Electrostatic and Hydrophobic Interactions Differentially Tune Membrane Binding Kinetics of the C2 Domain of Protein
نویسندگان
چکیده
Background: The C2 domain is a Ca2 sensor that drives the first step in the activation of conventional PKC isozymes. Results:Hydrophobic interactions drive membrane association and electrostatic interactions drive membrane retention of the C2 domain. Conclusion: The amplitude and location of conventional PKC signaling is controlled by residues in the C2 domain. Significance: Point mutations in the C2 domain are associated with disease.
منابع مشابه
Electrostatic and hydrophobic interactions differentially tune membrane binding kinetics of the C2 domain of protein kinase Cα.
The cellular activation of conventional protein kinase C (PKC) isozymes is initiated by the binding of their C2 domains to membranes in response to elevations in intracellular Ca(2+). Following this C2 domain-mediated membrane recruitment, the C1 domain binds its membrane-embedded ligand diacylglycerol, resulting in activation of PKC. Here we explore the molecular mechanisms by which the C2 dom...
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