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  Formation of complexes between Ca2+center dot calmodulin and the synapse-associated protein SAP97 requires the SH3 domain- guanylate kinase domain-connecting HOOK region

Paarmann, I., Spangenberg, O., Lavie, A., & Konrad, M. (2002). Formation of complexes between Ca2+center dot calmodulin and the synapse-associated protein SAP97 requires the SH3 domain- guanylate kinase domain-connecting HOOK region. Journal of Biological Chemistry, 277(43), 40832-40838. Retrieved from http://www.jbc.org/content/277/43/40832.full.pdf+html.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F2B5-F Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E234-4
Genre: Journal Article

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Paarmann, I., Author
Spangenberg, O.1, Author              
Lavie, A., Author
Konrad, M.2, Author              
Affiliations:
1Department of Molecular Genetics, MPI for biophysical chemistry, Max Planck Society, ou_578622              
2Research Group of Enzyme Biochemistry, MPI for biophysical chemistry, Max Planck Society, ou_578612              

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 Abstract: Mammalian synapse-associated protein SAP97, a structural and functional homolog of Drosophila Dlg, is a membrane-associated guanylate kinase (MAGUK) that is present at pre- and postsynaptic sites as well as in epithelial cell-cell contact sites. It is a multidomain scaffolding protein that shares with other members of the MAGUK protein family a characteristic modular organization composed of three sequential protein interaction motifs known as PDZ domains, followed by an Sre homology 3 (SH3) domain, and an enzymatically inactive guanylate kinase (GK)-like domain. Specific binding partners are known for each domain, and different modes of intramolecular interactions have been proposed that particularly involve the SH3 and GK domains and the so-called HOOK region located between these two domains. We identified the HOOK region as a specific site for calmodulin binding and studied the dynamics of complex formation of recombinant calmodulin and SAP97 by surface plasmon resonance spectroscopy. Binding of various SAP97 deletion constructs to immobilized calmodulin was strictly calcium-dependent. From the rate constants of association and dissociation we determined an equilibrium dissociation constant K-d of 122 nM for the association of calcium-saturated calmodulin and a SAP97 fragment, which encompassed the entire SH3-HOOK-GK module. Comparative structure-based sequence analysis of calmodulin binding regions from various target proteins predicts variable affinities for the interaction of calmodulin with members of the MAGUK protein family. Our findings suggest that calmodulin could regulate the intramolecular interaction between the SH3, HOOK, and GK domains of SAP97.

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Language(s): eng - English
 Dates: 2002-10-25
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 277 (43) Sequence Number: - Start / End Page: 40832 - 40838 Identifier: -