377
Views
14
CrossRef citations to date
0
Altmetric
SPECIAL SECTION ARTICLES REVIEWS

The History of the Prolonged Depolarizing Afterpotential (PDA) and Its Role in Genetic Dissection of Drosophila Phototransduction

Pages 106-117 | Received 27 Dec 2011, Accepted 09 Feb 2012, Published online: 20 Mar 2012

REFERENCES

  • Alloway, P. G., & Dolph, P. J. (1999). A role for the light-dependent phosphorylation of visual arrestin. Proc Natl Acad Sci U S A, 96, 6072–6077.
  • Alloway, P. G., Howard, L., & Dolph, P. J. (2000). The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration. Neuron, 28, 129–138.
  • Benzer, S. (1967). Behavioral mutants of Drosophila isolated by countercurrent distribution. Proc Natl Acad Sci U S A, 58, 1112–1119.
  • Blumenfeld, A., Erusalimsky, J., Heichal, O., Selinger, Z., & Minke, B. (1985). Light-activated guanosinetriphosphatase in Musca eye membranes resembles the prolonged depolarizing afterpotential in photoreceptor cells. Proc Natl Acad Sci U S A, 82, 7116–7120.
  • Byk, T., Bar Yaacov, M., Doza, Y. N., Minke, B., & Selinger, Z. (1993). Regulatory arrestin cycle secures the fidelity and maintenance of the fly photoreceptor cell. Proc Natl Acad Sci U S A, 90, 1907–1911.
  • Cosens, D., & Briscoe, D. (1972). A switch phenomenon in the compound eye of the white-eyed mutant of Drosophila melanogaster. J Insect Physiol, 18, 627–632.
  • Devary, O., Heichal, O., Blumenfeld, A., Cassel, D., Suss, E., Barash, S., . (1987). Coupling of photoexcited rhodopsin to inositol phospholipid hydrolysis in fly photoreceptors. Proc Natl Acad Sci U S A, 84, 6939–6943.
  • Dolph, P. J., Ranganathan, R., Colley, N. J., Hardy, R. W., Socolich, M., & Zuker, C. S. (1993). Arrestin function in inactivation of G protein-coupled receptor rhodopsin in vivo. Science, 260, 1910–1916.
  • Hamdorf, K. (1979). The physiology of invertebrate visual pigments. In H. Autrum (Ed.), Handbook of sensory physiology. Comparative physiology and evolution of vision in invertebrates (pp. 145–224). Berlin: Springer-Verlag.
  • Hamdorf, K., & Razmjoo, S. (1977). The prolonged depolarizing afterpotential and its contribution to the understanding of photoreceptor function. Biophys Struct Mech, 3, 163–170.
  • Heisenberg M., & Goetz K. G. (1975). The use of mutations for the partial degradation of vision in Drosophila melanogaster. J Comp Physiol, 98, 217–241.
  • Hillman P., Dodge F. A., Hochstein, S., Knight, B. W., & Minke, B. (1973). Rapid dark recovery of the invertebrate early receptor potential. J Gen Physiol, 62, 77–86.
  • Hillman, P., Hochstein, S., & Minke, B. (1972). A visual pigment with two physiologically active stable states. Science, 175, 1486–1488.
  • Hillman, P., Hochstein, S., & Minke, B. (1983). Transduction in invertebrate photoreceptors: Role of pigment bistability. Physiol Rev, 63, 668–772.
  • Hochstein, S., Minke, B., & Hillman, P. (1973). Antagonistic components of the late receptor potential in the barnacle photoreceptor arising from different stages of the pigment process. J Gen Physiol, 62, 105–128.
  • Hubbard, R., & St George, R. C. (1958). The rhodopsin system of the squid. J Gen Physiol, 41, 501–528.
  • Katz, B., & Minke, B. (2009). Drosophila photoreceptors and signaling mechanisms. Front Cell Neurosci, 3, 1–10.
  • Kirschfeld, K., Franceschini, N., & Minke, B. (1977). Evidence for a sensitising pigment in fly photoreceptors. Nature, 269, 386–390.
  • Kiselev, A., Socolich, M., Vinos, J., Hardy, R W., Zuker, C. S., & Ranganathan, R. (2000). A molecular pathway for light-dependent photorecptor apoptosis in Drosophila. Neuron, 28, 139–152.
  • Koenig, J., & Merriam, J. (1977). Autosomal ERG mutants. Drosoph Inf Ser, 52, 50–51.
  • Lee, S. J., & Montell, C. (2004). Light-dependent translocation of visual arrestin regulated by the NINAC myosin III. Neuron, 43, 95–103.
  • Liu, C. H., Satoh, A. K., Postma, M., Huang, J., Ready, D. F., & Hardie, R. C. (2008). Ca2 + -dependent metarhodopsin inactivation mediated by calmodulin and NINAC myosin III. Neuron, 59, 778–789.
  • Matsumoto, H., O'Tousa, J. E., & Pak, W L. (1982). Light-induced modification of Drosophila retinal polypeptides in vivo. Science, 217, 839–841.
  • Matsumoto, H., Kurien, B.T., Takagi, Y., Kahn, E.S., Kinumi, T., Komori, N., Yamada, T., Hayashi, F., Isono, K., & Pak, W.L., . (1994). Phosrestin I undergoes the earliest light-induced phosphorylation by a calcium/calmodulin-dependent protein kinase in Drosophila photoreceptors. Neuron, 12, 997–1010.
  • Minke, B. (1979). Transduction in photoreceptors with bistable pigment:Intermediate processes. Biophys Struct Mech, 5, 163–174.
  • Minke, B., & Kirschfeld, K. (1978). Microspectrophotometric evidence for two photoconvertible states of visual pigments in the barnacle lateral eye. J Gen Physiol, 71, 37–45.
  • Minke, B. (1986). Photopigment-dependent adaptation in invertebrates–implications for vertebrates. In H. Stieve (Ed.), The molecular mechanism of photoreception (pp. 241–265). Berlin: Springer-Verlag.
  • Minke, B., Hochstein, S., & Hillman, P. (1973a). Early receptor potential evidence for the existence of two thermally stable states in the barnacle visual pigment. J Gen Physiol, 62, 87–104.
  • Minke, B., Hochstein, S., & Hillman, P. (1973b). Letter: Antagonistic process as source of visible-light suppression of afterpotential in Limulus UV photoreceptors. J Gen Physiol, 62, 787–791.
  • Minke, B., & Kirschfeld, K. (1979). The contribution of a sensitizing pigment to the photosensitivity spectra of fly rhodopsin and metarhodopsin. J Gen Physiol, 73, 517 540.
  • Minke, B., & Kirschfeld, K. (1980). Fast electrical potentials arising from activation of metarhodopsin in the fly. J Gen Physiol, 75, 381–402.
  • Minke, B., Wu, C.-F., & Pak, W. L. (1975). Isolation of light-induce response of the central retinular cells from the electroretinogram of Drosophila. J Comp Physiol, 98, 345 355.
  • Morgan, T. H. (1910). Sex limited inheritance in Drosophila. Science, 32, 120–122.
  • Muijser, H., Leutscher-Hazelhoff, J. T., Stavenga, D. G., & Kuiper, J. W. (1975). Photopigment conversions expressed in receptor potential and membrane resistance of blowfly visual sense cells. Nature, 254, 520–522.
  • Nolte, J., & Brown, J. E. (1972a). Electrophysiological properties of cells in the median ocellus of Limulus. J Gen Physiol, 59, 167–185.
  • Nolte, J., & Brown, J. E. (1972b). Ultraviolet-induced sensitivity to visible light in ultraviolet receptors of Limulus. J Gen Physiol, 59, 186–200.
  • O'Tousa, J E., Baehr, W., Martin, R. L., Hirsh, J., Pak, W. L., & Applebury, M. L. (1985). The Drosophila ninaE gene encodes an opsin. Cell, 40, 839–850.
  • Pak, W.L., Shino, S., & Leung, H.T. (2012). PDA (Prolonged Depolarizing Afterpotential)-deffective mutants: The story of nina's and ina's—pinta and santa maria, too. J Neurogenetics, Jan 27. [Epub ahead of print].
  • Pak, W L. (1979). Study of photoreceptor function using Drosophila mutants. In X. Breakfield (Ed.), Neurogenetics, genetic approaches to the nervous system (pp. 67–99). New York: Elsevier North-Holland.
  • Pak, W. L. (1995). Drosophila in vision research. The Friedenwald Lecture. Invest Ophthalmol Vis Sci, 36, 2340 2357.
  • Pak, W L., Grossfield, J., & Arnold, K. S. (1970). Mutants of the visual pathway of Drosophila melanogaster. Nature, 227, 518–520.
  • Pak, W. L., Grossfield, J., & White, N. V. (1969). Nonphototactic mutants in a study of vision of Drosophila. Nature, 222, 351–354.
  • Pak, W. L., & Lidington, K. J. (1974). Fast electrical potential from a long-lived, long-wavelength photoproduct of fly visual pigment. J Gen Physiol, 63, 740–756.
  • Pak, W. L., Ostroy, S. E., Deland, M. C., & Wu, C. F. (1976). Photoreceptor mutant of Drosophila: Is protein involved in intermediate steps of phototransduction? Science, 194, 956–959.
  • Paulsen, J., & Bentrop, J. (1984). Reversible phosphorylation of opsin induced by irradiation of blowfly retinae. J Comp Physiol A, 155, 39–45.
  • Paulsen, R., & Hoppe, I. (1978). Light-activated phosphorylation of cephalopod rhodopsin. FEBS Lett, 96, 55–58.
  • Paulsen, R., & Schwemer, J. (1979). Vitamin A deficiency reduces the concentration of visual pigment protein within blowfly photoreceptor membranes. Biochim Biophys Acta, 557, 385 390.
  • Selinger, Z., Doza, Y. N., & Minke, B. (1993). Mechanisms and genetics of photoreceptors desensitization in Drosophila flies. Biochim Biophys Acta, 1179, 283 299.
  • Steele, F. R., Washburn, T., Rieger, R., & O'Tousa, J. E. (1992). Drosophila retinal degeneration C (rdgC) encodes a novel serine/threonine protein phosphatase. Cell, 69, 669–676.
  • Venkatachalam, K., Wasserman, D., Wang, X., Li, R., Mills, E., Elsaesser, R., . (2010). Dependence on a retinophilin/myosin complex for stability of PKC and INAD and termination of phototransduction. J Neurosci, 30, 11337–11345.
  • Vinos, J., Jalink, K., Hardy, R. W., Britt, S. G., & Zuker, C. S. (1997). A G protein-coupled receptor phosphatase required for rhodopsin function. Science, 277, 687–690.
  • Yamada, T., Takeuchi, Y., Komori, N., Kobayashi, H., Sakai, Y., Hotta, Y., . (1990). A 49-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog. Science, 248, 483–486.
  • Zuker, C. S. (1996). The biology of vision of Drosophila. Proc Natl Acad Sci U S A, 93, 571–576.
  • Zuker, C. S., Cowman, A. F., & Rubin, G. M. (1985). Isolation and structure of a rhodopsin gene from D. melanogaster. Cell, 40, 851–858.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.