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Regulation of Drosophila Ca2+/Calmodulin-Dependent Protein Kinase II by Autophosphorylation Analyzed by Site-Directed Mutagenesis by Zheng Wang; Glenn Palmer; Leslie C. Griffith is a Neuroscience article available to read on EtoBox.

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Abstract: In this study we demonstrate that __Drosophila__ calcium/calmodulin‐dependent protein kinase II (CaMKII) is capable of complex regulation by autophosphorylation of the three threonines within its regulatory domain. Specifically, we show that autophosphorylation of threonine‐287 in __Drosophila__ CaMKII is equivalent to phosphorylation of threonine‐286 in rat α CaMKII both in its ability to confer calcium independence on the enzyme and in the mechanistic details of how it becomes phosphorylated. Autophosphorylation of this residue occurs only within the holoenzyme structure and requires calmodulin (CaM) to be bound to the substrate subunit. Phosphorylation of threonine‐306 and threonine‐307 in the CaM binding domain of the __Drosophila__ kinase occurs only in the absence of CaM, and this phosphorylation is capable of inhibiting further CaM binding. Additionally, our findings suggest that phosphorylation of threonine‐306 and threonine‐307 does not mimic bound CaM to alleviate the requirement for CaM binding to the substrate subunit for intermolecular threonine‐287 phosphorylation. These results demonstrate that the mechanism of regulatory autophosphorylation of this kinase

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Author

Zheng Wang; Glenn Palmer; Leslie C. Griffith

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 0022-3042)

Published

1998

Language

EN

Field

Neuroscience (Life Sciences)