Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

ARFRP1 (ADP-Ribosylation Factor Related Protein 1)

  • Deike Hesse
  • Alexander Jaschke
  • Annette Schürmann
Reference work entry
First Online:
DOI: https://doi.org/10.1007/978-3-319-67199-4_177
How to cite

Historical Background

Due to the remote similarity of the ADP-ribosylation factor related protein 1 (ARFRP1) to other members of the ARF family, it was designated as a distant ARF family member (Fig. 1a). Discovered by the screening of adipocytes with degenerated primers for ARF proteins, ARFRP1 was shown to be highly conserved among species (97% identical amino acids between rat and human, 79% identical to Saccharomyces cerevisiae, and 74% identical to Drosophila melanogaster) and closest related to ARL1 (33% identical) and ARL3 (39% identical) (Schürmann et al. 1995, 1999). In comparison to the membrane association motif of other members of the ARF family (myristoylation), membrane association of ARFRP1 is mediated by acetylation of the initial methionine and interaction with an integral membrane protein Sys1 (Behnia et al. 2004; Setty et al. 2003). The Arfrp1gene consists of eight exons and is located on distal mouse chromosome 2 (human chromosome 20) with the transcriptional...
This is a preview of subscription content, log in to check access.

References

  1. Behnia R, Panic B, Whyte JR, Munro S. Targeting of the Arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p. Nat Cell Biol. 2004;6(5):405–13.PubMedCrossRefGoogle Scholar
  2. Boström P, Andersson L, Rutberg M, Perman J, Lidberg U, Johansson BR, Fernandez-Rodriguez J, Ericson J, Nilsson T, Borén J, Olofsson SO. SNARE proteins mediate fusion between cytosolic lipid droplets and are implicated in insulin sensitivity. Nat Cell Biol. 2007;9(11):1286–93.PubMedCrossRefGoogle Scholar
  3. Bryant NJ, Govers R, James DE. Regulated transport of the glucose transporter GLUT4. Nat Rev Mol Cell Biol. 2002;3(4):267–77.PubMedCrossRefGoogle Scholar
  4. He W, Barak Y, Hevener A, Olson P, Liao D, Le J, Nelson M, Ong E, Olefsky JM, Evans RM. Adipose-specific peroxisome proliferator-activated receptor gamma knockout causes insulin resistance in fat and liver but not in muscle. Proc Natl Acad Sci U S A. 2003;100(26):15712–7.PubMedPubMedCentralCrossRefGoogle Scholar
  5. Hesse D, Hommel A, Jaschke A, Moser M, Bernhardt U, Zahn C, Kluge R, Wittschen P, Gruber AD, Al-Hasani H, Joost HG, Schürmann A. Altered GLUT4 trafficking in adipocytes in the absence of the GTPase Arfrp1. Biochem Biophys Res Commun. 2010;394(4):896–903.PubMedCrossRefGoogle Scholar
  6. Hesse D, Jaschke A, Augustin R, Hommel A, Püschel GP, Petzke KJ, Joost HG, Schürmann A. Altered glucose metabolism in mice lacking Arfrp1 in the liver.Google Scholar
  7. Hickson GR, Chamberlain LH, Maier VH, Gould GW. Quantification of SNARE protein levels in 3 T3-L1 adipocytes: implications for insulin-stimulated glucose transport. Biochem Biophys Res Commun. 2000;270(3):841–5.PubMedCrossRefGoogle Scholar
  8. Hommel A, Hesse D, Völker W, Jaschke A, Moser M, Engel T, Blüher M, Zahn C, Chadt A, Ruschke K, Vogel H, Kluge R, Robenek H, Joost HG, Schürmann A. The ARF-like GTPase ARFRP1 is essential for lipid droplet growth and is involved in the regulation of lipolysis. Mol Cell Biol. 2010;30(5):1231–42.PubMedCrossRefGoogle Scholar
  9. Jaschke A, Chung B, Hesse D, Kluge R, Zahn C, Moser M, Petzke KJ, Koepsell H, Heeren J, Joost HG, Schuermann A. The Golgi-associated GTPase ARFRP1 controls the final step of intestinal chylomicron maturation.Google Scholar
  10. Kahn RA, Cherfils J, Elias M, Lovering RC, Munro S, Schurmann A. Nomenclature for the human Arf family of GTP-binding proteins: ARF, ARL, and SAR proteins. J Cell Biol. 2006;172(5):645–50.PubMedPubMedCentralCrossRefGoogle Scholar
  11. Kawanishi M, Tamori Y, Okazawa H, Araki S, Shinoda H, Kasuga M. Role of SNAP23 in insulin-induced translocation of GLUT4 in 3 T3-L1 adipocytes. Mediation of complex formation between syntaxin4 and VAMP2. J Biol Chem. 2000;275(11):8240–7.PubMedCrossRefGoogle Scholar
  12. Mueller AG, Joost HG, Schürmann A. Mouse ARF-related protein 1: genomic organization and analysis of its promoter. Biochem Biophys Res Commun. 2002a;292(1):113–20.PubMedCrossRefGoogle Scholar
  13. Mueller AG, Moser M, Kluge R, Leder S, Blum M, Büttner R, Joost HG, Schürmann A. Embryonic lethality caused by apoptosis during gastrulation in mice lacking the gene of the ADP-ribosylation factor-related protein 1. Mol Cell Biol. 2002b;22(5):1488–94.PubMedPubMedCentralCrossRefGoogle Scholar
  14. Munro S. The golgin coiled-coil proteins of the Golgi apparatus. Cold Spring Harb Perspect Biol. 2011;3(6):pii: a005256. doi:10.1101/cshperspect.a005256.CrossRefGoogle Scholar
  15. Panic B, Perisic O, Veprintsev DB, Williams RL, Munro S. Structural basis for Arl1-dependent targeting of homodimeric GRIP domains to the Golgi apparatus. Mol Cell. 2003;12(4):863–74.PubMedCrossRefGoogle Scholar
  16. Paratore S, Parenti R, Cavallaro S. Distribution of ADP-ribosylation factor-related protein 1 in mouse brain. Arch Ital Biol. 2008;146(1):53–61.PubMedPubMedCentralGoogle Scholar
  17. Schürmann A, Massmann S, Joost HG. ARP is a plasma membrane-associated Ras-related GTPase with remote similarity to the family of ADP-ribosylation factors. J Biol Chem. 1995;270(51):30657–63.PubMedCrossRefGoogle Scholar
  18. Schürmann A, Schmidt M, Asmus M, Bayer S, Fliegert F, Koling S, Massmann S, Schilf C, Subauste MC, Voss M, Jakobs KH, Joost HG. 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. 1999;274(14):9744–51.PubMedCrossRefGoogle Scholar
  19. Setty SR, Shin ME, Yoshino A, Marks MS, Burd CG. Golgi recruitment of GRIP domain proteins by Arf-like GTPase 1 is regulated by Arf-like GTPase 3. Curr Biol. 2003;13(5):401–4.PubMedCrossRefGoogle Scholar
  20. Zahn C, Hommel A, Lu L, Hong W, Walther DJ, Florian S, Joost HG, Schürmann A. Knockout of Arfrp1 leads to disruption of ARF-like1 (ARL1) targeting to the trans-Golgi in mouse embryos and HeLa cells. Mol Membr Biol. 2006;23(6):475–85.PubMedCrossRefGoogle Scholar
  21. Zahn C, Jaschke A, Weiske J, Hommel A, Hesse D, Augustin R, Lu L, Hong W, Florian S, Scheepers A, Joost HG, Huber O, Schürmann A. ADP-ribosylation factor-like GTPase ARFRP1 is required for trans-Golgi to plasma membrane trafficking of E-cadherin. J Biol Chem. 2008;283(40):27179–88.PubMedCrossRefGoogle Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  • Deike Hesse
    • 1
  • Alexander Jaschke
    • 1
  • Annette Schürmann
    • 1
  1. 1.Department of Experimental DiabetologyGerman Institute of Human Nutrition Potsdam-RehbrückeNuthetalGermany