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Journal Article

Presynaptic Calmodulin targets: lessons from structural proteomics

MPS-Authors

Lipstein,  Noa
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Göth,  Melanie
Molecular Physics, Fritz Haber Institute, Max Planck Society;
Free University Berlin;

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Pagel,  Kevin
Molecular Physics, Fritz Haber Institute, Max Planck Society;

Jahn,  Olaf
Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Lipstein, N., Göth, M., Piotrowski, C., Pagel, K., Sinz, A., & Jahn, O. (2017). Presynaptic Calmodulin targets: lessons from structural proteomics. Expert Review of Proteomics, 14(3), 223-242. doi:10.1080/14789450.2017.1275966.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002D-2B1E-9
Abstract
Introduction: Calmodulin (CaM) is a highly conserved Ca2+-binding protein that is exceptionally abundant in the brain. In the presynaptic compartment of neurons, CaM transduces changes in Ca2+ concentration into the regulation of synaptic transmission dynamics. Areas covered: We review selected literature including published CaM interactor screens and outlineestablished and candidate presynaptic CaM targets. We present a workflow of biochemical andstructural proteomic methods that were used to identify and characterize the interactions between CaM and Munc13 proteins. Finally, we outline the potential of ion mobility-mass spectrometry (IM-MS) for conformational screening and of protein-protein cross-linking for the structural characterization of CaM complexes. Expert commentary: Cross-linking/MS and native MS can be applied with considerable throughput to protein mixtures under near-physiological conditions, and thus effectively complement high-resolution structural biology techniques. Experimental distance constraints are applicable best when obtained by combining different cross-linking strategies, i.e. by using cross-linkers with different spacer length and reactivity, and by using the incorporation of unnatural photo-reactive amino acids. Insights from structural proteomics can be used to generate CaM-insensitive mutants of CaM targets for functional studies in vitro or ideally in vivo.