Skip Navigation

Journal of Biochemistry 2005 138(2):177-182; doi:10.1093/jb/mvi107
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Fukunaga, Y.
Right arrow Articles by Miyazawa, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fukunaga, Y.
Right arrow Articles by Miyazawa, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2005 The Japanese Biochemical Society

Regular Paper

The Interaction between PSD-95 and Ca2+/Calmodulin Is Enhanced by PDZ-Binding Proteins

Yuko Fukunaga1, Mamoru Matsubara2, Rina Nagai1 and Atsuo Miyazawa1,*

1 Membrane Dynamics Project, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki, Sayo, Hyogo 679-5148; and 2 Carna Biosciences Incorporation, KIBC 511, 5-5-2 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047

* To whom correspondence should be addressed. Tel: +81-791-58-1825, Fax: +81-791-58-1826, E-mail: atsuo{at}spring8.or.jp

In this study, we evaluate the interaction between the postsynaptic scaffolding protein, PSD-95, and calmodulin. Surface plasmon resonance spectroscopy was used to characterize the binding of PSD-95 to calmodulin that had been immobilized on a sensor chip. Additionally, soluble calmodulin was found to inhibit the binding of PSD-95 to immobilized calmodulin. The HOOK region of PSD-95, which is located between the src homology 3 domain and the guanylate kinase–like domain, was determined to be involved in the binding of PSD-95 to calmodulin. We also found that C-terminal peptides from proteins such as CRIPT and the N-methyl-d-aspartate receptor NR2B subunit, which associate with the PDZ domain of PSD-95, enhanced the affinity of PSD-95 for calmodulin. The binding of ligands to the PDZ domain may change the conformation of PSD-95 and affect the interaction between PSD-95 and calmodulin.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
R. A. Newman and K. E. Prehoda
Intramolecular Interactions Between the Src Homology 3 Guanylate Kinase Domains of Discs Large Regulate Its Function in Asymmetric Cell Division
J. Biol. Chem., May 8, 2009; 284(19): 12924 - 12932.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.