QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

HOME  |   SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, August 16, 2006, 26(33):8570-8577; doi:10.1523/JNEUROSCI.1478-06.2006

This Article Full Text Full Text (PDF) Submit an eLetter Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Web of Science (15) Citing Articles via Google Scholar Google Scholar Articles by Popescu, D. C. Articles by Shieh, B.-H. Search for Related Content PubMed PubMed Citation Articles by Popescu, D. C. Articles by Shieh, B.-H.

 Previous Article  |  Next Article 

Cellular/Molecular
Scaffolding Protein INAD Regulates Deactivation of Vision by Promoting Phosphorylation of Transient Receptor Potential by Eye Protein Kinase C in Drosophila

Daniela C. Popescu,¹ Amy-Joan L. Ham,² and Bih-Hwa Shieh¹

¹Department of Pharmacology and Center for Molecular Neuroscience, Vanderbilt University Medical Center, and ²Department of Biochemistry and Mass Spectrometry Research Center, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

Correspondence should be addressed to Dr. Bih-Hwa Shieh, Department of Pharmacology, 402 Robinson Research Building, Vanderbilt University Medical Center, Nashville, TN 37232-6600. Email: bih-hwa.shieh{at}vanderbilt.edu

Drosophila visual signaling is one of the fastest G-protein-coupled transduction cascades, because effector and modulatory proteins are organized into a macromolecular complex ("transducisome"). Assembly of the complex is orchestrated by inactivation no afterpotential D (INAD), which colocalizes the transient receptor potential (TRP) Ca²⁺ channel, phospholipase C, and eye protein kinase C (eye-PKC), for more efficient signal transduction. Eye-PKC is critical for deactivation of vision. Moreover, deactivation is regulated by the interaction between INAD and TRP, because abrogation of this interaction in InaD^p215 results in slow deactivation similar to that of inaC^p209 lacking eye-PKC. To elucidate the mechanisms whereby eye-PKC modulates deactivation, here we demonstrate that eye-PKC, via tethering to INAD, phosphorylates TRP in vitro. We reveal that Ser⁹⁸² of TRP is phosphorylated by eye-PKC in vitro and, importantly, in the fly eye, as shown by mass spectrometry. Furthermore, transgenic expression of modified TRP bearing an Ala substitution leads to slow deactivation of the visual response similar to that of InaD^p215. These results suggest that the INAD macromolecular complex plays an essential role in termination of the light response by promoting efficient phosphorylation at Ser⁹⁸² of TRP for fast deactivation of the visual signaling.

Key words: Drosophila; INAD; PKC; TRP; vision; phosphorylation

---

Received April 6, 2006; revised July 14, 2006; accepted July 17, 2006.

Correspondence should be addressed to Dr. Bih-Hwa Shieh, Department of Pharmacology, 402 Robinson Research Building, Vanderbilt University Medical Center, Nashville, TN 37232-6600. Email: bih-hwa.shieh{at}vanderbilt.edu

This article has been cited by other articles:

				R. Bao and M. Friedrich Molecular Evolution of the Drosophila Retinome: Exceptional Gene Gain in the Higher Diptera Mol. Biol. Evol., June 1, 2009; 26(6): 1273 - 1287. [Abstract] [Full Text] [PDF]

				H. Lu, H.-T. Leung, N. Wang, W. L. Pak, and B.-H. Shieh Role of Ca2+/Calmodulin-dependent Protein Kinase II in Drosophila Photoreceptors J. Biol. Chem., April 24, 2009; 284(17): 11100 - 11109. [Abstract] [Full Text] [PDF]

				R. A. Falin, R. Morrison, A.-J. L. Ham, and K. Strange Identification of Regulatory Phosphorylation Sites in a Cell Volume- and Ste20 Kinase-dependent ClC Anion Channel J. Gen. Physiol., December 29, 2008; 133(1): 29 - 42. [Abstract] [Full Text] [PDF]

				C. J. Bashor, N. C. Helman, S. Yan, and W. A. Lim Using Engineered Scaffold Interactions to Reshape MAP Kinase Pathway Signaling Dynamics Science, March 14, 2008; 319(5869): 1539 - 1543. [Abstract] [Full Text] [PDF]

				N. Wang, H.-T. Leung, W. L. Pak, Y. T. Carl, B. E. Wadzinski, and B.-H. Shieh Role of Protein Phosphatase 2A in Regulating the Visual Signaling in Drosophila J. Neurosci., February 6, 2008; 28(6): 1444 - 1451. [Abstract] [Full Text] [PDF]

				J. S. Myers, R. Zhao, X. Xu, A.-J. L. Ham, and D. Cortez Cyclin-Dependent Kinase 2 Dependent Phosphorylation of ATRIP Regulates the G2-M Checkpoint Response to DNA Damage Cancer Res., July 15, 2007; 67(14): 6685 - 6690. [Abstract] [Full Text] [PDF]

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help