TRP and the PDZ protein, INAD, form the core complex required for retention of the signalplex in Drosophila photoreceptor cells

被引:139
作者
Li, HS
Montell, C
机构
[1] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
[2] Johns Hopkins Univ, Sch Med, Dept Neurosci, Baltimore, MD 21205 USA
关键词
PDZ; Drosophila; TRP; INAD; phototransduction;
D O I
10.1083/jcb.150.6.1411
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The light response in Drosophila photoreceptor cells is mediated by a series of proteins that assemble into a macromolecular complex referred to as the signalplex, The central player in the signalplex is inactivation no afterpotential D (INAD), a protein consisting of a tandem array of five PDZ domains. At least seven proteins bind INAD, including the transient receptor potential (TRP) channel, which depends on INAD for localization to the phototransducing organelle, the rhabdomere, However! the determinants required for localization of INAD are not known. In this work, we showed that INAD was required for retention rather than targeting of TRP to the rhabdomeres, In addition, we demonstrated that TRP bound to INAD through the COOH terminus, and this interaction was required for localization of INAD, Other proteins that depend on INAD for localization, phospholipase C and protein kinase C, also mislocalized. However, elimination of any other member of the signalplex had no impact on the spatial distribution of INAD. A direct interaction between TRP and INAD did not appear to have a role in the photoresponse independent of localization of multiple signaling components. Rather, the primary function of the TRP/INAD complex is to form the core unit required for localization of the signalplex to the rhabdomeres.
引用
收藏
页码:1411 / 1421
页数:11
相关论文
共 43 条
  • [1] Interaction of eye protein kinase C and INAD in Drosophila -: Localization of binding domains and electrophysiological characterization of a loss of association in transgenic flies
    Adamski, FM
    Zhu, MY
    Bahiraei, F
    Shieh, BH
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (28) : 17713 - 17719
  • [2] Molecular determinants for subcellular localization of PSD-95 with an interacting K+ channel
    Arnold, DB
    Clapham, DE
    [J]. NEURON, 1999, 23 (01) : 149 - 157
  • [3] Blest A., 1988, ADV INSECT PHYSL, P1, DOI 10.1016/s0065-2806(08)60021-1
  • [4] Requirement for the PDZ domain protein, INAD, for localization of the TRP store-operated channel to a signaling complex
    Chevesich, J
    Kreuz, AJ
    Montell, C
    [J]. NEURON, 1997, 18 (01) : 95 - 105
  • [5] Phospholipase C and termination of G-protein-mediated signalling in vivo
    Cook, B
    Bar-Yaacov, M
    Ben-Ami, HC
    Goldstein, RE
    Paroush, Z
    Selinger, Z
    Minke, B
    [J]. NATURE CELL BIOLOGY, 2000, 2 (05) : 296 - 301
  • [6] PDZ proteins organize synaptic signaling pathways
    Craven, SE
    Bredt, DS
    [J]. CELL, 1998, 93 (04) : 495 - 498
  • [7] Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition
    Daniels, DL
    Cohen, AR
    Anderson, JM
    Brünger, AT
    [J]. NATURE STRUCTURAL BIOLOGY, 1998, 5 (04) : 317 - 325
  • [8] DECOUET HG, 1987, EUR J CELL BIOL, V44, P50
  • [9] Dimitratos SD, 1999, BIOESSAYS, V21, P912, DOI 10.1002/(SICI)1521-1878(199911)21:11<912::AID-BIES3>3.0.CO
  • [10] 2-Z