WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, November 14, 2007, 27(46):12743-12754; doi:10.1523/JNEUROSCI.4264-07.2007

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Web of Science
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 Web of Science (1)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lee, A.
Right arrow Articles by Haeseleer, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lee, A.
Right arrow Articles by Haeseleer, F.

 Previous Article  |  Next Article 

Cellular/Molecular
Phosphorylation of the Ca2+-Binding Protein CaBP4 by Protein Kinase C {zeta} in Photoreceptors

Amy Lee,1 Amber Jimenez,2 Guiying Cui,1 and Françoise Haeseleer2

1Department of Pharmacology and Center for Neurodegenerative Disease, Emory University School of Medicine, Atlanta, Georgia 30322, and 2Department of Ophthalmology, University of Washington, Seattle, Washington 98195

Correspondence should be addressed to Françoise Haeseleer, University of Washington, Department of Ophthalmology, 1959 North East Pacific Street, Box 356485, Seattle, WA 98195. Email: fanfan{at}u.washington.edu

CaBP4 is a calmodulin-like neuronal calcium-binding protein that is crucial for the development and/or maintenance of the cone and rod photoreceptor synapse. Previously, we showed that CaBP4 directly regulates Cav1 L-type Ca2+ channels, which are essential for normal photoreceptor synaptic transmission. Here, we show that the function of CaBP4 is regulated by phosphorylation. CaBP4 is phosphorylated by protein kinase C {zeta} (PKC{zeta}) at serine 37 both in vitro and in the retina and colocalizes with PKC{zeta} in photoreceptors. CaBP4 phosphorylation is greater in light-adapted than dark-adapted mouse retinas. In electrophysiological recordings of cells transfected with Cav1.3 and CaBP4, mutation of the serine 37 to alanine abolished the effect of CaBP4 in prolonging the Ca2+ current through Cav1.3 channel, whereas inactivating mutations in the CaBP4 Ca2+-binding sites strengthened Cav1.3 modulation. These findings demonstrate how light-stimulated changes in CaBP4 phosphorylation and Ca2+ binding may regulate presynaptic Ca2+ signals in photoreceptors.

Key words: CaBP4; Ca2+-binding proteins; phosphorylation; protein kinase C {zeta}; Ca2+ channel; photoreceptors


Received June 22, 2007; accepted Oct. 9, 2007.

Correspondence should be addressed to Françoise Haeseleer, University of Washington, Department of Ophthalmology, 1959 North East Pacific Street, Box 356485, Seattle, WA 98195. Email: fanfan{at}u.washington.edu




This article has been cited by other articles:


Home page
IOVSHome page
K. W. Littink, M. M. van Genderen, R. W. J. Collin, S. Roosing, A. P. M. de Brouwer, F. C. C. Riemslag, H. Venselaar, A. A. H. J. Thiadens, C. B. Hoyng, K. Rohrschneider, et al.
A Novel Homozygous Nonsense Mutation in CABP4 Causes Congenital Cone-Rod Synaptic Disorder
Invest. Ophthalmol. Vis. Sci., May 1, 2009; 50(5): 2344 - 2350.
[Abstract] [Full Text] [PDF]


Home page
IOVSHome page
F. Rieke, A. Lee, and F. Haeseleer
Characterization of Ca2+-Binding Protein 5 Knockout Mouse Retina
Invest. Ophthalmol. Vis. Sci., November 1, 2008; 49(11): 5126 - 5135.
[Abstract] [Full Text] [PDF]



-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2009 by Society for Neuroscience ONLINE ISSN: 1529-2401
-