PKA Phosphorylates the ATPase Inhibitory Factor 1 and Inactivates Its Capacity to Bind and Inhibit the Mitochondrial H+-ATP Synthase

PKA Phosphorylates the ATPase Inhibitory Factor 1 and Inactivates Its Capacity to Bind and Inhibit the Mitochondrial H+-ATP Synthase

The mitochondrial H+-ATP synthase synthesizes most of cellular ATP requirements by oxidative phosphorylation (OXPHOS). The ATPase Inhibitory Factor 1 (IF1) is known to inhibit the hydrolase activity of the H+-ATP synthase in situations that compromise OXPHOS. Herein, we demonstrate that phosphorylat...

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Bibliographic Details
Main Authors: Javier García-Bermúdez, María Sánchez-Aragó, Beatriz Soldevilla, Araceli del Arco, Cristina Nuevo-Tapioles, José M. Cuezva
Format: Article
Language:English
Published: Elsevier 2015-09-01
Series:Cell Reports
Online Access:http://www.sciencedirect.com/science/article/pii/S2211124715009493

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