Skip to main content
SpringerLink
Log in
Book cover

ARF Family GTPases pp 325–350Cite as

Arf-Like Proteins

  • Chapter

  • 146 Accesses

Part of the book series: Proteins and Cell Regulation ((PROR,volume 1))

Abstract

At least 10 different proteins have homology to members of the Arf family but each lacks activities that define “true” Arfs. In addition, the percent identity between these 10 proteins, when aligned with Arfs or to each other, is lower (typically 40–60%) than that between Arfs (greater than 65% identity). A summary of current information on each is presented below. Despite extensive conservation of structure between Arfs and Arls, the Arls represent a much more functionally divergent collection of GTPases, with apparent roles in vesicle traffic (Arl1, Sarl), microtubule organization (Arl2, Arl3), spermatogenesis (Arl4), and differentiation (Arfrp1). However, the overlap in binding partners between functionally distinct Arls suggests that Arfs and Arls are likely to have a complex web of overlapping and distinct functions.

This is a preview of subscription content, log in via an institution.

Chapter
USD   29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD   129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD   169.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD   169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Learn about institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Allan, B. B., Moyer, B. D., and Balch, W. E. (2000). Rab1 recruitment of p115 into a cis-SNARE complex: programming budding COP-II vesicles for fusion. Science, 289, 444–448.

    Article  CAS  PubMed  Google Scholar 

  • Amor, J. C., Horton, J. R., Zhu, X., Wang, Y., Sullards, C., Ringe, D., Cheng, X., and Kahn, R. A. (2001). 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, 42477–42484

    Article  CAS  PubMed  Google Scholar 

  • Aridor, M., Fish, K. N., Bannykh, S., Weissman, J., Roberts, T. H., Lippincott-Schwartz, J., and Balch, W. E. (2001). The Sar1 GTPase coordinates biosynthetic cargo selection with endoplasmic reticulum export site assembly. J. Cell Biol., 152, 213–229.

    Article  CAS  PubMed  Google Scholar 

  • Aridor, M., Weissman, J., Bannykh, S., Nuoffer, C., and Balch, W. E. (1998). Cargo selection by the COP-II budding machinery during export from the ER. J. Cell Biol., 141, 61–70.

    Article  CAS  PubMed  Google Scholar 

  • Balch, W. E., McCaffery, J. M., Plutner, H., and Farquhar, M. G. (1994). Vesicular stomatitis virus glycoprotein is sorted and concentrated during export from the endoplasmic reticulum. Cell, 76, 841–852.

    Article  CAS  PubMed  Google Scholar 

  • Barlowe, C., ďEnfert, C., and Schekman, R. (1993). Purification and characterization of SAR1p, a small GTP-binding protein required for transport vesicle formation from the endoplasmic reticulum. J. Biol. Chem., 268, 873–879.

    CAS  PubMed  Google Scholar 

  • Barlowe, C., and Schekman, R. (1993). SEC12 encodes a guanine-nucleotide-exchange factor essential for transport vesicle budding from the ER. Nature, 365, 347–349.

    Article  CAS  PubMed  Google Scholar 

  • Bhamidipati, A., Lewis, S. A., and Cowan, N. J. (2000). ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J. Cell. Biol., 149, 1087–1096.

    Article  CAS  PubMed  Google Scholar 

  • Boman, A. L., Kuai, J., Zhu, X., Chen, J., Kuriyama, R., and Kahn, R. A. (1999). Arf proteins bind to mitotic kinesin-like protein 1 (MKLP1) in a GTP-dependent fashion. Cell Motil. Cytoskeleton., 44, 119–132.

    Article  CAS  PubMed  Google Scholar 

  • Breiner, M., Schürmann, A., Becker, W., and Joost, H.-G. (1996). Cloning of a novel member (Arl5) of the Arf family of Ras related GTPases. Biochim. Biophys. Acta., 1308, 1–6.

    PubMed  Google Scholar 

  • Brown, H. A., Gutowski, S., Moomaw, C. R., Slaughter, C., and Sternweis, P. C. (1993). ADP-ribosylation factor, a small GTP-dependent regulatory protein, stimulates phospholipase D activity. Cell, 75, 1137–1144.

    Article  CAS  PubMed  Google Scholar 

  • Cavenagh, M. M., Breiner, M., Schürmann. A., Rosenwald, A. G., Terui, T., Zhang, C., Randazzo, P. A., Adams, M., Joost, H.-G., and Kahn, R. A. (1994). ADP-ribosylation factor (Arf)-like 3, a new member of the Arf family of GTP-binding proteins cloned from human and rat tissues. J. Biol. Chem., 269, 18937–18942.

    CAS  PubMed  Google Scholar 

  • Clark, J., Moore, L., Krasinskas, A., Way, J., Battey, J., Tamkun, J., and Kahn, R. A. (1993). Selective amplification of additional members of the ADP-ribosylation factor (Arf) family: cloning of additional human and Drosophila Arf-like genes. Proc. Natl. Acad. Sci., USA, 90, 8952–8956.

    CAS  PubMed  Google Scholar 

  • Cockcroft, S., Thomas, G. M., Fensome, A., Geny, B., Cunningham, E., Gout, I., Hiles, I., Totty, N. F., Truong, O., and Hsuan, J. J. (1994). Phospholipase D: a downstream effector of Arf in granulocytes. Science, 263, 523–526.

    CAS  PubMed  Google Scholar 

  • Cook, T. A., Ghomashchi, F., Gelb, M. H., Florio, S. K., and Beavo, J. A. (2001). The delta subunit of type 6 phosphodiesterase reduces light-induced cGMP hydrolysis in rod outer segments. J. Biol. Chem., 276, 5248–5255.

    Article  CAS  PubMed  Google Scholar 

  • Dascher, C., and Balch, W. E. (1994). Dominant inhibitory mutants of Arf1 block endoplasmic reticulum to Golgi transport and trigger disassembly of the Golgi apparatus. J. Biol. Chem., 269, 1437–1448.

    CAS  PubMed  Google Scholar 

  • Donaldson, J. G., Kahn, R. A., Lippincott-Schwartz, J., and Klausner, R. D. (1991). Binding of Arf and beta-COP to Golgi membranes: possible regulation by a trimeric G protein. Science, 254, 1197–1199.

    CAS  PubMed  Google Scholar 

  • D’Souza-Schorey, C., Boshans R. L., McDonough, M., Stahl, P. D., and Van Aelst, L. (1997). A role for POR, a Rac1-interacting protein, in ARF6-mediated cytoskeletal rearrangements. EMBO J., 16, 5445–5454.

    Google Scholar 

  • Fiore, C., Trezeguet, V., Le Saux, A., Roux, P., Schwimmer, C., Dianoux, A. C., Noel, F., Lauquin, G. J., Brandolin, G., and Vignais, P. V. (1998). The mitochondrial ADP/ATP carrier: structural, physiological and pathological aspects. Biochimie, 80, 137–150.

    Article  CAS  PubMed  Google Scholar 

  • Florio, S. K., Prusti, R. K., and Beavo, J. A. (1996). Solubilization of membrane-bound rod phosphodiesterase by the rod phosphodiesterase recombinant delta subunit. J. Biol. Chem., 271, 24036–24047.

    CAS  PubMed  Google Scholar 

  • Gillespie, P. G., Prusti, R. K., Apel, E. D., and Beavo, J. A. (1989). A soluble form of bovine rod photoreceptor phosphodiesterase has a novel 15-kDa subunit. J. Biol. Chem., 264, 12187–12193.

    CAS  PubMed  Google Scholar 

  • Görlich, D., and Mattaj, I. W. (1996). Nucleocytoplasmic transport. Science, 271, 1513–1518.

    PubMed  Google Scholar 

  • Goldberg, J. (1998). Structural basis for activation of Arf GTPase: mechanisms of guanine nucleotide exchange and GTP-myristoyl switching. Cell, 95, 237–248.

    Article  CAS  PubMed  Google Scholar 

  • Goldberg, J. (1999). Structural and functional analysis of the Arf1-ArfGAP complex reveals a role for coatomer in GTP hydrolysis. Cell, 96, 893–902.

    Article  CAS  PubMed  Google Scholar 

  • Graham, B. H., Waymire, K. G., Cottrell, B., Trounce, I. A., MacGregor, G. R., and Wallace, D. C. (1997). A mouse model for mitochondrial myopathy and cardiomyopathy resulting from a deficiency in the heart/muscle isoform of the adenine nucleotide translocator. Nat. Genet., 16, 226–234.

    Article  CAS  PubMed  Google Scholar 

  • Hanzal-Bayer, M., Renault, L., Roversi, P., Wittinghofer, A., and Hillig R. C. (2002). The complex of Arl2-GTP and PDE delta: from structure to function. EMBO J., 21, 2095–2106.

    Article  CAS  PubMed  Google Scholar 

  • Hillig, R. C., Hanzal-Bayer, M., Linari, M., Becker, J., Wittinghofer, A., and Renault, L. (2000). Structural and biochemical properties show Arl3-GDP as a distinct GTP binding protein. Structure Fold. Des., 8, 1239–1245.

    CAS  PubMed  Google Scholar 

  • Honda, A., Nogami, M., Yokozeki, T., Yamazaki, M., Nakamura, H., Watanabe, H., Kawamoto, K., Nakayama, K., Morris, A. J., Frohman, M. A., and Kanaho, Y. (1999). Phosphatidylinositol 4-phosphate 5-kinase alpha is a downstream effector of the small G protein Arf6 in membrane ruffle formation. Cell, 99, 521–532.

    Article  CAS  PubMed  Google Scholar 

  • Hoyt, M. A., Stearns, T., and Botstein, D. (1990). Chromosome instability mutants of Saccharomyces cerevisiae that are defective in microtubule-mediated processes. Mol. Cell Biol., 10, 223–234.

    CAS  PubMed  Google Scholar 

  • Huang, C. F., Buu, L. M., Yu, W. L., and Lee, F. J. (1999). Characterization of a novel ADP-ribosylation factor-like protein (yArl3) in Saccharomyces cerevisiae. J. Biol. Chem., 274, 3819–3827.

    CAS  PubMed  Google Scholar 

  • Ingley, E., Williams, J. H., Walker, C. E., Tsai, S., Colley, S., Sayer, M. S., Tilbrook, P. A., Sarna, M., Beaumont, J. G., and Klinken, S. P. (1999). A novel ADP-ribosylation like factor (Arl-6), interacts with the protein-conducting channel SEC61beta subunit. FEBS Lett., 459, 69–74.

    Article  CAS  PubMed  Google Scholar 

  • Jacobs, S., Schilf, C., Fliegert, F., Koling, S., Weber, Y., Schürmann, A., and Joost, H.-G. (1999). ADP-ribosylation factor (Arf)-like 4, 6, and 7 represent a subgroup of the Arf family characterization by rapid nucleotide exchange and a nuclear localization signal. FEBS Lett., 456, 384–388.

    Article  CAS  PubMed  Google Scholar 

  • Jacobs, S., Schürmann, A., Becker, W., Böckers, T. M., Copeland, N.G., Jenkins, N. A., and Joost, H.-G. (1998). The mouse ADP-ribosylation factor-like 4 gene: two separate promoters direct specific transcription in tissues and testicular germ cell. Biochem. J., 335, 259–265.

    CAS  PubMed  Google Scholar 

  • Kahn, R. A., and Gilman, A. G. (1984). ADP-ribosylation of Gs promotes the dissociation of its alpha and beta subunits. J. Biol. Chem., 259, 6235–6240.

    CAS  PubMed  Google Scholar 

  • Kahn, R. A., and Gilman, A. G. (1986). The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein. J. Biol. Chem., 261, 7906–7911.

    CAS  PubMed  Google Scholar 

  • Kahn, R. A., Kern, F. G., Clark, J., Gelmann, E. P., and Rulka, C. (1991). Human ADP-ribosylation factors. A functionally conserved family of GTP-binding proteins. J. Biol. Chem., 266, 2606–2614.

    CAS  PubMed  Google Scholar 

  • Kahn, R. A., Randazzo, P., Serafini, T., Weiss, O., Rulka, C., Clark, J., Amherdt, M., Roller, P., Orci, L., and Rothman J. E. (1992). The amino terminus of ADP-ribosylation factor (Arf) is a critical determinant of Arf activities and is a potent and specific inhibitor of protein transport. J. Biol. Chem., 267, 13039–13046.

    CAS  PubMed  Google Scholar 

  • Kahn, R. A., Terui, T., and Randazzo, P. A. (1996). Effects of acid phospholipids on Arf activities: potential roles in membrane traffic. J. Lipid Mediat. Cell. Signal., 14, 209–214.

    Article  CAS  PubMed  Google Scholar 

  • Kanoh, H., Williger, B. T., and Exton, J. H. (1997). Arfaptin 1, a putative cytosolic target protein of ADP-ribosylation factor, is recruited to Golgi membranes. J. Biol. Chem., 272, 5421–5429.

    CAS  PubMed  Google Scholar 

  • Klausner, R. D., Donaldson, J. G., and Lippincott-Schwartz, J. (1992). Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell Biol., 116, 1071–1080.

    Article  CAS  PubMed  Google Scholar 

  • Kuehn, M. J., Herrmann, J. M., and Schekman, R. (1998). COP-II-cargo interactions direct protein sorting into ER-derived transport vesicles. Nature, 391, 187–190.

    CAS  PubMed  Google Scholar 

  • Kuge, O., Dascher, C., Orci, L., Rowe, T., Amherdt, M., Plutner, H., Ravazzola, M., Tanigawa, G., Rothman, J. E., and Balch, W. E. (1994). Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J. Cell Biol., 25, 51–65.

    Google Scholar 

  • Kuriyama, R., Gustus, C., Terada, Y., Uetake, Y., and Matuliene, J. (2002). CHO1, a mammalian kinesin-like protein, interacts with F-actin and is involved in the terminal phase of cytokinesis. J. Cell Biol., 156, 783–790.

    Article  CAS  PubMed  Google Scholar 

  • Lacal, J. C. and McCormick, F. (1993). The Ras superfamily of GTPases. Boca Raton, FL. CRC Press.

    Google Scholar 

  • Lee, F. J., Moss, J., and Vaughan, M. (1992). Human and Giardia ADP-ribosylation factors (Arfs) complement Arf function in Saccharomyces cerevisiae. J. Biol. Chem., 267, 24441–24445.

    CAS  PubMed  Google Scholar 

  • Levy, S. E., Chen, Y. S., Graham, B. H., and Wallace, D. C. (2000). Expression and sequence analysis of the mouse adenine nucleotide translocase 1 and 2 genes. Gene, 254, 57–66.

    Article  CAS  PubMed  Google Scholar 

  • Lewis, S. A., Tian, G., and Cowan, N. J. (1997). Thel alpha and beta tubulin folding pathways. Trends Cell Biol., 7, 479–485.

    CAS  Google Scholar 

  • Lin, C. Y., Huang, P. H., Liao, W. L., Cheng, H. J., Huang, C. F., Kuo, J. C., Patton, W. A., Massenburg, D., Moss, J., and Lee, F. J. (2000). Arl4, an Arf-like protein that is developmentally regulated and localized to nuclei and nucleoli. J. Biol. Chem., 275, 37815–37823.

    CAS  PubMed  Google Scholar 

  • Linari, M., Hanzal-Bayer, M., and Becker, J. (1999a). The delta subunit of rod specific cyclic GMP phosphodiesterase, PDE delta, interacts with the Arf-like protein Arl3 in a GTP specific manner. FEBS Lett., 458, 55–59.

    Article  CAS  PubMed  Google Scholar 

  • Linari, M., Ueffing, M., Manson, F., Wright, A., Meitinger, T., and Becker, J. (1999b). The retinitis pigmentosa GTPase regulator, RPGR, interacts with the delta subunit of rod cyclic GMP phosphodiesterase. Proc. Natl. Acad. Sci., USA, 96, 1315–1320.

    Article  CAS  PubMed  Google Scholar 

  • Lowe, S. L., Wong, S. H., and Hong, W. (1996). The mammalian Arf-like protein 1 (Arl1) is associated with the Golgi complex. J. Cell. Sci., 109, 209–220.

    CAS  PubMed  Google Scholar 

  • Lu, L., Horstmann, H., Ng, C., and Hong, W. (2001). Regulation of Golgi structure and function by Arf-like protein 1 (Arl1). J. Cell. Sci., 114, 4543–4555.

    CAS  PubMed  Google Scholar 

  • Marzesco, A. M., Galli, T., Louvard, D., and Zahraoui, A. (1998). The rod cGMP phosphodiesterase delta subunit dissociates the small GTPase Rab13 from membranes. J. Biol. Chem., 273, 22340–22345.

    Article  CAS  PubMed  Google Scholar 

  • Matsuoka, K., Orci, L., Amherdt, M., Bednarek, S. Y., Hamamoto, S., Schekman, R., and Yeung, T. (1998). COP-II-coated vesicle formation reconstituted with purified coat proteins and chemically defined liposomes. Cell, 93, 263–275.

    Article  CAS  PubMed  Google Scholar 

  • Meindl, A., Dry, K., Herrmann, K., Manson, F., Ciccodicola, A., Edgar, A., Carvalho, M. R., Achatz, H., Hellebrand, H., Lennon, A., Migliaccio, C., Porter, K., Zrenner, E., Bird, A., Jay, M., Lorenz, B., Wittwer, B., D’Urso, M., Meitinger, T., and Wright A. (1996). A gene (RPGR) with homology to the RCC1 guanine nucleotide exchange factor is mutated in X-linked retinitis pigmentosa (RP3). Nat. Genet., 13, 35–42.

    Article  CAS  PubMed  Google Scholar 

  • Moyer, B. D., Allan, B. B., and Balch, W. E. (2001). Rab1 interaction with a GM130 effector complex regulates COP-II vesicle cis-Golgi tethering. Traffic, 2, 268–276.

    Article  CAS  PubMed  Google Scholar 

  • Mueller, A. G., Joost, H.-G., and Schürmann A. (2002a). Mouse Arf-Related Protein 1: Genomic Organization and Analysis of Its Promoter. Biochem. Biophys. Res. Commun. 292, 113–120.

    Article  CAS  PubMed  Google Scholar 

  • Mueller, A. G., Moser, M., Kluge, R., Leder, S., Blum, M., Büttner, R., Joost, H.-G., and Schürmann, A. (2002b). Embryonic lethality caused by apoptosis during gastrulation in mice lacking the gene of the ADP-ribosylation factor-related protein 1. Mol. Cell. Biol., 22, 1488–1494.

    CAS  PubMed  Google Scholar 

  • Murtagh, J. J., Jr, Lee, F. J., Deak, P., Hall, L. M., Monaco, L., Lee, C. M., Stevens, L. A., Moss, J., and Vaughan, M. (1993). Molecular characterization of a conserved, guanine nucleotide-dependent ADP-ribosylation factor in Drosophila melanogaster. Biochemistry, 32, 6011–6018.

    Article  CAS  PubMed  Google Scholar 

  • Nakano, A. and Muramatsu, M. (1989). A novel GTP-binding protein, Sar1p, is involved in transport from the endoplasmic reticulum to the Golgi apparatus. J. Cell Biol., 109, 2677–2691.

    Article  CAS  PubMed  Google Scholar 

  • Nigg, E. A. (1997). Nucleocytoplasmic transport: signals, mechanisms and regulation. Nature, 386, 779–787

    Article  CAS  PubMed  Google Scholar 

  • Radcliffe, P. A., Vardy, L., and Toda, T. (2000). A conserved small GTP-binding protein Alp41 is essential for the cofactor-dependent biogenesis of microtubules in fission yeast. FEBS Lett., 468, 84–88.

    Article  CAS  PubMed  Google Scholar 

  • Renault, L., Nassar, N., Vetter, I., Becker, J., Klebe, C., Roth, M., and Wittinghofer, A. (1998). The 1.7 A crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature, 392, 97–101.

    CAS  PubMed  Google Scholar 

  • Rothman, J. E. and Wieland, F. T. (1996). Protein sorting by transport vesicles. Science, 272, 227–234.

    CAS  PubMed  Google Scholar 

  • Schekman, R. and Orci, L. (1996). Coat proteins and vesicle budding. Science, 271, 1526–1533.

    CAS  PubMed  Google Scholar 

  • Schürmann, A., Breiner, M., Becker, W., Huppertz, C., Kainulainen, H., Kentrup, H. and Joost, H.-G. (1994). Cloning of two novel ADP-ribosylation factor-like proteins and characterization of their differential expression in 3T3-L1 cells. J. Biol. Chem. 269, 15683–15688.

    PubMed  Google Scholar 

  • Schürmann, A., Koling, S., Jacobs, S., Saftig, P., Krauss, S., Wennemuth, G., Kluge, R., and Joost, H.-G. (2002). Reduced sperm count and normal fertility in male mice with targeted disruption of the ADP-ribosylation factor-like (Arl4) gene. Mol. Cell. Biol., 22, 2761–2768.

    PubMed  Google Scholar 

  • Schürmann, A., Massmann, S., and Joost, H.-G. (1995). ARP is a plasma membrane-associated Ras-related GTPase with remote similarity to the family of ADP-ribosylation factors. J. Biol. Chem., 270, 30657–30563.

    PubMed  Google Scholar 

  • Schürmann, A., Schmidt, M., Asmus, M., Bayer, S., Fliegert, F., Koling, S., Massmann, S., Schilf, C., Subauste, M.C., Voss, M., Jakobs, K.H., and Joost, H.-G. (1999). 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.

    PubMed  Google Scholar 

  • Sharer, J. D. and Kahn, R. A. (1999). The Arf-like 2 (Arl2)-binding protein, BART. J. Biol. Chem., 274, 27553–27561.

    Article  CAS  PubMed  Google Scholar 

  • Sharer, J. D., Shern, J. F., Van Valkenburgh, H., Wallace, D. C., and Kahn, R. A. (2002). Arl2 and BART Enter Mitochondria and Bind the Adenine Nucleotide Transporter. Mol. Biol. Cell, 13, 71–83.

    Article  CAS  PubMed  Google Scholar 

  • Smith, S. A., Holik, P. R., Stevens, J., Melis, R., White, R., and Albertsen, H. (1995). Isolation and mapping of a gene encoding a novel human ADP-ribosylation factor on chromosome 17q12–q21. Genomics, 28, 113–115.

    Article  CAS  PubMed  Google Scholar 

  • Springer, S., Spang, A., and Schekman R. (1999). A primer on vesicle budding. Cell, 97, 145–148.

    Article  CAS  PubMed  Google Scholar 

  • Stearns, T., Hoyt, M. A. and Botstein, D. (1990). Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics, 124, 251–262.

    CAS  PubMed  Google Scholar 

  • Stepien, G., Torroni, A., Chung, A. B., Hodge, J. A. and Wallace, D. C. (1992). Differential expression of adenine nucleotide translocator isoforms in mammalian tissues and during muscle cell differentiation. J. Biol. Chem., 267, 14592–14597.

    CAS  PubMed  Google Scholar 

  • Tamkun, J. W., Kahn, R. A., Kissinger, M., Brizuela, B. J., Rulka, C., Scott, M. P., and Kennison, J.A. (1991). The arflike gene encodes an essential GTP-binding protein in Drosophila. Proc. Natl. Acad. Sci., USA, 88, 3120–3124.

    CAS  PubMed  Google Scholar 

  • Tarricone, C., Xiao, B., Justin, N., Walker, P. A., Rittinger, K., Gamblin, S. J., and Smerdon, S. J. (2001). The structural basis of Arfaptin-mediated cross-talk between Rac and Arf signalling pathways. Nature, 411, 215–219

    Article  CAS  PubMed  Google Scholar 

  • Tian, G., Lewis, S. A., Feierbach, B., Stearns, T., Rommelaere, H., Ampe, C., and Cowan, N. J. (1997). Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J. Cell. Biol., 138, 821–832.

    Article  CAS  PubMed  Google Scholar 

  • Van Valkenburgh, H., Shern, J. F., Sharer, J. D., Zhu, X., and Kahn, R. A. (2001). ADP-ribosylation factors (Arfs) and Arf-like 1 (Arl1) have both specific and shared effectors: characterizing Arl1-binding proteins. J. Biol. Chem., 276, 22826–22837.

    PubMed  Google Scholar 

  • Weissman, J. T., Plutner, H., and Balch, W. E. (2001). The mammalian guanine nucleotide exchange factor mSec12 is essential for activation of the Sar1 GTPase directing endoplasmic reticulum export. Traffic, 2, 465–475.

    Article  CAS  PubMed  Google Scholar 

  • Zhu, X., Boman, A. L., Kuai, J., Cieplak, W., and Kahn R. A. (2000). Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding. J. Biol. Chem., 275, 13465–13475.

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. German Institute of Human Nutrition, Potsdam-Rehbrücke, Germany

    Annette Schürmann & Hans-Georg Joost

Authors
  1. Annette Schürmann
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Hans-Georg Joost
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 2004 Springer Science + Business Media, Inc.

About this chapter

Cite this chapter

Schürmann, A., Joost, HG. (2004). Arf-Like Proteins. In: ARF Family GTPases. Proteins and Cell Regulation, vol 1. Springer, Dordrecht. https://doi.org/10.1007/1-4020-2593-9_16

Download citation

  • DOI: https://doi.org/10.1007/1-4020-2593-9_16

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-1-4020-1719-3

  • Online ISBN: 978-1-4020-2593-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation