메뉴 건너뛰기




Volumn 171, Issue 6, 2006, Pages 707-717

The Arabidopsis ADP-ribosylation factor (ARF) and ARF-like (ARL) system and its regulation by BIG2, a large ARF-GEF

Author keywords

Arabidopsis ARF and ARL proteins; Catalysis of GDP GTP exchange; Sec7 ARF GEFs

Indexed keywords

ARABIDOPSIS ARF AND ARL PROTEINS; CATALYSIS OF GDP/GTP EXCHANGE; SEC7 ARF-GEF;

EID: 33749527682     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plantsci.2006.07.002     Document Type: Article
Times cited : (14)

References (46)
  • 1
    • 0036866606 scopus 로고    scopus 로고
    • Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for "front-back" communication
    • Pasqualato S., Renault L., and Cherfils J. Arf, Arl, Arp and Sar proteins: a family of GTP-binding proteins with a structural device for "front-back" communication. EMBO Rep. 3 (2002) 1035-1041
    • (2002) EMBO Rep. , vol.3 , pp. 1035-1041
    • Pasqualato, S.1    Renault, L.2    Cherfils, J.3
  • 2
    • 0142211351 scopus 로고    scopus 로고
    • Multiple roles for Arf6: sorting, structuring, and signaling at the plasma membrane
    • Donaldson J.G. Multiple roles for Arf6: sorting, structuring, and signaling at the plasma membrane. J. Biol. Chem. 278 (2003) 41573-41576
    • (2003) J. Biol. Chem. , vol.278 , pp. 41573-41576
    • Donaldson, J.G.1
  • 3
    • 0035933796 scopus 로고    scopus 로고
    • ADP-ribosylation factors (ARFs) and ARF-like (ARL1) have both specific and shared effectors
    • Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., and Kahn R.A. ADP-ribosylation factors (ARFs) and ARF-like (ARL1) have both specific and shared effectors. J. Biol. Chem. 276 (2001) 22826-22837
    • (2001) J. Biol. Chem. , vol.276 , pp. 22826-22837
    • Van Valkenburgh, H.1    Shern, J.F.2    Sharer, J.D.3    Zhu, X.4    Kahn, R.A.5
  • 4
    • 1642464740 scopus 로고    scopus 로고
    • Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers
    • Cox R., Mason-Gamer R.J., Jackson C.L., and Segev N. Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers. Mol. Biol. Cell 15 (2004) 1487-1505
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1487-1505
    • Cox, R.1    Mason-Gamer, R.J.2    Jackson, C.L.3    Segev, N.4
  • 5
    • 0032538317 scopus 로고    scopus 로고
    • Structural basis for activation of ARF GTPase: mechanism of guanine nucleotide exchange and GTP-myristoyl switching
    • Goldberg J. Structural basis for activation of ARF GTPase: mechanism of guanine nucleotide exchange and GTP-myristoyl switching. Cell 95 (1998) 237-248
    • (1998) Cell , vol.95 , pp. 237-248
    • Goldberg, J.1
  • 6
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault L., Guibert B., and Cherfils J. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426 (2003) 525-530
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 8
    • 0036667381 scopus 로고    scopus 로고
    • Arf1 GTPase plays roles in the protein traffic between the endoplasmic reticulum and the Golgi apparatus in tobacco and Arabidopsis cultured cells
    • Takeuchi M., Ueda T., Yahara N., and Nakano A. Arf1 GTPase plays roles in the protein traffic between the endoplasmic reticulum and the Golgi apparatus in tobacco and Arabidopsis cultured cells. Plant J. 31 (2002) 499-515
    • (2002) Plant J. , vol.31 , pp. 499-515
    • Takeuchi, M.1    Ueda, T.2    Yahara, N.3    Nakano, A.4
  • 9
    • 0037008335 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis
    • Lee M.H., Min M.K., Lee Y.J., Jin J.B., Shin D.H., Kim D.H., Lee K.H., and Hwang I. ADP-ribosylation factor 1 of Arabidopsis plays a critical role in intracellular trafficking and maintenance of endoplasmic reticulum morphology in Arabidopsis. Plant Physiol. 129 (2002) 1507-1520
    • (2002) Plant Physiol. , vol.129 , pp. 1507-1520
    • Lee, M.H.1    Min, M.K.2    Lee, Y.J.3    Jin, J.B.4    Shin, D.H.5    Kim, D.H.6    Lee, K.H.7    Hwang, I.8
  • 10
    • 0038366776 scopus 로고    scopus 로고
    • The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole
    • Pimpl P., Hanton S.L., Taylor J.P., Pinto-DaSilva L.L., and Denecke J. The GTPase ARF1p controls the sequence-specific vacuolar sorting route to the lytic vacuole. Plant Cell 15 (2003) 1242-1256
    • (2003) Plant Cell , vol.15 , pp. 1242-1256
    • Pimpl, P.1    Hanton, S.L.2    Taylor, J.P.3    Pinto-DaSilva, L.L.4    Denecke, J.5
  • 11
    • 21744446803 scopus 로고    scopus 로고
    • Dissection of Arabidopsis ADP-ribosylation factor. Part 1. Function in epidermal cell polarity
    • Xu J., and Scheres B. Dissection of Arabidopsis ADP-ribosylation factor. Part 1. Function in epidermal cell polarity. Plant Cell. 17 (2005) 525-536
    • (2005) Plant Cell. , vol.17 , pp. 525-536
    • Xu, J.1    Scheres, B.2
  • 12
    • 0029015710 scopus 로고
    • Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes
    • Moss J., and Vaughan M. Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270 (1995) 12327-12330
    • (1995) J. Biol. Chem. , vol.270 , pp. 12327-12330
    • Moss, J.1    Vaughan, M.2
  • 13
    • 0036707861 scopus 로고    scopus 로고
    • Protein secretion in plants: from the trans-Golgi network to the outer space
    • Jurgens G., and Geldner N. Protein secretion in plants: from the trans-Golgi network to the outer space. Traffic 3 (2002) 605-613
    • (2002) Traffic , vol.3 , pp. 605-613
    • Jurgens, G.1    Geldner, N.2
  • 14
    • 0142252552 scopus 로고    scopus 로고
    • Analysis of the small GTPase gene superfamily of Arabidopsis
    • Vernoud V., Horton A.C., Yang Z., and Nielsen E. Analysis of the small GTPase gene superfamily of Arabidopsis. Plant Phys. 131 (2003) 1191-1208
    • (2003) Plant Phys. , vol.131 , pp. 1191-1208
    • Vernoud, V.1    Horton, A.C.2    Yang, Z.3    Nielsen, E.4
  • 15
    • 17144372270 scopus 로고    scopus 로고
    • Genes encoding ADP-ribosylation factors in Arabidopsis thaliana L. Heyn.; genome analysis and antisense suppression
    • Gebbie L.K., Burn J.E., Hocart C.H., and Williamson R.E. Genes encoding ADP-ribosylation factors in Arabidopsis thaliana L. Heyn.; genome analysis and antisense suppression. J. Exp. Bot. 56 (2005) 1079-1091
    • (2005) J. Exp. Bot. , vol.56 , pp. 1079-1091
    • Gebbie, L.K.1    Burn, J.E.2    Hocart, C.H.3    Williamson, R.E.4
  • 16
    • 0033827695 scopus 로고    scopus 로고
    • The TITAN5 gene of Arabidopsis encodes a protein related to the ADP ribosylation factor family of GTP binding proteins
    • McElver J., Patton D., Rumbaugh M., Liu C.-M., Yang L.J., and Meinke D. The TITAN5 gene of Arabidopsis encodes a protein related to the ADP ribosylation factor family of GTP binding proteins. Plant Cell 12 (2000) 1379-1392
    • (2000) Plant Cell , vol.12 , pp. 1379-1392
    • McElver, J.1    Patton, D.2    Rumbaugh, M.3    Liu, C.-M.4    Yang, L.J.5    Meinke, D.6
  • 18
    • 0028322046 scopus 로고
    • EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7
    • Shevell D.E., Leu W.M., Gillmor C.S., Xia G., Feldmann K.A., and Chua N.H. EMB30 is essential for normal cell division, cell expansion, and cell adhesion in Arabidopsis and encodes a protein that has similarity to Sec7. Cell 77 (1994) 1051-1062
    • (1994) Cell , vol.77 , pp. 1051-1062
    • Shevell, D.E.1    Leu, W.M.2    Gillmor, C.S.3    Xia, G.4    Feldmann, K.A.5    Chua, N.H.6
  • 20
    • 8444232728 scopus 로고    scopus 로고
    • The secretory system of Arabidopsis
    • Somerville C.R., and Meyerowitz E.M. (Eds), American Society of Plant Biologists, Rockville, MD
    • Sanderfoot A.A., and Raikhel N.V. The secretory system of Arabidopsis. In: Somerville C.R., and Meyerowitz E.M. (Eds). The Arabidopsis Book (2003), American Society of Plant Biologists, Rockville, MD 1-24
    • (2003) The Arabidopsis Book , pp. 1-24
    • Sanderfoot, A.A.1    Raikhel, N.V.2
  • 21
    • 0033617147 scopus 로고    scopus 로고
    • Purification and cloning of a Brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors
    • Togawa A., Morinaga N., Ogasawara M., Moss J., and Vaughan M. Purification and cloning of a Brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. J. Biol. Chem. 274 (1999) 12308-12315
    • (1999) J. Biol. Chem. , vol.274 , pp. 12308-12315
    • Togawa, A.1    Morinaga, N.2    Ogasawara, M.3    Moss, J.4    Vaughan, M.5
  • 23
    • 0142097228 scopus 로고    scopus 로고
    • Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity
    • Menetrey J., Macia E., Pasqualato S., Franco M., and Cherfils J. Structure of Arf6-GDP suggests a basis for guanine nucleotide exchange factors specificity. Nat. Struct. Biol. 7 (2000) 466-469
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 466-469
    • Menetrey, J.1    Macia, E.2    Pasqualato, S.3    Franco, M.4    Cherfils, J.5
  • 24
    • 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., and Chabre M. N-terminal hydrophobic residues of the G-protein ADP-ribosylation factor-1 insert into membrane phospholipids upon GDP to GTP exchange. Biochemistry 36 (1997) 4675-4684
    • (1997) Biochemistry , vol.36 , pp. 4675-4684
    • Antonny, B.1    Beraud-Dufour, S.2    Chardin, P.3    Chabre, M.4
  • 25
    • 0027495918 scopus 로고
    • Tryptophan W207 in transducin T alpha is the fluorescence sensor of the G protein activation switch and is involved in the effector binding
    • Faurobert E., Otto-Bruc A., Chardin P., and Chabre M. Tryptophan W207 in transducin T alpha is the fluorescence sensor of the G protein activation switch and is involved in the effector binding. EMBO J. 12 (1993) 4191-4198
    • (1993) EMBO J. , vol.12 , pp. 4191-4198
    • Faurobert, E.1    Otto-Bruc, A.2    Chardin, P.3    Chabre, M.4
  • 27
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg J. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96 (1999) 893-902
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 28
    • 0034566505 scopus 로고    scopus 로고
    • Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain
    • Jensen R.B., Lykke-Andersen K., Frandsen G.I., Nielsen H.B., Haseloff J., Jespersen H.M., Mundy J., and Skriver K. Promiscuous and specific phospholipid binding by domains in ZAC, a membrane-associated Arabidopsis protein with an ARF GAP zinc finger and a C2 domain. Plant Mol. Biol. 44 (2000) 799-814
    • (2000) Plant Mol. Biol. , vol.44 , pp. 799-814
    • Jensen, R.B.1    Lykke-Andersen, K.2    Frandsen, G.I.3    Nielsen, H.B.4    Haseloff, J.5    Jespersen, H.M.6    Mundy, J.7    Skriver, K.8
  • 29
    • 0027389461 scopus 로고
    • cDNA cloning and expression of an Arabidopsis GTP-binding protein of the ARF family
    • Regad F., Bardet C., Tremousaygue D., Moisan A., Lescure B., and Axelos M. cDNA cloning and expression of an Arabidopsis GTP-binding protein of the ARF family. FEBS Lett. 316 (1993) 133-136
    • (1993) FEBS Lett. , vol.316 , pp. 133-136
    • Regad, F.1    Bardet, C.2    Tremousaygue, D.3    Moisan, A.4    Lescure, B.5    Axelos, M.6
  • 31
    • 0032488847 scopus 로고    scopus 로고
    • Structure of the guanine nucleotide exchange factor Sec7 domain of human ARNO and analysis of the interaction with ARF GTPase
    • Mossessova E., Gulbis J.M., and Goldberg J. Structure of the guanine nucleotide exchange factor Sec7 domain of human ARNO and analysis of the interaction with ARF GTPase. Cell 92 (1998) 415-423
    • (1998) Cell , vol.92 , pp. 415-423
    • Mossessova, E.1    Gulbis, J.M.2    Goldberg, J.3
  • 33
    • 0035816551 scopus 로고    scopus 로고
    • Specificities for the small G proteins ARF1 and ARF6 of the guanine nucleotide exchange factors ARNO and EFA6
    • Macia E., Chabre M., and Franco M. Specificities for the small G proteins ARF1 and ARF6 of the guanine nucleotide exchange factors ARNO and EFA6. J. Biol. Chem. 276 (2001) 24925-24930
    • (2001) J. Biol. Chem. , vol.276 , pp. 24925-24930
    • Macia, E.1    Chabre, M.2    Franco, M.3
  • 34
    • 0035817625 scopus 로고    scopus 로고
    • Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D
    • Santy L.C., and Casanova J.E. Activation of ARF6 by ARNO stimulates epithelial cell migration through downstream activation of both Rac1 and phospholipase D. J. Cell Biol. 154 (2001) 599-610
    • (2001) J. Cell Biol. , vol.154 , pp. 599-610
    • Santy, L.C.1    Casanova, J.E.2
  • 35
    • 0035834688 scopus 로고    scopus 로고
    • Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases
    • Amor J.C., Horton J.R., Zhu X., Wang Y., Sullards C., Ringe D., Cheng X., and Kahn R.A. Structures of yeast ARF2 and ARL1: distinct roles for the N terminus in the structure and function of ARF family GTPases. J. Biol. Chem. 276 (2001) 42477-42484
    • (2001) J. Biol. Chem. , vol.276 , pp. 42477-42484
    • Amor, J.C.1    Horton, J.R.2    Zhu, X.3    Wang, Y.4    Sullards, C.5    Ringe, D.6    Cheng, X.7    Kahn, R.A.8
  • 36
    • 0033049656 scopus 로고    scopus 로고
    • Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors
    • Sata M., Moss J., and Vaughan M. Structural basis for the inhibitory effect of brefeldin A on guanine nucleotide-exchange proteins for ADP-ribosylation factors. Proc. Natl. Acad. Sci. 96 (1999) 2752-2757
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 2752-2757
    • Sata, M.1    Moss, J.2    Vaughan, M.3
  • 37
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain
    • Peyroche A., Antonny B., Robineau S., Acker J., Cherfils J., and Jackson C.L. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3 (1999) 275-285
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 38
    • 0034730123 scopus 로고    scopus 로고
    • Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain
    • Robineau S., Chabre M., and Antonny B. Binding site of brefeldin A at the interface between the small G protein ADP-ribosylation factor 1 (ARF1) and the nucleotide-exchange factor Sec7 domain. Proc. Natl. Acad. Sci. 97 (2000) 9913-9918
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 9913-9918
    • Robineau, S.1    Chabre, M.2    Antonny, B.3
  • 39
    • 9444274139 scopus 로고    scopus 로고
    • Big2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity
    • Shin H.W., Morinaga N., Noda M., and Nakayama K. Big2, a guanine nucleotide exchange factor for ADP-ribosylation factors: its localization to recycling endosomes and implication in the endosome integrity. Mol. Biol. Cell 15 (2004) 5283-5294
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5283-5294
    • Shin, H.W.1    Morinaga, N.2    Noda, M.3    Nakayama, K.4
  • 40
    • 0027500969 scopus 로고
    • SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER
    • Barlowe C., and Schekman R. SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature 365 (1993) 347-349
    • (1993) Nature , vol.365 , pp. 347-349
    • Barlowe, C.1    Schekman, R.2
  • 41
    • 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., and Vaughan M. Isolation of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP ribosylation factor (ARF) 1 and ARF3 that contains a Sec7-like domain. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 12856-12860
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12856-12860
    • Morinaga, N.1    Tsai, S.-C.2    Moss, J.3    Vaughan, M.4
  • 42
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: A Novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude A., Zhao B.-P., Kuziemsky C.E., Dahan S., Berger S.J., Yan J.-P., Armold A.D., Sullivan E.M., and Melangon P. GBF1: A Novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146 (1999) 71-84
    • (1999) J. Cell Biol. , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.-P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5    Yan, J.-P.6    Armold, A.D.7    Sullivan, E.M.8    Melangon, P.9
  • 43
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu T.K., Pfeifer A.C., Lippincott-Schwartz J., and Jackson C.L. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16 (2005) 1213-1222
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 44
    • 26244448510 scopus 로고    scopus 로고
    • Isoform-selective effects on the depletion of ADP-ribosylation factors 1-5 on membrane traffic
    • Volpicelli-Daley L.A., Li Y., Zhang C.-J., and Kahn R.A. Isoform-selective effects on the depletion of ADP-ribosylation factors 1-5 on membrane traffic. Mol. Biol. Cell 16 (2005) 4495-4508
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4495-4508
    • Volpicelli-Daley, L.A.1    Li, Y.2    Zhang, C.-J.3    Kahn, R.A.4
  • 45
    • 0029670289 scopus 로고    scopus 로고
    • Protein sorting by transport vesicles
    • Rothman J.E., and Wieland F.T. Protein sorting by transport vesicles. Science 272 (1996) 227-234
    • (1996) Science , vol.272 , pp. 227-234
    • Rothman, J.E.1    Wieland, F.T.2
  • 46
    • 0036007958 scopus 로고    scopus 로고
    • Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPl antisera
    • Ritzenthaler C., Nebenfuhr A., Movafeghi A., Stussi-Garaud C., Behnia L., Pimpl P., Staehelin L.A., and Robinson D.G. Reevaluation of the effects of brefeldin A on plant cells using tobacco Bright Yellow 2 cells expressing Golgi-targeted green fluorescent protein and COPl antisera. Plant Cell 14 (2002) 237-261
    • (2002) Plant Cell , vol.14 , pp. 237-261
    • Ritzenthaler, C.1    Nebenfuhr, A.2    Movafeghi, A.3    Stussi-Garaud, C.4    Behnia, L.5    Pimpl, P.6    Staehelin, L.A.7    Robinson, D.G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.