Calmodulin: Structure, Mechanisms and Functions


Vahid Ohme (Editor)

Series: Cell Biology Research Progress
BISAC: SCI017000

In Calmodulin: Structure, Mechanisms and Functions, the authors consider small and poorly-studied groups of plant calcium-dependent protein kinases that directly interact with calmodulin molecules. In plants, Ca2+ activates calmodulin-like domain kinases that do not require calmodulin or phospholipids. Thus these kinases differ from both CaMK and PKC families prevalent in mammalian cells.

Next, various strategies of purification of recombinant proteins using CaM-based purification systems are reviewed and discussed. Protein purification is a crucial process in biotechnology industries and life science research laboratories. Amongst these purification strategies, affinity purification has garnered a lot of attention due to its higher speed and selectivity, leading to enhanced purity in fewer steps.

In the closing chapter, the authors describe atomic-level structures of Ca2+-bound CaM (Ca2+/CaM) bound to the PSD-95 N-terminal domain. The N-lobe of CaM forms a cap that binds to the N-terminus of PSD-95 and sterically blocks the palmitoylation of PSD-95 at Cys3 and Cys5. The CaM C-lobe forms hydrophobic contacts with PSD-95 residue Y12, and the Y12E mutation abolishes Ca2+-induced postsynaptic release of PSD-95.
(Imprint: Nova)


Table of Contents

Table of Contents


Chapter 1. Calmodulin in Action: CaM Protein Kinases as Canonical Targets in Plant Cell
(Pavel A. Karpov, Alla I. Yemets and Yaroslav B. Blume, Institute of Food Biotechnology and Genomics, National Academy of Sciences of Ukraine, Kyiv, Ukraine)

Chapter 2. Calmodulin-Based Recombinant Protein Purification Strategies
(Bidhan Chandra Nayak and Zhiguang Yuchi, School of Pharmaceutical Science and Technology, Tianjin University, Tianjin, China)

Chapter 3. Calmodulin Targeting of the Postsynaptic Density Protein 95 (PSD-95) Triggers Its Postsynaptic Release and Modulates Neuronal Excitability
(James B. Ames, Department of Chemistry, University of California, Davis, CA, US)



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