Student or educator? Sign up with your school email and get 6 months of Pro free.
Cited by 1,378

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

ARF proteins: roles in membrane traffic and beyond

D'Souza-Schorey, Crislyn, Chavrier, Philippe·2006·Nature Reviews Molecular Cell Biology

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1038/nrm1910

Cites

2 of 2 references verified0 citation errors · 0 not checkable

Statistics

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 2 references

Research works printed but not linked: 207

  1. Kahn, R. & Gilman, A. The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem. 261, 7906–7911 (1986). · DOI
  2. Jackson, C. L. & Casanova, J. E. Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell. Biol. 10, 60–67 (2000). · DOI
  3. Randazzo, P. A. & Hirsch, D. S. Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling. Cell Signal 16, 401–413 (2004). This review summarizes a series of studies on ARF-dependent and -independent activities of large multi-domain-ARF GAPs in the regulation of cell function. · DOI
  4. Amor, J. C., Harrison, D. H., Kahn, R. A. & Ringe, D. Structure of the human ADP-ribosylation factor 1 complexed with GDP. Nature 372, 704–708 (1994). · DOI
  5. Kahn, R. A. et al. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J. Cell Biol. 172, 645–650 (2006). Provides a complete and up-to-date nomenclature for the human members of the ARF family. · DOI
  6. Bonifacino, J. S. & Glick, B. S. The mechanisms of vesicle budding and fusion. Cell 116, 153–166 (2004). · DOI
  7. Claude, A. et al. GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146, 71–84 (1999).
  8. Takatsu, H., Yoshino, K., Toda, K. & Nakayama, K. GGA proteins associate with Golgi membranes through interaction between their GGAH domains and ADP-ribosylation factors. Biochem. J. 365, 369–378 (2002). · DOI
  9. D'Souza-Schorey, C., Li, G., Colombo, M. I. & Stahl, P. D. A regulatory role for ARF6 in receptor-mediated endocytosis. Science 267, 1175–1178 (1995). · DOI
  10. Peters, P. J. et al. Overexpression of wild-type and mutant ARF1 and ARF6: distinct perturbations of nonoverlapping membrane compartments. J. Cell Biol. 128, 1003–1017 (1995). · DOI
  11. Burd, C. G., Strochlic, T. I. & Gangi Setty, S. R. Arf-like GTPases: not so Arf-like after all. Trends Cell Biol. 14, 687–694 (2004). · DOI
  12. Kuge, O. et al. Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J. Cell Biol. 125, 51–65 (1994). · DOI
  13. Mueller, A. G., Joost, H. G. & Schurmann, A. Mouse ARF-related protein 1: genomic organization and analysis of its promoter. Biochem. Biophys. Res. Commun. 292, 113–120 (2002). · DOI
  14. Murtagh, J. J. Jr. et al. Guanine nucleotide-binding proteins in the intestinal parasite Giardia lamblia. Isolation of a gene encoding an approximately 20-kDa ADP-ribosylation factor. J. Biol. Chem. 267, 9654–9662 (1992). · DOI
  15. Li, Y. et al. Functional genomic analysis of the ADP-ribosylation factor family of GTPases: phylogeny among diverse eukaryotes and function in C. elegans. FASEB J. 18, 1834–1850 (2004). · DOI
  16. Pasqualato, S., Menetrey, J., Franco, M. & Cherfils, J. The structural GDP/GTP cycle of human Arf6. EMBO Rep. 2, 234–238 (2001). · DOI
  17. Shin, O. H., Couvillon, A. D. & Exton, J. H. Arfophilin is a common target of both class II and class III ADP-ribosylation factors. Biochemistry 40, 10846–10852 (2001). · DOI
  18. Shin, O. H. & Exton, J. H. Differential binding of arfaptin 2/POR1 to ADP-ribosylation factors and Rac1. Biochem. Biophys. Res. Commun. 285, 1267–1273 (2001). · DOI
  19. Kawasaki, M., Nakayama, K. & Wakatsuki, S. Membrane recruitment of effector proteins by Arf and Rab GTPases. Curr. Opin. Struct. Biol. 15, 681–689 (2005). · DOI
  20. Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C. & Sternweis, P. C. ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell 75, 1137–1144 (1993). · DOI
  21. Cockcroft, S. et al. Phospholipase D: a downstream effector of ARF in granulocytes. Science 263, 523–526 (1994). References 20 and 21 provide the first evidence that the catalytic activity of phospholipase D is stimulated by ARF proteins using permeabilized cells and cell-free assays. · DOI · Paper page
  22. Al-Awar, O., Radhakrishna, H., Powell, N. N. & Donaldson, J. G. Separation of membrane trafficking and actin remodeling functions of ARF6 with an effector domain mutant. Mol. Cell Biol. 20, 5998–6007 (2000). · DOI
  23. Stearns, T., Willingham, M. C., Botstein, D. & Kahn, R. A. ADP-ribosylation factor is functionally and physically associated with the Golgi complex. Proc. Natl Acad. Sci. USA 87, 1238–1242 (1990). · DOI
  24. Lee, M. C. S., Miller, E. A., Goldberg, J., Orci, L. & Schekman, R. Bi-directional protein transport between the ER and Golgi. Annu. Rev. Cell Dev. Biol. 20, 87–123 (2004). · DOI · Paper page
  25. Kirchhausen, T. Three ways to make a vesicle. Nature Rev. Mol. Cell Biol. 1, 187–198 (2000). · DOI · Paper page
  26. Bonifacino, J. S. The GGA proteins: adaptors on the move. Nature Rev. Mol. Cell Biol. 5, 23–32 (2004). · DOI · Paper page
  27. Spang, A., Matsuoka, K., Hamamoto, S., Schekman, R. & Orci, L. Coatomer, Arf1p, and nucleotide are required to bud coat protein complex I-coated vesicles from large synthetic liposomes. Proc. Natl Acad. Sci. USA 95, 11199–11204 (1998). Shows that ARF1–GTP and coatomer comprise the minimum apparatus necessary to create a COPI-coated vesicle. · DOI
  28. Bremser, M. et al. Coupling of coat assembly and vesicle budding to packaging of putative cargo receptors. Cell 96, 495–506 (1999). · DOI
  29. Cox, R., Mason-Gamer, R. J., Jackson, C. L. & Segev, N. Phylogenetic analysis of Sec7-domain-containing Arf nucleotide exchangers. Mol. Biol. Cell 15, 1487–1505 (2004). · DOI
  30. Kawamoto, K. et al. GBF1, a guanine nucleotide exchange factor for ADP-ribosylation factors, is localized to the cis-Golgi and involved in membrane association of the COPI coat. Traffic 3, 483–495 (2002). · DOI
  31. Shinotsuka, C., Waguri, S., Wakasugi, M., Uchiyama, Y. & Nakayama, K. Dominant-negative mutant of BIG2, an ARF-guanine nucleotide exchange factor, specifically affects membrane trafficking from the trans-Golgi network through inhibiting membrane association of AP-1 and GGA coat proteins. Biochem. Biophys. Res. Commun. 294, 254–260 (2002). · DOI
  32. Garcia-Mata, R., Szul, T., Alvarez, C. & Sztul, E. ADP-ribosylation factor/COPI-dependent events at the endoplasmic eeticulum-Golgi interface are regulated by the guanine nucleotide exchange factor GBF1. Mol. Biol. Cell 14, 2250–2261 (2003). · DOI
  33. Szul, T. et al. Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1. Traffic 6, 374–385 (2005). · DOI
  34. Yamaji, R. et al. Identification and localization of two brefeldin A-inhibited guanine nucleotide-exchange proteins for ADP-ribosylation factors in a macromolecular complex. Proc. Natl Acad. Sci. USA 97, 2567–2572 (2000). · DOI
  35. Zhao, X., Lasell, T. K. & Melancon, P. Localization of large ADP-ribosylation factor-guanine nucleotide exchange factors to different Golgi compartments: evidence for distinct functions in protein traffic. Mol. Biol. Cell 13, 119–133 (2002). · DOI
  36. Niu, T. -K., Pfeifer, A. C., Lippincott-Schwartz, J. & Jackson, C. L. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16, 1213–1222 (2005). · DOI
  37. Stamnes, M. A. et al. An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding. Proc. Natl Acad. Sci. USA 92, 8011–8015 (1995). · DOI
  38. Gommel, D. U. et al. Recruitment to Golgi membranes of ADP-ribosylation factor 1 is mediated by the cytoplasmic domain of p23. EMBO J. 20, 6751–6760 (2001). · DOI
  39. Majoul, I., Straub, M., Hell, S. W., Duden, R. & Soling, H. D. KDEL-cargo regulates interactions between proteins involved in COPI vesicle traffic: measurements in living cells using FRET. Dev. Cell 1, 139–153 (2001). · DOI
  40. Lee, S. Y., Yang, J. -S., Hong, W., Premont, R. T. & Hsu, V. W. ARFGAP1 plays a central role in coupling COPI cargo sorting with vesicle formation. J. Cell Biol. 168, 281–290 (2005). · DOI
  41. Honda, A., Al-Awar, O. S., Hay, J. C. & Donaldson, J. G. Targeting of Arf-1 to the early Golgi by membrin, an ER-Golgi SNARE. J. Cell Biol. 168, 1039–1051 (2005). · DOI
  42. Springer, S., Spang, A. & Schekman, R. A primer on vesicle budding. Cell 97, 145–148 (1999). · DOI · Paper page
  43. Tanigawa, G. et al. Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles. J. Cell Biol. 123, 1365–1371 (1993). · DOI
  44. Cukierman, E., Huber, I., Rotman, M. & Cassel, D. The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization. Science 270, 1999–2002 (1995). Cloning and the characterization of the first ARF1 GAP, ARFGAP1, and its recruitment to the Golgi complex. · DOI · Paper page
  45. Reinhard, C., Schweikert, M., Wieland, F. T. & Nickel, W. Functional reconstitution of COPI coat assembly and disassembly using chemically defined components. Proc. Natl Acad. Sci. USA 100, 8253–8257 (2003). · DOI
  46. Bigay, J., Gounon, P., Robineau, S. & Antonny, B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426, 563–566 (2003). Shows that increases in membrane curvature induce uncoating of COPI-coated vesicles, which is mediated by ARFGAP1 activity. This study proposes a model for COPI dynamics in which GTP hydrolysis in ARF1 is organized temporally and spatially according to the changes in lipid packing that are induced by the coat. · DOI
  47. Nickel, W. et al. Uptake by COPI-coated vesicles of both anterograde and retrograde cargo is inhibited by GTPgS in vitro. J. Cell. Sci. 111, 3081–3090 (1998). · DOI
  48. Malsam, J., Gommel, D., Wieland, F. T. & Nickel, W. A role for ADP ribosylation factor in the control of cargo uptake during COPI-coated vesicle biogenesis. FEBS Lett. 462, 267–372 (1999). · DOI
  49. Lanoix, J. et al. GTP hydrolysis by arf-1 mediates sorting and concentration of Golgi resident enzymes into functional COP I vesicles. EMBO J. 18, 4935–4948 (1999). · DOI
  50. Pepperkok, R., Whitney, J. A., Gomez, M. & Kreis, T. E. COPI vesicles accumulating in the presence of a GTP restricted arf1 mutant are depleted of anterograde and retrograde cargo. J. Cell. Sci. 113, 135–144 (2000). · DOI
  51. Yang, J. -S. et al. ARFGAP1 promotes the formation of COPI vesicles, suggesting function as a component of the coat. J. Cell Biol. 159, 69–78 (2002). · DOI
  52. Lanoix, J. et al. Sorting of Golgi resident proteins into different subpopulations of COPI vesicles: a role for ArfGAP1. J. Cell Biol. 155, 1199–1212 (2001). · DOI
  53. Elsner, M. et al. Spatiotemporal dynamics of the COPI vesicle machinery. EMBO Rep. 4, 1000–1004 (2003). · DOI
  54. Liu, W., Duden, R., Phair, R. D. & Lippincott-Schwartz, J. ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cells. J. Cell Biol. 168, 1053–1063 (2005). · DOI
  55. Aoe, T. et al. The KDEL receptor, ERD2, regulates intracellular traffic by recruiting a GTPase-activating protein for ARF1. EMBO J. 16, 7305–7316 (1997). · DOI
  56. Goldberg, J. Decoding of sorting signals by coatomer through a GTPase switch in the COPI coat complex. Cell 100, 671–679 (2000). · DOI
  57. Rein, U., Andag, U., Duden, R., Schmitt, H. D. & Spang, A. ARF-GAP-mediated interaction between the ER–Golgi v-SNAREs and the COPI coat. J. Cell Biol. 157, 395–404 (2002). · DOI
  58. Goldberg, J. Structural and functional analysis of the ARF1–ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96, 893–902 (1999). · DOI
  59. Bigay, J., Casella, J. F., Drin, G., Mesmin, B. & Antonny, B. ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. EMBO J. 24, 2244–2253 (2005). · DOI
  60. Presley, J. F. et al. Dissection of COPI and Arf1 dynamics in vivo and role in Golgi membrane transport. Nature 417, 187–193 (2002). · DOI
  61. Stamnes, M. A. & Rothman, J. E. The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73, 999–1005 (1993). · DOI · Paper page
  62. Traub, L. M., Ostrom, J. A. & Kornfeld, S. Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123, 561–573 (1993). · DOI · Paper page
  63. Ooi, C. E., Dell'Angelica, E. C. & Bonifacino, J. S. ADP-Ribosylation Factor 1 (ARF1) Regulates Recruitment of the AP-3 Adaptor Complex to Membranes. J. Cell Biol. 142, 391–402 (1998). · DOI
  64. Boehm, M., Aguilar, R. C. & Bonifacino, J. S. Functional and physical interactions of the adaptor protein complex AP-4 with ADP-ribosylation factors (ARFs). EMBO. J. 20, 6265–6276 (2001). · DOI
  65. Zhu, Y., Drake, M. T. & Kornfeld, S. ADP-ribosylation factor 1 dependent clathrin-coat assembly on synthetic liposomes. Proc. Natl Acad. Sci. USA 96, 5013–5018 (1999). · DOI
  66. Crottet, P., Meyer, D. M., Rohrer, J. & Spiess, M. ARF1:GTP, yyrosine-based signals, and phosphatidylinositol 4, 5-bisphosphate constitute a minimal machinery to recruit the AP-1 clathrin adaptor to membranes. Mol. Biol. Cell 13, 3672–3682 (2002). · DOI
  67. Drake, M. T., Zhu, Y. & Kornfeld, S. The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes. Mol. Biol. Cell 11, 3723–3736 (2000). · DOI
  68. Austin, C., Boehm, M. & Tooze, S. A. Site-specific cross-linking reveals a differential direct interaction of class 1, 2, and 3 ADP-ribosylation factors with adaptor protein complexes 1 and 3. Biochemistry 41, 4669–4677 (2002). · DOI
  69. Wang, Y. J. et al. Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. Cell 114, 299–310 (2003). · DOI
  70. De Matteis, M. A. & Godi, A. PI-loting membrane traffic. Nature Cell. Biol. 6, 487–492 (2004). · DOI
  71. Collins, B. M., Watson, P. J. & Owen, D. J. The structure of the GGA1-GAT domain reveals the molecular basis for ARF binding and membrane association of GGAs. Dev. Cell 4, 321–332 (2003). · DOI
  72. Shiba, T. et al. Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport. Nature Struct. Biol. 10, 386–393 (2003). · DOI
  73. Shinotsuka, C., Yoshida, Y., Kawamoto, K., Takatsu, H. & Nakayama, K. Overexpression of an ADP-ribosylation factor-guanine nucleotide exchange factor, BIG2, uncouples brefeldin A-induced adaptor protein-1 coat dissociation and membrane tubulation. J. Biol. Chem. 277, 9468–9473 (2002). · DOI
  74. Shin, H. -W., Morinaga, N., Noda, M. & 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, 5283–5294 (2004). · DOI
  75. Zhu, Y., Traub, L. M. & Kornfeld, S. ADP-ribosylation factor 1 transiently activates high-Affinity adaptor protein complex AP-1 binding sites on Golgi membranes. Mol. Biol. Cell 9, 1323–1337 (1998). · DOI
  76. Hirst, J., Motley, A., Harasaki, K., Peak Chew, S. Y. & Robinson, M. S. EpsinR: an ENTH domain-containing protein that interacts with AP-1. Mol. Biol. Cell 14, 625–641 (2003). · DOI
  77. Meyer, D. M. et al. Oligomerization and dissociation of AP-1 adaptors are regulated by cargo signals and by ArfGAP1-induced GTP hydrolysis. Mol. Biol. Cell 16, 4745–4754 (2005). · DOI
  78. Nie, Z. et al. Specific regulation of the adaptor protein complex AP-3 by the Arf GAP AGAP1. Dev Cell 5, 513–521 (2003). · DOI
  79. Nie, Z., Fei, J., Premont, R. T. & Randazzo, P. A. The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3. J. Cell. Sci. 118, 3555–3566 (2005). · DOI
  80. Stamnes, M. Regulating the actin cytoskeleton during vesicular transport. Curr. Opin. Cell. Biol. 14, 428–433 (2002). · DOI
  81. Valderrama, F. et al. Actin microfilaments facilitate the retrograde transport from the Golgi complex to the endoplasmic reticulum in mammalian cells. Traffic 2, 717–726 (2001). · DOI
  82. Percival, J. M. et al. Targeting of a tropomyosin isoform to short microfilaments associated with the Golgi complex. Mol. Biol. Cell 15, 268–280 (2004). · DOI
  83. Godi, A. et al. ADP ribosylation factor regulates spectrin binding to the Golgi complex. Proc. Natl Acad. Sci. USA 95, 8607–8612 (1998). · DOI
  84. Fucini, R. V. et al. Activated ADP-ribosylation factor assembles distinct pools of actin on Golgi membranes. J. Biol. Chem. 275, 18824–18829 (2000). The first demonstration that activation of ARF1 stimulates actin-filament assembly on Golgi membranes. This study indicates that regulation of the actin-based cytoskeleton might have an important role during ARF-mediated transport vesicle assembly or release on the Golgi. · DOI
  85. Fucini, R. V., Chen, J. L., Sharma, C., Kessels, M. M. & Stamnes, M. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1. Mol. Biol. Cell. 13, 621–631 (2002). · DOI
  86. Godi, A. et al. ARF mediates recruitment of PtdIns-4-OH kinase-β and stimulates synthesis of PtdIns(4,5)P2 on the Golgi complex. Nature Cell. Biol. 1, 280–287 (1999). Shows that ARF1 regulates cellular levels of PI(4,5)P 2 by controlling the recruitment and activity of phosphatidylinositol-4-phosphate kinase on Golgi membranes. · DOI
  87. Jones, D. H. et al. Type I phosphatidylinositol 4-phosphate 5-kinase directly interacts with ADP-ribosylation factor 1 and is responsible for phosphatidylinositol 4,5-bisphosphate synthesis in the golgi compartment. J. Biol. Chem. 275, 13962–13966 (2000). · DOI
  88. Beck, K. A. Spectrins and the Golgi. Biochim. Biophys. Acta 1744, 374–382 (2005). · DOI
  89. Luna, A. et al. Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol. Biol. Cell 13, 866–879 (2002). · DOI
  90. Chen, J. L., Lacomis, L., Erdjument-Bromage, H., Tempst, P. & Stamnes, M. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes. FEBS. Lett. 566, 281–286 (2004). · DOI
  91. Matas, O. B., Martinez-Menarguez, J. A. & Egea, G. Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 5, 838–846 (2004). · DOI
  92. Wu, W. J., Erickson, J. W., Lin, R. & Cerione, R. A. The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 405, 800–804 (2000). · DOI
  93. Erickson, J. W., Zhang, C. -J., Kahn, R. A., Evans, T. & Cerione, R. A. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J. Biol. Chem. 271, 26850–26854 (1996). · DOI
  94. Kroschewski, R., Hall, A. & Mellman, I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nature Cell Biol. 1, 8–13 (1999). · DOI
  95. Musch, A., Cohen, D., Kreitzer, G. & Rodriguez-Boulan, E. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J. 20, 2171–2179 (2001). · DOI
  96. Dubois, T. et al. Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. Nature Cell Biol. 7, 353–364 (2005). · DOI
  97. Cao, H. et al. Actin and Arf1-dependent recruitment of a cortactin–dynamin complex to the Golgi regulates post-Golgi transport. Nature Cell Biol. 7, 483–492 (2005). · DOI · Paper page
  98. Carreno, S., Engqvist-Goldstein, A. E., Zhang, C. X., McDonald, K. L. & Drubin, D. G. Actin dynamics coupled to clathrin-coated vesicle formation at the trans-Golgi network. J. Cell Biol. 165, 781–788 (2004). · DOI · Paper page
  99. Garcia-Mata, R. & Sztul, E. The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. EMBO Rep. 4, 320–325 (2003). · DOI
  100. Volpicelli-Daley, L. A., Li, Y., Zhang, C. -J. & Kahn, R. A. Isoform-selective effects of the depletion of ADP-ribosylation factors 1–5 on membrane traffic. Mol. Biol. Cell 16, 4495–4508 (2005). Shows that every combination of the double knock-downs of ARF1, ARF3, ARF4, and ARF5 yielded a distinct pattern of defects on membrane traffic. This study indicates that the cooperation of two ARF proteins at the same site might be a general feature of ARF signalling. · DOI
  101. Honda, A. et al. Phosphatidylinositol 4-phosphate 5-kinase α is a downstream effector of the small G protein ARF6 in membrane ruffle formation. Cell 99, 521–532 (1999). Showed that ARF6 regulates levels of PI(4,5)P 2 at the cell surface by controlling the recruitment and activity of PIP5K Type Iα at sites of membrane ruffling. · DOI
  102. Krauss, M. et al. ARF6 stimulates clathrin/AP-2 recruitment to synaptic membranes by activating phosphatidylinositol phosphate kinase type Iγ. J Cell Biol 162, 113–124 (2003). · DOI
  103. Martin, T. F. PI(4,5)P2 regulation of surface membrane traffic. Curr. Opin. Cell. Biol. 13, 493–499 (2001). · DOI
  104. Wenk, M. R. & De Camilli, P. Protein-lipid interactions and phosphoinositide metabolism in membrane traffic: Insights from vesicle recycling in nerve terminals. Proc. Natl Acad. Sci. USA 101, 8262–8269 (2004). · DOI
  105. Paleotti, O. et al. The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes. J Biol Chem 280, 21661–21666 (2005). · DOI
  106. Tanabe, K. et al. A novel GTPase-activating protein for ARF6 directly interacts with clathrin and regulates clathrin-dependent endocytosis. Mol. Biol. Cell 16, 1617–1628 (2005). · DOI
  107. Altschuler, Y. et al. ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells. J. Cell. Biol. 147, 7–12 (1999). · DOI
  108. Hyman, T., Shmuel, M. & Altschuler, Y. Actin is required for endocytosis at the apical surface of MDCK cells where ARF6 and clathrin regulate the actin cytoskeleton. Mol. Biol. Cell. 17, 427–437 (2005). · DOI
  109. Palacios, F., Price, L., Schweitzer, J., Collard, J. G. & D'Souza-Schorey, C. An essential role for ARF6-regulated membrane traffic in adherens junction turnover and epithelial cell migration. EMBO J. 20, 4973–4986 (2001). References 109 and 110 show that the ARF6-GTPase cycle regulates the trafficking of E-cadherin along the endocytic pathway and the formation of membrane ruffles. References 109 and 147 show that ARF6 activation occurs downstream of HGF signalling to promote epithelial cell migration. · DOI
  110. Palacios, F., Schweitzer, J. K., Boshans, R. L. & D'Souza-Schorey, C. ARF6–GTP recruits Nm23-H1 to facilitate dynamin-mediated endocytosis during adherens junctions disassembly. Nature Cell Biol. 4, 929–936 (2002). · DOI
  111. Krishnan, K. S. et al. Nucleoside diphosphate kinase, a source of GTP, is required for dynamin-dependent synaptic vesicle recycling. Neuron 30, 197–210 (2001). · DOI
  112. Claing, A. et al. β-arrestin-mediated ADP-ribosylation factor 6 activation and β2-adrenergic receptor endocytosis. J. Biol. Chem. 276, 42509–42513 (2001). · DOI
  113. Mukherjee, S. et al. The ADP ribosylation factor nucleotide exchange factor ARNO promotes β-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization. Proc. Natl Acad. Sci. USA 97, 5901–5906 (2000). · DOI
  114. Ikeda, S. et al. Novel role of ARF6 in vascular endothelial growth factor-induced signaling and angiogenesis. Circ. Res. 96, 467–475 (2005). · DOI
  115. Xu, L. et al. Elevated phospholipase D activity in H-Ras- but not K-Ras-transformed cells by the synergistic action of RalA and ARF6. Mol. Cell. Biol. 23, 645–654 (2003). · DOI
  116. Donaldson, J. G. Multiple roles for Arf6: Sorting, structuring, and signaling at the plasma membrane. J. Biol. Chem. 278, 41573–41576 (2003). · DOI · Paper page
  117. Blagoveshchenskaya, A. D., Thomas, L., Feliciangeli, S. F., Hung, C. H. & Thomas, G. HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway. Cell 111, 853–866 (2002). · DOI
  118. Naslavsky, N., Weigert, R. & Donaldson, J. G. Convergence of non-clathrin- and clathrin-derived endosomes involves Arf6 inactivation and changes in phosphoinositides. Mol. Biol. Cell 14, 417–431 (2003). · DOI
  119. Brown, F. D., Rozelle, A. L., Yin, H. L., Balla, T. & Donaldson, J. G. Phosphatidylinositol 4, 5-bisphosphate and Arf6-regulated membrane traffic. J. Cell Biol. 154, 1007–1017 (2001). · DOI · Paper page
  120. Arnaoutova, I., Jackson, C. L., Al-Awar, O. S., Donaldson, J. G. & Loh, Y. P. Recycling of Raft-associated prohormone sorting receptor carboxypeptidase E requires interaction with ARF6. Mol. Biol. Cell 14, 4448–44457 (2003). · DOI
  121. Houndolo, T., Boulay, P. -L. & Claing, A. G protein-coupled receptor endocytosis in ADP-ribosylation factor 6-depleted cells. J. Biol. Chem. 280, 5598–5604 (2005). · DOI
  122. Maxfield, F. R. & McGraw, T. E. Endocytic recycling. Nature Rev. Mol. Cell. Biol. 5, 121–132 (2004). · DOI · Paper page
  123. D'Souza-Schorey, C. et al. ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation. J. Cell Biol. 140, 603–616 (1998). · DOI
  124. Franco, M. et al. EFA6, a sec7 domain-containing exchange factor for ARF6, coordinates membrane recycling and actin cytoskeleton organization. EMBO J. 18, 1480–1491 (1999). Cloning and characterization of the first member of the EFA6 family of ARF6 GEFS. · DOI
  125. Padron, D., Tall, R. D. & Roth, M. G. PLD2 is required for efficient endocytic recycling of transferrin receptors. Mol. Biol. Cell 17, 598–606 (2005). · DOI
  126. Mayor, S., Presley, J. & Maxfield, F. Sorting of membrane components from endosomes and subsequent recycling to the cell surface occurs by a bulk flow process. J. Cell Biol. 121, 1257–1269 (1993). · DOI · Paper page
  127. Radhakrishna, H. & Donaldson, J. G. ADP-ribosylation factor 6 regulates a novel plasma membrane recycling pathway. J. Cell Biol. 139, 49–61 (1997). Shows that ARF6 regulates the recycling of plasma-membrane proteins that lack AP-2 and clathrin-sorting signals through a unique endosomal trafficking pathway. · DOI · Paper page
  128. Caplan, S. et al. A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane. EMBO J. 21, 2557–2567 (2002). · DOI · Paper page
  129. Weigert, R., Yeung, A. C., Li, J. & Donaldson, J. G. Rab22a regulates the recycling of membrane proteins internalized independently of clathrin. Mol. Biol. Cell. 15, 3758–3770 (2004). · DOI
  130. Jovanovic, O. A., Brown, F. D. & Donaldson, J. G. An effector domain mutant of Arf6 implicates phospholipase D in endosomal membrane recycling. Mol. Biol. Cell 17, 327–335 (2006). · DOI
  131. Martinu, L. et al. The TBC (Tre-2/Bub2/Cdc16) domain protein TRE17 regulates plasma membrane-endosomal trafficking through activation of Arf6. Mol. Cell. Biol. 24, 9752–9762 (2004). · DOI
  132. Powelka, A. M. et al. Stimulation-dependent recycling of integrin β1 regulated by ARF6 and Rab11. Traffic 5, 20–36 (2004). · DOI
  133. Aikawa, Y. & Martin, T. F. ARF6 regulates a plasma membrane pool of phosphatidylinositol(4, 5)bisphosphate required for regulated exocytosis. J. Cell Biol. 162, 647–659 (2003). · DOI
  134. Prigent, M. et al. ARF6 controls post-endocytic recycling through its downstream exocyst complex effector. J. Cell Biol. 163, 1111–1121 (2003). · DOI
  135. Jackson, T. R. et al. ACAPs are arf6 GTPase-activating proteins that function in the cell periphery. J. Cell Biol. 151, 627–638 (2000). · DOI
  136. Dai, J. et al. ACAP1 promotes endocytic recycling by recognizing recycling sorting signals. Dev. Cell 7, 771–776 (2004). · DOI
  137. Li, J. et al. Phosphorylation of ACAP1 by Akt regulates the stimulation-dependent recycling of integrin β1 to control cell migration. Dev. Cell 9, 663–673 (2005). Shows that the ARF6 GAP ACAP1 regulates the endosomal recycling of β1 integrin. In contrast to its effect on transferrin receptor recycling (Ref. 136), the role of ACAP1 in β1 integrin recycling requires its phosphorylation by AKT/PKB which is regulated by a canonical signalling pathway. · DOI
  138. Caumont, A. S. et al. Identification of a plasma membrane-associated guanine nucleotide exchange factor for ARF6 in chromaffin cells. Possible role in the regulated exocytotic pathway. J. Biol. Chem. 275, 15637–15644 (2000). · DOI
  139. Vitale, N. et al. The small GTPase RalA controls exocytosis of large dense core secretory granules by interacting with ARF6-dependent phospholipase D1. J. Biol. Chem. 280, 29921–29928 (2005). · DOI
  140. Liu, L. et al. SCAMP2 interacts with Arf6 and phospholipase D1 and links their function to exocytotic fusion pore formation in PC12 cells. Mol. Biol. Cell 16, 4463–4472 (2005). · DOI
  141. Radhakrishna, H., Klausner, R. D. & Donaldson, J. G. Aluminum fluoride stimulates surface protrusions in cells overexpressing the ARF6 GTPase. J. Cell Biol. 134, 935–947 (1996). Showed that ARF6 activation at the cell surface is accompanied by the formation of actin-rich membrane protrusions. · DOI
  142. D'Souza-Schorey, C., Boshans, R. L., McDonough, M., Stahl, P. D. & Van Aelst, L. A role for POR1, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. EMBO J. 16, 5445–5454 (1997). · DOI
  143. Schafer, D. A., D'Souza-Schorey, C. & Cooper, J. A. Actin assembly at membranes controlled by ARF6. Traffic 1, 896–907 (2000). · DOI
  144. Albertinazzi, C., Za, L., Paris, S. & de Curtis, I. ADP-ribosylation factor 6 and a functional PIX–p95-APP1 complex are required for Rac1B-mediated neurite outgrowth. Mol. Biol. Cell 14, 1295–307 (2003). · DOI
  145. Hernandez-Deviez, D. J., Roth, M. G., Casanova, J. E. & Wilson, J. M. ARNO and ARF6 regulate axonal elongation and branching through downstream activation of phosphatidylinositol 4-phosphate 5-kinase α. Mol. Biol. Cell. 15, 111–120 (2004). · DOI
  146. Santy, L. C. & 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, 599–610 (2001). Showed that ARF6 activation by ARNO stimulates two distinct signalling pathways; one that results in Rac activation, and a second one that leads to changes in membrane phospholipid composition. Both pathways were shown to be required for cell motility. · DOI
  147. Riley, K. N., Maldonado, A. E., Tellier, P., D'Souza-Schorey, C. & Herman, I. M. βcap73-ARF6 interactions modulate cell shape and motility after injury in vitro. Mol. Biol. Cell 14, 4155–4161 (2003). · DOI
  148. Zhang, Q., Cox, D., Tseng, C. C., Donaldson, J. G. & Greenberg, S. A requirement for ARF6 in Fcγ receptor-mediated phagocytosis in macrophages. J. Biol Chem. 273, 19977–19981 (1998). · DOI
  149. Niedergang, F., Colucci-Guyon, E., Dubois, T., Raposo, G. & Chavrier, P. ADP ribosylation factor 6 is activated and controls membrane delivery during phagocytosis in macrophages. J. Cell Biol. 161, 1143–1150 (2003). · DOI
  150. Wong, K. W. & Isberg, R. R. Arf6 and phosphoinositol-4-phosphate-5-kinase activities permit bypass of the Rac1 requirement for β1 integrin-mediated bacterial uptake. J. Exp. Med. 198, 603–614 (2003). · DOI
  151. Radhakrishna, H., Al-Awar, O., Khachikian, Z. & Donaldson, J. G. ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J. Cell. Sci. 112, 855–866 (1999). · DOI
  152. Boshans, R. L., Szanto, S., van Aelst, L. & D'Souza-Schorey, C. ADP-ribosylation factor 6 regulates actin cytoskeleton remodeling in coordination with Rac1 and RhoA. Mol. Cell. Biol. 20, 3685–3694 (2000). · DOI
  153. Santy, L. C., Ravichandran, K. S. & Casanova, J. E. The DOCK180/Elmo complex couples ARNO-mediated Arf6 activation to the downstream activation of Rac1. Curr. Biol. 15, 1749–1754 (2005). · DOI
  154. Peters, P. J. et al. Arfaptin 2 regulates the aggregation of mutant huntingtin protein. Nature Cell. Biol. 4, 240–245 (2002). · DOI
  155. Rangone, H. et al. Phosphorylation of arfaptin 2 at Ser260 by Akt Inhibits PolyQ-huntingtin-induced toxicity by rescuing proteasome impairment. J. Biol Chem. 280, 22021–22028 (2005). · DOI
  156. Doye, A. et al. CNF1 exploits the ubiquitin-proteasome machinery to restrict Rho GTPase activation for bacterial host cell invasion. Cell 111, 553–564 (2002). · DOI · Paper page
  157. Wang, H. R. et al. Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302, 1775–1779 (2003). · DOI · Paper page
  158. Palacios, F. & D'Souza-Schorey, C. Modulation of Rac1 and ARF6 activation during epithelial cell scattering. J. Biol Chem. 278, 17395–17400 (2003). · DOI
  159. Otsuki, Y. et al. Tumor metastasis suppressor nm23H1 regulates Rac1 GTPase by interaction with Tiam1. Proc. Natl Acad. Sci. USA 98, 4385–4390 (2001). · DOI
  160. Hilpela, P., Vartiainen, M. K. & Lappalainen, P. Regulation of the actin cytoskeleton by PI(4,5)P2 and PI(3,4,5)P3. Curr. Opin. Microbiol. Immunol. 282, 117–163 (2004).
  161. Niedergang, F. & Chavrier, P. Signaling and membrane dynamics during phagocytosis: many roads lead to the phagos(R)ome. Curr. Opin. Cell. Biol. 16, 422–428 (2004). · DOI
  162. Uchida, H., Kondo, A., Yoshimura, Y., Mazaki, Y. & Sabe, H. PAG3/Papα/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcγ receptor-mediated phagocytosis of macrophages. J. Exp. Med. 193, 955–966 (2001). · DOI
  163. Chen, E. H., Pryce, B. A., Tzeng, J. A., Gonzalez, G. A. & Olson, E. N. Control of myoblast fusion by a guanine nucleotide exchange factor, loner, and its effector ARF6. Cell 114, 751–762 (2003). · DOI
  164. D'Souza-Schorey, C. Disassembling adherens junctions: breaking up is hard to do. Trends Cell. Biol. 15, 19–26 (2005). · DOI
  165. Zimmermann, P. et al. Syndecan recyling is controlled by syntenin–PIP2 interaction and Arf6. Dev. Cell 9, 377–388 (2005). · DOI
  166. Buccione, R., Orth, J. D. & McNiven, M. A. Foot and mouth: podosomes, invadopodia and circular dorsal ruffles. Nature Rev. Mol. Cell. Biol. 5, 647–557 (2004). · DOI · Paper page
  167. Tague, S. E., Muralidharan, V. & D'Souza-Schorey, C. ADP-ribosylation factor 6 regulates tumor cell invasion through the activation of the MEK–ERK signaling pathway. Proc. Natl Acad. Sci. USA 101, 9671–9676 (2004). · DOI
  168. Hashimoto, S. et al. Requirement for Arf6 in breast cancer invasive activities. Proc. Natl Acad. Sci. USA 101, 6647–6652 (2004). · DOI
  169. Schweitzer, J. K. & D'Souza-Schorey, C. Localization and activation of the ARF6 GTPase during cleavage furrow ingression and cytokinesis. J. Biol. Chem. 277, 27210–27216 (2002). · DOI
  170. Schweitzer, J. K. & D'Souza-Schorey, C. A requirement for ARF6 during the completion of cytokinesis. Exp. Cell. Res. 311, 74–83 (2005). · DOI
  171. Schweitzer, J. K., Burke, E. E., Goodson, H. V. & D'Souza-Schorey, C. Endocytosis resumes during late mitosis and is required for cytokinesis. J. Biol. Chem. 280, 41628–41635 (2005). · DOI
  172. Fielding, A. B. et al. Rab11-FIP3 and FIP4 interact with Arf6 and the Exocyst to control membrane traffic in cytokinesis. EMBO J. 24, 3389–3399 (2005). · DOI
  173. Rothman, J. E. & Wieland, F. T. Protein sorting by transport vesicles. Science 272, 227–234 (1996). · DOI · Paper page
  174. Pelham, H. R. & Rothman, J. E. The debate about transport in the Golgi — two sides of the same coin? Cell 102, 713–719 (2000). · DOI
  175. Owen, D. J., Collins, B. M. & Evans, P. R. Adaptors for clathrin coats: structure and function. Annu. Rev. Cell. Dev. Biol. 20, 153–191 (2004). · DOI
  176. Pasqualato, S., Renault, L. & 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, 1035–1041 (2002). · DOI
  177. Morinaga, N., Tsai, S. C., Moss, J. & 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. USA 93, 12856–12860 (1996). · DOI
  178. Saeki, N., Tokuo, H. & Ikebe, M. BIG1 is a binding partner of myosin IXb and regulates its Rho-GTPase activating protein activity. J. Biol. Chem. 280, 10128–10134 (2005). · DOI
  179. Padilla, P. I. et al. Interaction of FK506-binding protein 13 with brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1): effects of FK506. Proc. Natl Acad. Sci. USA 100, 2322–2327 (2003). · DOI
  180. Li, H., Adamik, R., Pacheco-Rodriguez, G., Moss, J. & Vaughan, M. Protein kinase A-anchoring (AKAP) domains in brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BIG2). Proc. Natl. Acad. Sci. USA 100, 1627–1632 (2003). · DOI
  181. Xu, K. -F. et al. Interaction of BIG2, a brefeldin A-inhibited guanine nucleotide-exchange protein, with exocyst protein Exo70. Proc. Natl Acad. Sci USA 102, 2784–2789 (2005). · DOI
  182. Kolanus, W. et al. αL β2 integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule. Cell 86, 233–242 (1996). · DOI
  183. Pacheco-Rodriguez, G., Meacci, E., Vitale, N., Moss, J. & Vaughan, M. Guanine nucleotide exchange on ADP-ribosylation factors catalyzed by cytohesin-1 and its Sec7 domain. J. Biol. Chem. 273, 26543–265438 (1998). · DOI
  184. Ashery, U., Koch, H., Scheuss, V., Brose, N. & Rettig, J. A presynaptic role for the ADP ribosylation factor (ARF)-specific GDP/GTP exchange factor msec7–1. Proc. Natl Acad. Sci. USA 96, 1094–1099 (1999). · DOI
  185. Schurmann, A. et al. The ADP-ribosylation factor (ARF)-related GTPase ARF-related protein binds to the ARF-specific guanine nucleotide exchange factor cytohesin and inhibits the ARF-dependent activation of phospholipase D. J. Biol. Chem. 274, 9744–9751 (1999). · DOI
  186. Vitale, N. et al. Specific Functional Interaction of Human Cytohesin-1 and ADP-ribosylation Factor Domain Protein (ARD1). J. Biol. Chem. 275, 21331–21339 (2000). · DOI
  187. Mansour, M., Lee, S. Y. & Pohajdak, B. The N-terminal coiled coil domain of the cytohesin/ARNO family of guanine nucleotide exchange factors interacts with the scaffolding protein CASP. J. Biol. Chem. 277, 32302–32309 (2002). · DOI
  188. Chardin, P. et al. A human exchange factor for ARF contains Sec7- and pleckstrin-homology domains. Nature 384, 481–484 (1996). Cloning and characterization of the first member of the ARNO family of ARF GEFs. The study also identified the Sec7 catalytic domain in ARNO, which is common in all ARF GEFs and is essential for catalytic activity. · DOI
  189. Frank, S., Upender, S., Hansen, S. H. & Casanova, J. E. ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6. J. Biol. Chem. 273, 23–27 (1998). · DOI
  190. Frank, S. R., Hatfield, J. C. & Casanova, J. E. Remodeling of the actin cytoskeleton is coordinately regulated by protein kinase C and the ADP-ribosylation factor nucleotide exchange factor ARNO. Mol. Biol. Cell. 9, 3133–3146 (1998). · DOI
  191. Kitano, J. et al. Tamalin, a PDZ domain-containing protein, links a protein complex formation of group 1 metabotropic glutamate receptors and the guanine nucleotide exchange factor cytohesins. J. Neurosci. 22, 1280–1289 (2002). · DOI
  192. Hernandez-Deviez, D. J., Casanova, J. E. & Wilson, J. M. Regulation of dendritic development by the ARF exchange factor ARNO. Nature Neurosci. 5, 623–624 (2002). · DOI
  193. Venkateswarlu, K. Interaction protein for cytohesin exchange factors 1 (IPCEF1) binds cytohesin 2 and modifies its activity. J. Biol. Chem. 278, 43460–43469 (2003). · DOI
  194. Gsandtner, I. et al. Heterotrimeric G protein-independent signaling of a G protein-coupled receptor. Direct binding of ARNO–cytohesin-2 to the carboxyl terminus of the A2A adenosine receptor is necessary for sustained activation of the ERK–MAP kinase pathway. J. Biol. Chem. 280, 31898–31905 (2005). · DOI
  195. Hurtado-Lorenzo, A. et al. V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway. Nature Cell Biol. 8, 124–136 (2006). · DOI
  196. Franco, M. et al. ARNO3, a Sec7-domain guanine nucleotide exchange factor for ADP ribosylation factor 1, is involved in the control of Golgi structure and function. Proc. Natl Acad. Sci. USA 95, 9926–9931 (1998). · DOI
  197. Langille, S. E. et al. ADP-ribosylation factor 6 as a target of guanine nucleotide exchange factor GRP1. J. Biol. Chem. 274, 27099–27104 (1999). · DOI
  198. Nevrivy, D. J. et al. Interaction of grasp, a protein encoded by a novel retinoic acid-induced gene, with members of the cytohesin family of guanine nucleotide exchange factors. J. Biol. Chem. 275, 16827–16836 (2000). · DOI
  199. Klarlund, J. K. et al. Signaling complexes of the ferm domain-containing protein GRSP1 bound to ARF exchange factor GRP1. J. Biol. Chem. 276, 40065–40070 (2001). · DOI
  200. Poirier, M. -B. et al. General receptor for phosphoinositides 1, a novel repressor of thyroid hormone receptor action that prevents deoxyribonucleic acid binding. Mol. Endocrinol. 19, 1991–2005 (2005). · DOI

200 of 207 shown

Cited by

See all 1,378

Metadata

Authors
D'Souza-Schorey, C., & Chavrier, P.
Venue
Nature Reviews Molecular Cell Biology
Published
2006-05
Volume
7
Issue
5
Pages
347-358
ISSN
  • 1471-0072 (ISSN-L)
  • 1471-0080
OpenAlex
W2068358300
Cited by
1,378
References
2
FWCI
4.80
Type
journal article
Language
en
Open access
closed

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

How to cite

Cite CoChat for the checks on this page, and the paper for its own findings.

This page
CoChat. (2026). Citation check: ARF proteins: roles in membrane traffic and beyond. https://app.cochat.ai/papers/10.1038/nrm1910
The paper
D'Souza-Schorey, C., & Chavrier, P. (2006). ARF proteins: roles in membrane traffic and beyond. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm1910

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.