로고
    • Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein
    • Fugmann T., Hausser A., Schöffler P., Schmid S., Pfizenmaier K., Olayioye M.A. Regulation of secretory transport by protein kinase D-mediated phosphorylation of the ceramide transfer protein. J. Cell Biol. 2007, 178:15-22.
    • (2007) J. Cell Biol. , vol.178 , pp. 15-22
    • Fugmann, T.1    Hausser, A.2    Schöffler, P.3    Schmid, S.4    Pfizenmaier, K.5    Olayioye, M.A.6
  • 13
    • 40449128054 scopus 로고    scopus 로고
    • Identification of a guanine nucleotide exchange factor for Arf3, the yeast orthologue of mammalian Arf6
    • Gillingham A.K., Munro S. Identification of a guanine nucleotide exchange factor for Arf3, the yeast orthologue of mammalian Arf6. PLoS ONE 2007, 2:e842.
    • (2007) PLoS ONE , vol.2
    • Gillingham, A.K.1    Munro, S.2
  • 14
    • 3543025954 scopus 로고    scopus 로고
    • The BAR-domain family of proteins: a case of bending and binding?
    • Habermann B. The BAR-domain family of proteins: a case of bending and binding?. EMBO Rep. 2004, 5:250-255.
    • (2004) EMBO Rep. , vol.5 , pp. 250-255
    • Habermann, B.1
  • 15
    • 26944446652 scopus 로고    scopus 로고
    • Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex
    • Hausser A., Storz P., Märtens S., Link G., Toker A., Pfizenmaier K. Protein kinase D regulates vesicular transport by phosphorylating and activating phosphatidylinositol-4 kinase IIIbeta at the Golgi complex. Nat. Cell Biol. 2005, 7:880-886.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 880-886
    • Hausser, A.1    Storz, P.2    Märtens, S.3    Link, G.4    Toker, A.5    Pfizenmaier, K.6
  • 16
    • 0142149014 scopus 로고    scopus 로고
    • A novel interaction between protein kinase D and TNF receptor-associated factor molecules regulates B cell receptor-CD40 synergy
    • Haxhinasto S.A., Bishop G.A. A novel interaction between protein kinase D and TNF receptor-associated factor molecules regulates B cell receptor-CD40 synergy. J. Immunol. 2003, 171:4655-4662.
    • (2003) J. Immunol. , vol.171 , pp. 4655-4662
    • Haxhinasto, S.A.1    Bishop, G.A.2
  • 18
    • 0031041589 scopus 로고    scopus 로고
    • Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes
    • Kanoh H., Williger B.T., Exton J.H. Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. J. Biol. Chem. 1997, 272:5421-5429.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5421-5429
    • Kanoh, H.1    Williger, B.T.2    Exton, J.H.3
  • 19
    • 0034572830 scopus 로고    scopus 로고
    • Three ways to make a vesicle
    • Kirchhausen T. Three ways to make a vesicle. Nature Rev. 2000, 1:187-198.
    • (2000) Nature Rev. , vol.1 , pp. 187-198
    • Kirchhausen, T.1
  • 21
    • 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 2001, 104:409-420.
    • (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
  • 22
    • 84863865272 scopus 로고    scopus 로고
    • PKD regulates membrane fission to generate TGN to cell surface transport carriers
    • Malhotra V., Campelo F. PKD regulates membrane fission to generate TGN to cell surface transport carriers. Cold Spring Harb. Perspect. Biol. 2011, 3:3.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 3
    • Malhotra, V.1    Campelo, F.2
  • 23
    • 79953172625 scopus 로고    scopus 로고
    • Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs
    • Man Z., Kondo Y., Koga H., Umino H., Nakayama K., Shin H.W. Arfaptins are localized to the trans-Golgi by interaction with Arl1, but not Arfs. J. Biol. Chem. 2011, 286:11569-11578.
    • (2011) J. Biol. Chem. , vol.286 , pp. 11569-11578
    • Man, Z.1    Kondo, Y.2    Koga, H.3    Umino, H.4    Nakayama, K.5    Shin, H.W.6
  • 24
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 2005, 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 26
    • 39749147110 scopus 로고    scopus 로고
    • Mechanisms of disease: molecular and metabolic mechanisms of insulin resistance and beta-cell failure in type 2 diabetes
    • Muoio D.M., Newgard C.B. Mechanisms of disease: molecular and metabolic mechanisms of insulin resistance and beta-cell failure in type 2 diabetes. Nature Rev. 2008, 9:193-205.
    • (2008) Nature Rev. , vol.9 , pp. 193-205
    • Muoio, D.M.1    Newgard, C.B.2
  • 27
    • 84864083155 scopus 로고    scopus 로고
    • Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase
    • Nakamura K., Man Z., Xie Y., Hanai A., Makyio H., Kawasaki M., Kato R., Shin H.W., Nakayama K., Wakatsuki S. Structural basis for membrane binding specificity of the Bin/Amphiphysin/Rvs (BAR) domain of Arfaptin-2 determined by Arl1 GTPase. J. Biol. Chem. 2012, 287:25478-25489.
    • (2012) J. Biol. Chem. , vol.287 , pp. 25478-25489
    • Nakamura, K.1    Man, Z.2    Xie, Y.3    Hanai, A.4    Makyio, H.5    Kawasaki, M.6    Kato, R.7    Shin, H.W.8    Nakayama, K.9    Wakatsuki, S.10
  • 28
    • 65249161758 scopus 로고    scopus 로고
    • Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function
    • Ngo M., Ridgway N.D. Oxysterol binding protein-related Protein 9 (ORP9) is a cholesterol transfer protein that regulates Golgi structure and function. Mol. Biol. Cell 2009, 20:1388-1399.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1388-1399
    • Ngo, M.1    Ridgway, N.D.2
  • 31
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions of membrane active GTPases in coated vesicle formation
    • Pucadyil T.J., Schmid S.L. Conserved functions of membrane active GTPases in coated vesicle formation. Science 2009, 325:1217-1220.
    • (2009) Science , vol.325 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 32
    • 77949477235 scopus 로고    scopus 로고
    • Role of the second cysteine-rich domain and Pro275 in protein kinase D2 interaction with ADP-ribosylation factor 1, trans-Golgi network recruitment, and protein transport
    • Pusapati G.V., Krndija D., Armacki M., von Wichert G., von Blume J., Malhotra V., Adler G., Seufferlein T. Role of the second cysteine-rich domain and Pro275 in protein kinase D2 interaction with ADP-ribosylation factor 1, trans-Golgi network recruitment, and protein transport. Mol. Biol. Cell 2010, 21:1011-1022.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1011-1022
    • Pusapati, G.V.1    Krndija, D.2    Armacki, M.3    von Wichert, G.4    von Blume, J.5    Malhotra, V.6    Adler, G.7    Seufferlein, T.8
  • 36
    • 78649681291 scopus 로고    scopus 로고
    • Interaction of calcium-dependent activator protein for secretion 1 (CAPS1) with the class II ADP-ribosylation factor small GTPases is required for dense-core vesicle trafficking in the trans-Golgi network
    • Sadakata T., Shinoda Y., Sekine Y., Saruta C., Itakura M., Takahashi M., Furuichi T. Interaction of calcium-dependent activator protein for secretion 1 (CAPS1) with the class II ADP-ribosylation factor small GTPases is required for dense-core vesicle trafficking in the trans-Golgi network. J. Biol. Chem. 2010, 285:38710-38719.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38710-38719
    • Sadakata, T.1    Shinoda, Y.2    Sekine, Y.3    Saruta, C.4    Itakura, M.5    Takahashi, M.6    Furuichi, T.7
  • 39
    • 0034812543 scopus 로고    scopus 로고
    • Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1
    • Shin O.H., Exton J.H. Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1. Biochem. Biophys. Res. Commun. 2001, 285:1267-1273.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 1267-1273
    • Shin, O.H.1    Exton, J.H.2
  • 40
    • 52549092941 scopus 로고    scopus 로고
    • The life cycle of a transport vesicle
    • Spang A. The life cycle of a transport vesicle. Cell. Mol. Life Sci. 2008, 65:2781-2789.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2781-2789
    • Spang, A.1
  • 41
    • 80053183724 scopus 로고    scopus 로고
    • Sphingomyelin synthases regulate protein trafficking and secretion
    • Subathra M., Qureshi A., Luberto C. Sphingomyelin synthases regulate protein trafficking and secretion. PLoS ONE 2011, 6:e23644.
    • (2011) PLoS ONE , vol.6
    • Subathra, M.1    Qureshi, A.2    Luberto, C.3
  • 43
    • 0035997044 scopus 로고    scopus 로고
    • The effects of acyl chain length and saturation of diacylglycerols and phosphatidylcholines on membrane monolayer curvature
    • Szule J.A., Fuller N.L., Rand R.P. The effects of acyl chain length and saturation of diacylglycerols and phosphatidylcholines on membrane monolayer curvature. Biophys. J. 2002, 83:977-984.
    • (2002) Biophys. J. , vol.83 , pp. 977-984
    • Szule, J.A.1    Fuller, N.L.2    Rand, R.P.3
  • 44
  • 46
    • 0027964870 scopus 로고
    • Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain
    • Valverde A.M., Sinnett-Smith J., Van Lint J., Rozengurt E. Molecular cloning and characterization of protein kinase D: a target for diacylglycerol and phorbol esters with a distinctive catalytic domain. Proc. Natl. Acad. Sci. USA 1994, 91:8572-8576.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8572-8576
    • Valverde, A.M.1    Sinnett-Smith, J.2    Van Lint, J.3    Rozengurt, E.4
  • 47
    • 0035933884 scopus 로고    scopus 로고
    • Cooperativity between the preproinsulin mRNA untranslated regions is necessary for glucose-stimulated translation
    • Wicksteed B., Herbert T.P., Alarcon C., Lingohr M.K., Moss L.G., Rhodes C.J. Cooperativity between the preproinsulin mRNA untranslated regions is necessary for glucose-stimulated translation. J. Biol. Chem. 2001, 276:22553-22558.
    • (2001) J. Biol. Chem. , vol.276 , pp. 22553-22558
    • Wicksteed, B.1    Herbert, T.P.2    Alarcon, C.3    Lingohr, M.K.4    Moss, L.G.5    Rhodes, C.J.6
  • 48
    • 0033031679 scopus 로고    scopus 로고
    • Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D
    • Williger B.T., Provost J.J., Ho W.T., Milstine J., Exton J.H. Arfaptin 1 forms a complex with ADP-ribosylation factor and inhibits phospholipase D. FEBS Lett. 1999, 454:85-89.
    • (1999) FEBS Lett. , vol.454 , pp. 85-89
    • Williger, B.T.1    Provost, J.J.2    Ho, W.T.3    Milstine, J.4    Exton, J.H.5


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