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Volumn 5, Issue JANUARY2016, 2016, Pages

The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE EXCHANGE FACTOR; MEMBRANE PROTEIN; RHEB PROTEIN; ADENOSINE DIPHOSPHATE RIBOSYLATION FACTOR 1; SEC7 GUANINE NUCLEOTIDE EXCHANGE FACTORS;

EID: 84958559313     PISSN: None     EISSN: 2050084X     Source Type: Journal    
DOI: 10.7554/eLife.12411.001     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0023746682 scopus 로고
    • SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast golgi apparatus
    • Achstetter T, Franzusoff A, Field C, Schekman R. 1988. SEC7 encodes an unusual, high molecular weight protein required for membrane traffic from the yeast golgi apparatus. The Journal of Biological Chemistry 263: 11711-11717.
    • (1988) The Journal of Biological Chemistry , vol.263 , pp. 11711-11717
    • Achstetter, T.1    Franzusoff, A.2    Field, C.3    Schekman, R.4
  • 3
    • 79960766105 scopus 로고    scopus 로고
    • Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile
    • Amlacher S, Sarges P, Flemming D, van Noort V, Kunze R, Devos DP, Arumugam M, Bork P, Hurt E. 2011. Insight into structure and assembly of the nuclear pore complex by utilizing the genome of a eukaryotic thermophile. Cell 146: 277-289. doi: 10. 1016/j. cell. 2011. 06. 039.
    • (2011) Cell , vol.146 , pp. 277-289
    • Amlacher, S.1    Sarges, P.2    Flemming, D.3    van Noort, V.4    Kunze, R.5    Devos, D.P.6    Arumugam, M.7    Bork, P.8    Hurt, E.9
  • 4
    • 0030891289 scopus 로고    scopus 로고
    • N-terminal hydrophobic residues of the g-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange
    • Antonny B, Beraud-Dufour S, Chardin P, Chabre M. 1997. N-terminal hydrophobic residues of the g-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36: 4675-4684. doi: 10. 1021/bi962252b.
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 6
    • 84890216020 scopus 로고    scopus 로고
    • West syndrome, microcephaly, grey matter heterotopia and hypoplasia of corpus callosum due to a novel ARFGEF2 mutation
    • Banne E, Atawneh O, Henneke M, Brockmann K, Gartner J, Elpeleg O, Edvardson S. 2013. West syndrome, microcephaly, grey matter heterotopia and hypoplasia of corpus callosum due to a novel ARFGEF2 mutation. Journal of Medical Genetics 50: 772-775. doi: 10. 1136/jmedgenet-2013-101752.
    • (2013) Journal of Medical Genetics , vol.50 , pp. 772-775
    • Banne, E.1    Atawneh, O.2    Henneke, M.3    Brockmann, K.4    Gartner, J.5    Elpeleg, O.6    Edvardson, S.7
  • 9
    • 30544453616 scopus 로고    scopus 로고
    • Real-Time Assays for the Assembly-Disassembly Cycle of COP Coats on Liposomes of Defined Size
    • Elsevier
    • Bigay J, Antonny B. 2005. Real-Time Assays for the Assembly-Disassembly Cycle of COP Coats on Liposomes of Defined Size. in: Bigay Joëlle, Antonny Bruno eds GTPases Regulating Membrane Dynamics. Elsevier, pp. 95-107. doi: 10. 1016/S0076-6879(05)04010-3.
    • (2005) Bigay Joëlle, Antonny Bruno eds GTPases Regulating Membrane Dynamics , pp. 95-107
    • Bigay, J.1    Antonny, B.2
  • 10
    • 35348884249 scopus 로고    scopus 로고
    • Regulation of arf activation: The Sec7 family of guanine nucleotide exchange factors
    • Casanova JE. 2007. Regulation of arf activation: the Sec7 family of guanine nucleotide exchange factors. Traffic 8: 1476-1485. doi: 10. 1111/j. 1600-0854. 2007. 00634. x.
    • (2007) Traffic , vol.8 , pp. 1476-1485
    • Casanova, J.E.1
  • 13
    • 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. 2012. The small g protein Arl1 directs the trans-golgi-specific targeting of the Arf1 exchange factors BIG1 and BIG2. The Journal of Cell Biology 196: 327-335. doi: 10. 1083/jcb. 201107115.
    • (2012) The Journal of Cell Biology , vol.196 , pp. 327-335
    • Christis, C.1    Munro, S.2
  • 15
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: Expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky TJ, Czodrowski P, Li H, Nielsen JE, Jensen JH, Klebe G, Baker NA. 2007. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Research 35: W522-W525. doi: 10. 1093/nar/gkm276.
    • (2007) Nucleic Acids Research , vol.35 , pp. W522-W525
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6    Baker, N.A.7
  • 16
    • 79957473559 scopus 로고    scopus 로고
    • ARF family g proteins and their regulators: Roles in membrane transport, development and disease
    • Donaldson JG, Jackson CL. 2011. ARF family g proteins and their regulators: roles in membrane transport, development and disease. Nature Reviews Molecular Cell Biology 12: 362-375. doi: 10. 1038/nrm3117.
    • (2011) Nature Reviews Molecular Cell Biology , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 17
    • 0030045345 scopus 로고    scopus 로고
    • Origins of cell polarity
    • Drubin DG, Nelson WJ. 1996. Origins of cell polarity. Cell 84: 335-344.
    • (1996) Cell , vol.84 , pp. 335-344
    • Drubin, D.G.1    Nelson, W.J.2
  • 20
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: Mechanisms of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg J. 1998. Structural basis for activation of ARF GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95: 237-248.
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 23
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of gs by cholera toxin is itself a GTP binding protein
    • Kahn RA, Gilman AG. 1986. The protein cofactor necessary for ADP-ribosylation of gs by cholera toxin is itself a GTP binding protein. The Journal of Biological Chemistry 261: 7906-7911.
    • (1986) The Journal of Biological Chemistry , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 24
    • 79651475078 scopus 로고    scopus 로고
    • Modeling vesicle traffic reveals unexpected consequences for Cdc42p-mediated polarity establishment
    • Layton AT, Savage NS, Howell AS, Carroll SY, Drubin DG, Lew DJ. 2011. Modeling vesicle traffic reveals unexpected consequences for Cdc42p-mediated polarity establishment. Current Biology 21: 184-194. doi: 10. 1016/j. cub. 2011. 01. 012.
    • (2011) Current Biology , vol.21 , pp. 184-194
    • Layton, A.T.1    Savage, N.S.2    Howell, A.S.3    Carroll, S.Y.4    Drubin, D.G.5    Lew, D.J.6
  • 25
    • 84876567874 scopus 로고    scopus 로고
    • The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-golgi network (tGN)
    • Lowery J, Szul T, Styers M, Holloway Z, Oorschot V, Klumperman J, Sztul E. 2013. The Sec7 guanine nucleotide exchange factor GBF1 regulates membrane recruitment of BIG1 and BIG2 guanine nucleotide exchange factors to the trans-golgi network (tGN). The Journal of Biological Chemistry 288: 11532-11545. doi: 10. 1074/jbc. M112. 438481.
    • (2013) The Journal of Biological Chemistry , vol.288 , pp. 11532-11545
    • Lowery, J.1    Szul, T.2    Styers, M.3    Holloway, Z.4    Oorschot, V.5    Klumperman, J.6    Sztul, E.7
  • 28
    • 0036091999 scopus 로고    scopus 로고
    • Isolation and mapping of self-assembling protein domains encoded by the saccharomyces cerevisiae genome using lambda repressor fusions
    • Mariño-Ramírez L, Hu JC. 2002. Isolation and mapping of self-assembling protein domains encoded by the saccharomyces cerevisiae genome using lambda repressor fusions. Yeast 19: 641-650. doi: 10. 1002/yea. 867.
    • (2002) Yeast , vol.19 , pp. 641-650
    • Mariño-Ramírez, L.1    Hu, J.C.2
  • 29
    • 84908152566 scopus 로고    scopus 로고
    • Four GTPases differentially regulate the Sec7 arf-GEF to direct traffic at the trans-golgi network
    • McDonold CM, Fromme JC. 2014. Four GTPases differentially regulate the Sec7 arf-GEF to direct traffic at the trans-golgi network. Developmental Cell 30: 759-767. doi: 10. 1016/j. devcel. 2014. 07. 016.
    • (2014) Developmental Cell , vol.30 , pp. 759-767
    • McDonold, C.M.1    Fromme, J.C.2
  • 30
    • 0029803428 scopus 로고    scopus 로고
    • Isolation of a brefeldin a-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (aRF) 1 and ARF3 that contains a Sec7-like domain
    • Morinaga N, Tsai S-C, Moss J, Vaughan M. 1996. Isolation of a brefeldin a-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (aRF) 1 and ARF3 that contains a Sec7-like domain. Proceedings of the National Academy of Sciences of the United States of America 93: 12856-12860. doi: 10. 1073/pnas. 93. 23. 12856.
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 12856-12860
    • Morinaga, N.1    Tsai, S.-C.2    Moss, J.3    Vaughan, M.4
  • 32
    • 84859780873 scopus 로고    scopus 로고
    • High-throughput biological small-angle x-ray scattering with a robotically loaded capillary cell
    • Nielsen SS, Møller M, Gillilan RE. 2012. High-throughput biological small-angle x-ray scattering with a robotically loaded capillary cell. Journal of Applied Crystallography 45: 213-223. doi: 10. 1107/S0021889812000957.
    • (2012) Journal of Applied Crystallography , vol.45 , pp. 213-223
    • Nielsen, S.S.1    Møller, M.2    Gillilan, R.E.3
  • 33
    • 0018930046 scopus 로고
    • Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway
    • Novick P, Field C, Schekman R. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21: 205-215.
    • (1980) Cell , vol.21 , pp. 205-215
    • Novick, P.1    Field, C.2    Schekman, R.3
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Charles W, Carter J eds Academic Press
    • Otwinowski Z, Minor W. 1997. Processing of X-ray diffraction data collected in oscillation mode. in: Charles W, Carter J eds Methods in Enzymology. Academic Press. pp. 307-326.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 84868549149 scopus 로고    scopus 로고
    • The exomer cargo adaptor structure reveals a novel GTPase-binding domain
    • Paczkowski JE, Richardson BC, Strassner AM, Fromme JC. 2012. The exomer cargo adaptor structure reveals a novel GTPase-binding domain. The EMBO Journal 31: 4191-4203. doi: 10. 1038/emboj. 2012. 268.
    • (2012) The EMBO Journal , vol.31 , pp. 4191-4203
    • Paczkowski, J.E.1    Richardson, B.C.2    Strassner, A.M.3    Fromme, J.C.4
  • 36
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA. 2006. Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallographica Section D Biological Crystallography 62: 439-450. doi: 10. 1107/S0907444906005270.
    • (2006) Acta Crystallographica Section D Biological Crystallography , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 38
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI. 2005. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophysical Journal 89: 1237-1250. doi: 10. 1529/biophysj. 105. 064154.
    • (2005) Biophysical Journal , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 39
    • 0029851773 scopus 로고    scopus 로고
    • Nucleotide exchange on ARF mediated by yeast Gea1 protein
    • Peyroche A, Paris S, Jackson CL. 1996. Nucleotide exchange on ARF mediated by yeast Gea1 protein. Nature 384: 479-481. doi: 10. 1038/384479a0.
    • (1996) Nature , vol.384 , pp. 479-481
    • Peyroche, A.1    Paris, S.2    Jackson, C.L.3
  • 42
    • 0037133511 scopus 로고    scopus 로고
    • Mechanism of domain closure of Sec7 domains and role in BFA sensitivity
    • Renault L, Christova P, Guibert B, Pasqualato S, Cherfils J. 2002. Mechanism of domain closure of Sec7 domains and role in BFA sensitivity. Biochemistry 41: 3605-3612. doi: 10. 1021/bi012123h.
    • (2002) Biochemistry , vol.41 , pp. 3605-3612
    • Renault, L.1    Christova, P.2    Guibert, B.3    Pasqualato, S.4    Cherfils, J.5
  • 43
    • 84870230066 scopus 로고    scopus 로고
    • Autoregulation of Sec7 arf-GEF activity and localization by positive feedback
    • Richardson BC, Fromme JC. 2012. Autoregulation of Sec7 arf-GEF activity and localization by positive feedback. Small GTPases 3: 240-243. doi: 10. 4161/sgtp. 21828.
    • (2012) Small GTPases , vol.3 , pp. 240-243
    • Richardson, B.C.1    Fromme, J.C.2
  • 44
    • 84945478082 scopus 로고    scopus 로고
    • Biochemical methods for studying kinetic regulation of Arf1 activation by Sec7
    • Richardson Brian C., Fromme J. Elsevier
    • Richardson BC, Fromme JC. 2015. Biochemical methods for studying kinetic regulation of Arf1 activation by Sec7. in: Richardson Brian C., Fromme J. Christopher eds Sorting and Recycling Endosomes. Elsevier, pp. 101-126. doi: 10. 1016/bs. mcb. 2015. 03. 020.
    • (2015) Christopher eds Sorting and Recycling Endosomes , pp. 101-126
    • Richardson, B.C.1    Fromme, J.C.2
  • 45
    • 84859809253 scopus 로고    scopus 로고
    • The Sec7 arf-GEF is recruited to the trans-golgi network by positive feedback
    • Richardson BC, McDonold CM, Fromme JC. 2012. The Sec7 arf-GEF is recruited to the trans-golgi network by positive feedback. Developmental Cell 22: 799-810. doi: 10. 1016/j. devcel. 2012. 02. 006.
    • (2012) Developmental Cell , vol.22 , pp. 799-810
    • Richardson, B.C.1    McDonold, C.M.2    Fromme, J.C.3
  • 47
    • 2342497804 scopus 로고    scopus 로고
    • Golgi targeting of ARF-like GTPase Arl3p requires its nalpha-acetylation and the integral membrane protein Sys1p
    • Setty SR, Strochlic TI, Tong AH, Boone C, Burd CG. 2004. Golgi targeting of ARF-like GTPase Arl3p requires its nalpha-acetylation and the integral membrane protein Sys1p. Nature Cell Biology 6: 414-419. doi: 10. 1038/ncb1121.
    • (2004) Nature Cell Biology , vol.6 , pp. 414-419
    • Setty, S.R.1    Strochlic, T.I.2    Tong, A.H.3    Boone, C.4    Burd, C.G.5
  • 49
    • 0025221221 scopus 로고
    • ADP ribosylation factor is an essential protein in saccharomyces cerevisiae and is encoded by two genes
    • Stearns T, Kahn RA, Botstein D, Hoyt MA. 1990. ADP ribosylation factor is an essential protein in saccharomyces cerevisiae and is encoded by two genes. Molecular and Cellular Biology 10: 6690-6699.
    • (1990) Molecular and Cellular Biology , vol.10 , pp. 6690-6699
    • Stearns, T.1    Kahn, R.A.2    Botstein, D.3    Hoyt, M.A.4
  • 50
    • 0029185933 scopus 로고
    • CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
    • Svergun D, Barberato C, Koch MHJ. 1995. CRYSOL-a program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates. Journal of Applied Crystallography 28: 768-773. doi: 10. 1107/S0021889895007047.
    • (1995) Journal of Applied Crystallography , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3
  • 51
    • 84900831421 scopus 로고    scopus 로고
    • The arf family g protein Arl1 is required for secretory granule biogenesis in drosophila
    • Torres IL, Rosa-Ferreira C, Munro S. 2014. The arf family g protein Arl1 is required for secretory granule biogenesis in drosophila. Journal of Cell Science 127: 2151-2160. doi: 10. 1242/jcs. 122028.
    • (2014) Journal of Cell Science , vol.127 , pp. 2151-2160
    • Torres, I.L.1    Rosa-Ferreira, C.2    Munro, S.3
  • 52
    • 0024801630 scopus 로고
    • Nucleotide binding and cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor
    • Weiss O, Holden J, Rulka C, Kahn RA. 1989. Nucleotide binding and cofactor activities of purified bovine brain and bacterially expressed ADP-ribosylation factor. The Journal of Biological Chemistry 264: 21066-21072.
    • (1989) The Journal of Biological Chemistry , vol.264 , pp. 21066-21072
    • Weiss, O.1    Holden, J.2    Rulka, C.3    Kahn, R.A.4
  • 54
    • 2942729663 scopus 로고    scopus 로고
    • Differences between AGAP1, ASAP1 and arf GAP1 in substrate recognition: Interaction with the n-terminus of Arf1
    • Yoon HY, Jacques K, Nealon B, Stauffer S, Premont RT, Randazzo PA. 2004. Differences between AGAP1, ASAP1 and arf GAP1 in substrate recognition: interaction with the n-terminus of Arf1. Cellular Signalling 16: 1033-1044. doi: 10. 1016/j. cellsig. 2004. 02. 008.
    • (2004) Cellular Signalling , vol.16 , pp. 1033-1044
    • Yoon, H.Y.1    Jacques, K.2    Nealon, B.3    Stauffer, S.4    Premont, R.T.5    Randazzo, P.A.6


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