The protein calmodulin (CaM) is essential to cell development and adaptation. Although CaM is known for regulating protein targets in a calcium-dependent manner, its function is modulated by post-translational modifications (PTMs). As such, CaM integrates myriad signaling pathways utilized by cells. To better understand the molecular bases of CaM's target regulation, we developed a molecular simulation protocol for generating its complexes with calcineurin, a phosphatase. Importantly, our simulation data suggest that CaM utilizes its solvent-exposed surface to activate calcineurin, in addition to recognizing the canonical calmodulin-binding motifs. PTMs may in turn modify how CaM's solvent-exposed surface interfaces its targets. These findings provide insights into molecular mechanisms of signaling driven by CaM/target interactions.

Mechanisms of calmodulin-dependent activation of myofilament targets

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.