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Volumn 290, Issue 44, 2015, Pages 26373-26382

Structural basis for the interaction between the Golgi reassembly-stacking protein GRASP65 and the Golgi matrix protein GM130

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MEMBRANES; PROTEINS;

EID: 84946058005     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.657940     Document Type: Article
Times cited : (35)

References (47)
  • 1
    • 0019769965 scopus 로고
    • The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage
    • Farquhar, M. G., and Palade, G. E. (1981) The Golgi apparatus (complex)-(1954-1981)-from artifact to center stage. J. Cell Biol. 91, 77s-103s
    • (1981) J. Cell Biol. , vol.91 , pp. 77s-103s
    • Farquhar, M.G.1    Palade, G.E.2
  • 2
    • 0025233925 scopus 로고
    • Three-dimensional electron microscopy: Structure of the Golgi apparatus
    • Rambourg, A., and Clermont, Y. (1990) Three-dimensional electron microscopy: structure of the Golgi apparatus. Eur. J. Cell Biol. 51, 189-200
    • (1990) Eur. J. Cell Biol. , vol.51 , pp. 189-200
    • Rambourg, A.1    Clermont, Y.2
  • 4
    • 0027055402 scopus 로고
    • Adhesion of Golgi cisternae by proteinaceous interactions: Intercisternal bridges as putative adhesive structures
    • Cluett, E. B., and Brown, W. J. (1992) Adhesion of Golgi cisternae by proteinaceous interactions: intercisternal bridges as putative adhesive structures. J. Cell Sci. 103, 773-784
    • (1992) J. Cell Sci. , vol.103 , pp. 773-784
    • Cluett, E.B.1    Brown, W.J.2
  • 6
    • 0033568489 scopus 로고    scopus 로고
    • GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system
    • Shorter, J., Watson, R., Giannakou, M. E., Clarke, M., Warren, G., and Barr, F. A. (1999) GRASP55, a second mammalian GRASP protein involved in the stacking of Golgi cisternae in a cell-free system. EMBO J. 18, 4949-4960
    • (1999) EMBO J. , vol.18 , pp. 4949-4960
    • Shorter, J.1    Watson, R.2    Giannakou, M.E.3    Clarke, M.4    Warren, G.5    Barr, F.A.6
  • 7
    • 0028930157 scopus 로고
    • Reassembly of Golgi stacks from mitotic Golgi fragmentsin a cell-free system
    • Rabouille, C., Misteli, T., Watson, R., and Warren, G. (1995) Reassembly of Golgi stacks from mitotic Golgi fragmentsin a cell-free system. J. Cell Biol. 129, 605-618
    • (1995) J. Cell Biol. , vol.129 , pp. 605-618
    • Rabouille, C.1    Misteli, T.2    Watson, R.3    Warren, G.4
  • 8
    • 0030662715 scopus 로고    scopus 로고
    • GRASP65, a protein involved in the stacking of Golgi cisternae
    • Barr, F. A., Puype, M., Vandekerckhove, J., and Warren, G. (1997) GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91, 253-262
    • (1997) Cell , vol.91 , pp. 253-262
    • Barr, F.A.1    Puype, M.2    Vandekerckhove, J.3    Warren, G.4
  • 9
    • 51349095514 scopus 로고    scopus 로고
    • GRASP55 regulates Golgi ribbon formation
    • Feinstein, T. N., and Linstedt, A. D. (2008) GRASP55 regulates Golgi ribbon formation. Mol. Biol. Cell 19, 2696-2707
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2696-2707
    • Feinstein, T.N.1    Linstedt, A.D.2
  • 10
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • Puthenveedu, M. A., Bachert, C., Puri, S., Lanni, F., and Linstedt, A. D. (2006) GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat. Cell Biol. 8, 238-248
    • (2006) Nat. Cell Biol. , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 11
    • 76149083892 scopus 로고    scopus 로고
    • GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking
    • Xiang, Y., and Wang, Y. (2010) GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stacking. J. Cell Biol. 188, 237-251
    • (2010) J. Cell Biol. , vol.188 , pp. 237-251
    • Xiang, Y.1    Wang, Y.2
  • 12
    • 84877777009 scopus 로고    scopus 로고
    • Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65
    • Xiang, Y., Zhang, X., Nix, D. B., Katoh, T., Aoki, K., Tiemeyer, M., and Wang, Y. (2013) Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65. Nat. Commun. 4, 1659
    • (2013) Nat. Commun. , vol.4 , pp. 1659
    • Xiang, Y.1    Zhang, X.2    Nix, D.B.3    Katoh, T.4    Aoki, K.5    Tiemeyer, M.6    Wang, Y.7
  • 13
    • 84891812680 scopus 로고    scopus 로고
    • Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization
    • Jarvela, T., and Linstedt, A. D. (2014) Isoform-specific tethering links the Golgi ribbon to maintain compartmentalization. Mol. Biol. Cell 25, 133-144
    • (2014) Mol. Biol. Cell , vol.25 , pp. 133-144
    • Jarvela, T.1    Linstedt, A.D.2
  • 15
    • 43749087389 scopus 로고    scopus 로고
    • Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5in a p115-regulated manner
    • Diao, A., Frost, L., Morohashi, Y., and Lowe, M. (2008) Coordination of golgin tethering and SNARE assembly: GM130 binds syntaxin 5in a p115-regulated manner. J. Biol. Chem. 283, 6957-6967
    • (2008) J. Biol. Chem. , vol.283 , pp. 6957-6967
    • Diao, A.1    Frost, L.2    Morohashi, Y.3    Lowe, M.4
  • 16
    • 77950634328 scopus 로고    scopus 로고
    • Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions
    • Nakamura, N. (2010) Emerging new roles of GM130, a cis-Golgi matrix protein, in higher order cell functions. J. Pharmacol. Sci. 112, 255-264
    • (2010) J. Pharmacol. Sci. , vol.112 , pp. 255-264
    • Nakamura, N.1
  • 18
    • 84901640125 scopus 로고    scopus 로고
    • Crystal structure of a heterotetrameric NMDA receptor ion channel
    • Karakas, E., and Furukawa, H. (2014) Crystal structure of a heterotetrameric NMDA receptor ion channel. Science 344, 992-997
    • (2014) Science , vol.344 , pp. 992-997
    • Karakas, E.1    Furukawa, H.2
  • 19
    • 0036544571 scopus 로고    scopus 로고
    • Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115
    • Shorter, J., and Beard., M. B., Seemann, J., Dirac-Svejstrup, A. B., and Warren, G. (2002) Sequential tethering of Golgins and catalysis of SNAREpin assembly by the vesicle-tethering protein p115. J. Cell Biol. 157, 45-62
    • (2002) J. Cell Biol. , vol.157 , pp. 45-62
    • Shorter, J.1    Beard, M.B.2    Seemann, J.3    Dirac-Svejstrup, A.B.4    Warren, G.5
  • 20
    • 0033549551 scopus 로고    scopus 로고
    • A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system
    • Shorter, J., and Warren, G. (1999) A role for the vesicle tethering protein, p115, in the post-mitotic stacking of reassembling Golgi cisternae in a cell-free system. J. Cell Biol. 146, 57-70
    • (1999) J. Cell Biol. , vol.146 , pp. 57-70
    • Shorter, J.1    Warren, G.2
  • 21
    • 0030953187 scopus 로고    scopus 로고
    • The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
    • Nakamura, N., Lowe, M., Levine, T. P., Rabouille, C., and Warren, G. (1997) The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner. Cell 89, 445-455
    • (1997) Cell , vol.89 , pp. 445-455
    • Nakamura, N.1    Lowe, M.2    Levine, T.P.3    Rabouille, C.4    Warren, G.5
  • 22
    • 0034616420 scopus 로고    scopus 로고
    • Binding relationships of membrane tethering components: The Giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus
    • Linstedt, A. D., and Jesch., S. A., Mehta, A., Lee, T. H., Garcia-Mata, R., Nelson, D. S., and Sztul, E. (2000) Binding relationships of membrane tethering components: the Giantin N terminus and the GM130 N terminus compete for binding to the p115 C terminus. J. Biol. Chem. 275, 10196-10201
    • (2000) J. Biol. Chem. , vol.275 , pp. 10196-10201
    • Linstedt, A.D.1    Jesch, S.A.2    Mehta, A.3    Lee, T.H.4    Garcia-Mata, R.5    Nelson, D.S.6    Sztul, E.7
  • 23
    • 0035889084 scopus 로고    scopus 로고
    • Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components Giantin and GM130
    • Puthenveedu, M. A., and Linstedt, A. D. (2001) Evidence that Golgi structure depends on a p115 activity that is independent of the vesicle tether components Giantin and GM130. J. Cell Biol. 155, 227-238
    • (2001) J. Cell Biol. , vol.155 , pp. 227-238
    • Puthenveedu, M.A.1    Linstedt, A.D.2
  • 24
    • 0032526720 scopus 로고    scopus 로고
    • Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae
    • Barr, F. A., Nakamura, N., and Warren, G. (1998) Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae. EMBO J. 17, 3258-3268
    • (1998) EMBO J. , vol.17 , pp. 3258-3268
    • Barr, F.A.1    Nakamura, N.2    Warren, G.3
  • 25
    • 39449124362 scopus 로고    scopus 로고
    • The Golgi protein GM130 regulates centrosome morphology and function
    • Kodani, A., and Sütterlin, C. (2008) The Golgi protein GM130 regulates centrosome morphology and function. Mol. Biol. Cell 19, 745-753
    • (2008) Mol. Biol. Cell , vol.19 , pp. 745-753
    • Kodani, A.1    Sütterlin, C.2
  • 26
    • 77952417354 scopus 로고    scopus 로고
    • Dual anchoring of the GRASP membrane tether promotes trans pairing
    • Bachert, C., and Linstedt, A. D. (2010) Dual anchoring of the GRASP membrane tether promotes trans pairing. J. Biol. Chem. 285, 16294-16301
    • (2010) J. Biol. Chem. , vol.285 , pp. 16294-16301
    • Bachert, C.1    Linstedt, A.D.2
  • 27
    • 79957985741 scopus 로고    scopus 로고
    • Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis
    • Truschel, S. T., Sengupta, D., Foote, A., Heroux, A., and Macbeth., M. R., and Linstedt, A. D. (2011) Structure of the membrane-tethering GRASP domain reveals a unique PDZ ligand interaction that mediates Golgi biogenesis. J. Biol. Chem. 286, 20125-20129
    • (2011) J. Biol. Chem. , vol.286 , pp. 20125-20129
    • Truschel, S.T.1    Sengupta, D.2    Foote, A.3    Heroux, A.4    Macbeth, M.R.5    Linstedt, A.D.6
  • 28
    • 84884759069 scopus 로고    scopus 로고
    • Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins
    • Feng, Y., Yu, W., Li, X., Lin, S., Zhou, Y., Hu, J., and Liu, X. (2013) Structural insight into Golgi membrane stacking by GRASP65 and GRASP55 proteins. J. Biol. Chem. 288, 28418-28427
    • (2013) J. Biol. Chem. , vol.288 , pp. 28418-28427
    • Feng, Y.1    Yu, W.2    Li, X.3    Lin, S.4    Zhou, Y.5    Hu, J.6    Liu, X.7
  • 29
    • 84862023539 scopus 로고    scopus 로고
    • Allosteric regulation of GRASP protein-dependent Golgi membrane tethering by mitotic phosphorylation
    • Truschel, S. T., Zhang, M., Bachert, C., Macbeth, M. R., and Linstedt, A. D. (2012) Allosteric regulation of GRASP protein-dependent Golgi membrane tethering by mitotic phosphorylation. J. Biol. Chem. 287, 19870-19875
    • (2012) J. Biol. Chem. , vol.287 , pp. 19870-19875
    • Truschel, S.T.1    Zhang, M.2    Bachert, C.3    Macbeth, M.R.4    Linstedt, A.D.5
  • 30
    • 84964817434 scopus 로고    scopus 로고
    • Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly
    • Tang, D., Yuan, H., Vielemeyer, O., Perez, F., and Wang, Y. (2012) Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly. Biol. Open 1, 1204-1214
    • (2012) Biol. Open , vol.1 , pp. 1204-1214
    • Tang, D.1    Yuan, H.2    Vielemeyer, O.3    Perez, F.4    Wang, Y.5
  • 31
    • 67650475442 scopus 로고    scopus 로고
    • Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network
    • Sengupta, D., Truschel, S., Bachert, C., and Linstedt, A. D. (2009) Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network. J. Cell Biol. 186, 41-55
    • (2009) J. Cell Biol. , vol.186 , pp. 41-55
    • Sengupta, D.1    Truschel, S.2    Bachert, C.3    Linstedt, A.D.4
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of x-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of x-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 38
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace, A. C., and Laskowski., R. A., and Thornton, J. M. (1995) LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127-134
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 39
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: Structure, specificity, and modification
    • Lee, H. J., and Zheng, J. J. (2010) PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun. Signal. 8, 8
    • (2010) Cell Commun. Signal. , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 40
    • 84934934537 scopus 로고    scopus 로고
    • Interdomain interface-mediated target recognition by the Scribble PDZ34 supramodule
    • Ren, J., Feng, L., Bai, Y., Pei, H., Yuan, Z., and Feng, W. (2015) Interdomain interface-mediated target recognition by the Scribble PDZ34 supramodule. Biochem. J. 468, 133-144
    • (2015) Biochem. J. , vol.468 , pp. 133-144
    • Ren, J.1    Feng, L.2    Bai, Y.3    Pei, H.4    Yuan, Z.5    Feng, W.6
  • 42
    • 67651095767 scopus 로고    scopus 로고
    • Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering
    • An, Y., and Chen., C. Y., Moyer, B., Rotkiewicz, P., Elsliger, M. A., Godzik, A., and Wilson., I. A., and Balch, W. E. (2009) Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering. J. Mol. Biol. 391, 26-41
    • (2009) J. Mol. Biol. , vol.391 , pp. 26-41
    • An, Y.1    Chen, C.Y.2    Moyer, B.3    Rotkiewicz, P.4    Elsliger, M.A.5    Godzik, A.6    Wilson, I.A.7    Balch, W.E.8
  • 43
    • 84864285674 scopus 로고    scopus 로고
    • Unusual armadillo fold in the human general vesicular transport factor p115
    • Striegl, H., Roske, Y., Kümmel, D., and Heinemann, U. (2009) Unusual armadillo fold in the human general vesicular transport factor p115. PloS One 4, e4656
    • (2009) PloS One , vol.4
    • Striegl, H.1    Roske, Y.2    Kümmel, D.3    Heinemann, U.4
  • 44
    • 0034618073 scopus 로고    scopus 로고
    • Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments
    • Dirac-Svejstrup, A. B., Shorter, J., Waters, M. G., and Warren, G. (2000) Phosphorylation of the vesicle-tethering protein p115 by a casein kinase II-like enzyme is required for Golgi reassembly from isolated mitotic fragments. J. Cell Biol. 150, 475-488
    • (2000) J. Cell Biol. , vol.150 , pp. 475-488
    • Dirac-Svejstrup, A.B.1    Shorter, J.2    Waters, M.G.3    Warren, G.4
  • 45
    • 0033999010 scopus 로고    scopus 로고
    • The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo
    • Seemann, J., and Jokitalo., E. J., and Warren, G. (2000) The role of the tethering proteins p115 and GM130 in transport through the Golgi apparatus in vivo. Mol. Biol. Cell 11, 635-645
    • (2000) Mol. Biol. Cell , vol.11 , pp. 635-645
    • Seemann, J.1    Jokitalo, E.J.2    Warren, G.3
  • 46
    • 0032478142 scopus 로고    scopus 로고
    • Vesicles on strings: Morphological evidence for processive transport within the Golgi stack
    • Orci, L., Perrelet, A., and Rothman, J. E. (1998) Vesicles on strings: morphological evidence for processive transport within the Golgi stack. Proc. Natl. Acad. Sci. U.S.A. 95, 2279-2283
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 2279-2283
    • Orci, L.1    Perrelet, A.2    Rothman, J.E.3
  • 47
    • 84904790793 scopus 로고    scopus 로고
    • Deciphering key features in protein structures with the new ENDscript server
    • Robert, X., and Gouet, P. (2014) Deciphering key features in protein structures with the new ENDscript server. Nucleic Acids Res. 42, W320-324
    • (2014) Nucleic Acids Res. , vol.42 , pp. W320-W324
    • Robert, X.1    Gouet, P.2


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