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Gene Review

Arr2  -  Arrestin 2

Drosophila melanogaster

Synonyms: 49, 49 kDa arrestin-like protein, AH, ARR2, Arr, ...
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Disease relevance of Arr2


Psychiatry related information on Arr2

  • Odorant-specific requirements for arrestin function in Drosophila olfaction [4].

High impact information on Arr2

  • In this paper, we develop a theory that describes the kinetics of inactivation of the G protein-coupled receptor rhodopsin based on the rate of arrestin binding and test the theory using a combination of genetic and electrophysiological techniques in Drosophila photoreceptors [5].
  • The results demonstrate that the rate of arrestin binding determines the kinetics of receptor inactivation in vivo and thus is the event that controls signal amplification at the first step of this G protein-coupled transduction cascade [5].
  • Although visual arrestin has been shown to quench the catalytic activity of photoexcited, phosphorylated rhodopsin in a reconstituted system, its role in the intact rod cell remains unclear because phosphorylation alone reduces the catalytic activity of rhodopsin [6].
  • The intensity dependence of the photoresponse in rods lacking arrestin further suggests that, although arrestin is required for normal signal termination, it does not participate directly in light adaptation [6].
  • Analysis of the light response in these mutants shows that the Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade in vivo [7].

Biological context of Arr2


Anatomical context of Arr2

  • Also distinct from Arr2, Arr1 is essential for light-independent photoreceptor survival [8].
  • As the olfactory deficits vary according to chemical identity and concentration, they indicate that a spectrum of arrestin activity is essential for odor processing depending upon the particular olfactory pathway involved [4].
  • Interestingly, we found that the Arr2 phosphorylation mutant was still capable of binding to rhodopsin; however, it was unable to release from membranes once rhodopsin had converted back to its inactive form [2].
  • We find that phosrestin I (PRI), a Drosophila homolog of vertebrate photoreceptor arrestin, undergoes light-induced phosphorylation on a subsecond time scale which is faster than that of any other protein in vivo [11].
  • We observed that Drosophila PRI exists in the random preparation, but it also exists in other subcellular fractions [12].

Associations of Arr2 with chemical compounds


Enzymatic interactions of Arr2

  • Here we present biochemical evidence that a CaM PK that phosphorylates arrestin in Limulus eyes is structurally similar to mammalian CaM PK II [16].

Regulatory relationships of Arr2


Other interactions of Arr2


Analytical, diagnostic and therapeutic context of Arr2

  • Proteins were resolved by polyacrylamide gel electrophoresis (PAGE) and subjected to immunoblot analysis using antibodies directed to rhodopsin, NinaA, Arr1, and Arr2 [20].
  • Immunocytochemistry at the EM level revealed a distribution of both Drosophila and Musca PRI epitopes in membranous vesicular structures in the cytosol as well as in the rhabdomeric microvillar membranes where the visual pigment, rhodopsin, exists [12].
  • (2) Rabbit antibodies raised against Musca PRI, against bovine arrestin, and against a synthetic peptide based on the Drosophila PRI sequence stained the Drosophila and Musca PRIs specifically on 1 and 2-dimensional Western immunoblots [12].
  • Native gel electrophoresis, gel filtration, and analytical ultracentrifugation demonstrated the ability of IP(6) to promote arrestin-2 oligomerization via the two crystallographically defined ligand-binding locations [13].
  • 1 microm frozen sections were cut on an ultracryomicrotome, then stained with antibodies specific for rhodopsin or arrestin [21].


  1. An essential role for endocytosis of rhodopsin through interaction of visual arrestin with the AP-2 adaptor. Orem, N.R., Xia, L., Dolph, P.J. J. Cell. Sci. (2006) [Pubmed]
  2. A role for the light-dependent phosphorylation of visual arrestin. Alloway, P.G., Dolph, P.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  3. Twenty Drosophila visual system cDNA clones: one is a homolog of human arrestin. Hyde, D.R., Mecklenburg, K.L., Pollock, J.A., Vihtelic, T.S., Benzer, S. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  4. Odorant-specific requirements for arrestin function in Drosophila olfaction. Merrill, C.E., Sherertz, T.M., Walker, W.B., Zwiebel, L.J. J. Neurobiol. (2005) [Pubmed]
  5. Arrestin binding determines the rate of inactivation of the G protein-coupled receptor rhodopsin in vivo. Ranganathan, R., Stevens, C.F. Cell (1995) [Pubmed]
  6. Prolonged photoresponses in transgenic mouse rods lacking arrestin. Xu, J., Dodd, R.L., Makino, C.L., Simon, M.I., Baylor, D.A., Chen, J. Nature (1997) [Pubmed]
  7. Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo. Dolph, P.J., Ranganathan, R., Colley, N.J., Hardy, R.W., Socolich, M., Zuker, C.S. Science (1993) [Pubmed]
  8. Arrestin1 mediates light-dependent rhodopsin endocytosis and cell survival. Satoh, A.K., Ready, D.F. Curr. Biol. (2005) [Pubmed]
  9. Light-dependent translocation of visual arrestin regulated by the NINAC myosin III. Lee, S.J., Montell, C. Neuron (2004) [Pubmed]
  10. A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog. Yamada, T., Takeuchi, Y., Komori, N., Kobayashi, H., Sakai, Y., Hotta, Y., Matsumoto, H. Science (1990) [Pubmed]
  11. Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors. Matsumoto, H., Kurien, B.T., Takagi, Y., Kahn, E.S., Kinumi, T., Komori, N., Yamada, T., Hayashi, F., Isono, K., Pak, W.L. Neuron (1994) [Pubmed]
  12. Phosrestin I, an arrestin homolog that undergoes light-induced phosphorylation in dipteran photoreceptors. Komori, N., Usukura, J., Kurien, B., Shichi, H., Matsumoto, H. Insect Biochem. Mol. Biol. (1994) [Pubmed]
  13. Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding. Milano, S.K., Kim, Y.M., Stefano, F.P., Benovic, J.L., Brenner, C. J. Biol. Chem. (2006) [Pubmed]
  14. Arrestin-subtypes in insect antennae. Raming, K., Freitag, J., Krieger, J., Breer, H. Cell. Signal. (1993) [Pubmed]
  15. Modulating sphingolipid biosynthetic pathway rescues photoreceptor degeneration. Acharya, U., Patel, S., Koundakjian, E., Nagashima, K., Han, X., Acharya, J.K. Science (2003) [Pubmed]
  16. Calcium/calmodulin-dependent protein kinase II and arrestin phosphorylation in Limulus eyes. Calman, B.G., Andrews, A.W., Rissler, H.M., Edwards, S.C., Battelle, B.A. J. Photochem. Photobiol. B, Biol. (1996) [Pubmed]
  17. Loss of the phospholipase C gene product induces massive endocytosis of rhodopsin and arrestin in Drosophila photoreceptors. Orem, N.R., Dolph, P.J. Vision Res. (2002) [Pubmed]
  18. Myosin III illuminates the mechanism of arrestin translocation. Strissel, K.J., Arshavsky, V.Y. Neuron (2004) [Pubmed]
  19. Phosrestide-1, a peptide derived from the Drosophila photoreceptor protein phosrestin I, is a potent substrate for Ca2+/calmodulin-dependent protein kinase II from rat brain. Kahn, E.S., Kinumi, T., Tobin, S.L., Matsumoto, H. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (1998) [Pubmed]
  20. Expression of rhodopsin and arrestin during the light-dark cycle in Drosophila. Hartman, S.J., Menon, I., Haug-Collet, K., Colley, N.J. Mol. Vis. (2001) [Pubmed]
  21. Epitope masking of rhabdomeric rhodopsin during endocytosis-induced retinal degeneration. Orem, N.R., Dolph, P.J. Mol. Vis. (2002) [Pubmed]
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