JBC PeproTech; Our Business is Cytokines!

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M204075200 on July 9, 2002

J. Biol. Chem., Vol. 277, Issue 37, 33884-33889, September 13, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/37/33884    most recent
M204075200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hong, Y. S.
Right arrow Articles by Pak, W. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hong, Y. S.
Right arrow Articles by Pak, W. L.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Single Amino Acid Change in the Fifth Transmembrane Segment of the TRP Ca2+ Channel Causes Massive Degeneration of Photoreceptors*

Young Seok HongDagger §, Soyeon Park||, Chaoxian GengDagger , Kwanghee Baek, John D. BowmanDagger , Jaeseung Yoon, and William L. PakDagger **

From the Dagger  Department of Biological Sciences, Purdue University, West Lafayette, Indiana 47907 and the  Department and Institute of Genetic Engineering, Kyung Hee University, Yongin City, Kyungki-Do, 449-471, Korea

The trp gene encodes subunits of a highly Ca2+-permeable class of light-activated channels of Drosophila photoreceptors. The recently characterized mutation in this gene, TrpP365, is semidominant and causes massive degeneration of photoreceptors by making the TRP channel constitutively active. We show that a single amino acid change, Phe-550 to Ile, near the beginning of the fifth transmembrane domain of TRP channel subunits is necessary to induce, and sufficient to closely mimic, the original mutant phenotypes of TrpP365. Hypotheses are presented as to why the amino acid residues at position 550 and its immediate vicinity might be important in influencing the regulation of the TRP channel and why the substitution of Phe for Ile at this position, in particular, could result in constitutive activity of the channel.


* This work was supported by National Institutes of Health Grant EY00033 (to W. L. P.) and by the Molecular Medicine Research Group Program from the Ministry of Science and Technology, Korea (to J. Y.). The confocal fluorescent images were obtained in a departmental confocal facility supported by National Science Foundation Grant BIR-9512962.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present address: Dept. of Biological Sciences, University of Notre Dame, South Bend, IN 46556.

|| Present address: PanGen Biotech Laboratories, Inc., 802 Business Incubator Center, Kyung Hee University, Yongin City, Kyungki-Do, 449-701, Korea.

** To whom correspondence should be addressed: Dept. of Biological Sciences, Purdue University, 1392 Lilly Hall, West Lafayette, IN 47907-1392. Tel.: 765-494-8202; Fax: 765-494-0876; E-mail: wpak@bilbo.bio.purdue.edu.


Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
IOVSHome page
R. M. Sappington and D. J. Calkins
Contribution of TRPV1 to Microglia-Derived IL-6 and NF{kappa}B Translocation with Elevated Hydrostatic Pressure
Invest. Ophthalmol. Vis. Sci., July 1, 2008; 49(7): 3004 - 3017.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
Z. Su, X. Zhou, W. J. Haynes, S. H. Loukin, A. Anishkin, Y. Saimi, and C. Kung
Yeast gain-of-function mutations reveal structure function relationships conserved among different subfamilies of transient receptor potential channels
PNAS, December 4, 2007; 104(49): 19607 - 19612.
[Abstract] [Full Text] [PDF]


Home page
NeuroscientistHome page
M. M. Aarts and M. Tymianski
TRPM7 and Ischemic CNS Injury
Neuroscientist, April 1, 2005; 11(2): 116 - 123.
[Abstract] [PDF]


Home page
J. Cell Sci.Home page
P. Georgiev, I. Garcia-Murillas, D. Ulahannan, R. C. Hardie, and P. Raghu
Functional INAD complexes are required to mediate degeneration in photoreceptors of the Drosophila rdgA mutant
J. Cell Sci., April 1, 2005; 118(7): 1373 - 1384.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.