What question did this study set out to answer?

To identify the structural and electrostatic features of calmodulin required to activate the catalytic gamma-subunit of phosphorylase kinase.

February 1, 1993Journal of Biological ChemistryOpen Access

Features of calmodulin that are important in the activation of the catalytic subunit of phosphorylase kinase.

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To identify the structural and electrostatic features of calmodulin required to activate the catalytic gamma-subunit of phosphorylase kinase.
Engineered calmodulin mutants by substituting acidic residues with basic lysine residues across the four E-helices of its EF-hand domains.
Assayed the activation kinetics and maximal stimulation of the isolated catalytic gamma-subunit by the mutant calmodulins.
Compared activation properties and substrate kinetic parameters against known calmodulin interactions with myosin light chain kinase and calmodulin-dependent protein kinase II.
All charge-reversal mutations decreased the maximal activation of the isolated gamma-subunit, with the greatest reductions seen in the second and third E-helices (residues 45-47 and 82-84).
Electrostatic interactions distributed across both halves and multiple faces of calmodulin were required for activation.
Calmodulin charge mutations did not exert a major effect on substrate kinetic parameters, differing from observations in other calmodulin-dependent kinases.

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Implication

Biochemical mutagenesis demonstrates electrostatic interactions drive calmodulin activation of the phosphorylase kinase gamma-subunit, indicating a distinct multiregional binding mechanism.

Cite This Study

Farrar et al. (1993) studied this question.

synapsesocial.com/papers/6a92931784954b97993aac75 https://doi.org/10.1016/s0021-9258(18)53588-2

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Implication

Biochemical mutagenesis demonstrates electrostatic interactions drive calmodulin activation of the phosphorylase kinase gamma-subunit, indicating a distinct multiregional binding mechanism.

Features of calmodulin that are important in the activation of the catalytic subunit of phosphorylase kinase.

Key Points

Discussion

Implication

Cite This Study

Features of calmodulin that are important in the activation of the catalytic subunit of phosphorylase kinase.

Key Points

Discussion

Implication

Cite This Study

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