The organization of INAD-signaling complexes by a multivalent PDZ domain protein in Drosophila photoreceptor cells ensures sensitivity and speed of signaling.
Phototransduction in Drosophila has emerged as an attractive model system for studying the organization of signaling cascades in vivo. In photoreceptor neurons, the multivalent PDZ protein INAD serves as a scaffold to assemble different components of the phototransduction pathway, including the effector PLC, the light-activated ion channel TRP, and a protein kinase C involved in deactivation of the light response. INAD is required for organizing and maintaining signaling complexes in the rhabdomeres of photoreceptors. This macromolecular organization endows photoreceptors with many of their signaling properties, including high sensitivity, fast activation and deactivation kinetics, and exquisite feedback regulation by small localized changes in [Ca2+]i. Assembly of transduction components into signaling complexes is also an important cellular strategy for ensuring specificity of signaling while minimizing unwanted cross-talk. In this report, we review INAD's role as a signal transduction scaffold and its role in the assembly and localization of photoreceptor complexes.
Tsunoda
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Haward Hughes Medical Institute, University of California, San Diego 92093-0649, USA. susan@flyeye.ucsd.edu or charles@flyeye.ucsd.edu
Zuker
C S
CS
D000818:Animals; D004330:Drosophila / Q000502:physiology*; D005136:Eye Proteins / Q000502:physiology*; D008565:Membrane Proteins; D017956:Photoreceptor Cells, Invertebrate / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology*; D062725:Tight Junction Proteins
D005136:Eye Proteins; D008565:Membrane Proteins; C107903:PATJ protein, human; D062725:Tight Junction Proteins