140 mouse brain proteins identified by Ca2+-calmodulin affinity chromatography and tandem mass spectrometry.

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Abstract

Calmodulin is an essential Ca2+-binding protein that binds to a variety of targets that carry out critical signaling functions. We describe the proteomic characterization of mouse brain Ca2+-calmodulin-binding proteins that were purified using calmodulin affinity chromatography. Proteins in the eluates from four different affinity chromatography experiments were identified by 1-DE and in-gel digestion followed by LC-MS/MS. Parallel experiments were performed using two related control-proteins belonging to the EF-hand family. After comparing the results from the different experiments, we were able to exclude a significant number of proteins suspected to bind in a nonspecific manner. A total of 140 putative Ca2+-calmodulin-binding proteins were identified of which 87 proteins contained calmodulin-binding motifs. Among the 87 proteins that contained calmodulin-binding motifs, 48 proteins have not previously been shown to interact with calmodulin and 39 proteins were known calmodulin-binding proteins. Many proteins with ill-defined functions were identified as well as a number of proteins that at the time of the analysis were described only as ORFs. This study provides a functional framework for studies on these previously uncharacterized proteins.

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Subject classification (UKÄ) – MANDATORY

  • Basic Medicine

Keywords

  • calcium, protein-protein interactions, calmodulin, proteomics, brain
Original languageEnglish
Pages (from-to)669-687
JournalJournal of Proteome Research
Volume5
Issue number3
Publication statusPublished - 2006
Publication categoryResearch
Peer-reviewedYes