Cyclic AMP-dependent Protein Kinase Phosphorylation of Drp1 Regulates Its GTPase Activity and Mitochondrial Morphology

• Published in: The Journal of biological chemistry Vol. 282; no. 30; pp. 21583 - 21587
• Main Authors: Chang, Chuang-Rung, Blackstone, Craig
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 27.07.2007; American Society for Biochemistry and Molecular Biology
• Subjects: Cyclic AMP-Dependent Protein Kinases - genetics; Cyclic AMP-Dependent Protein Kinases - metabolism; Dynamins; Glutathione Transferase - metabolism; GTP Phosphohydrolases - chemistry; GTP Phosphohydrolases - genetics; GTP Phosphohydrolases - metabolism; HeLa Cells; Humans; Microtubule-Associated Proteins - chemistry; Microtubule-Associated Proteins - genetics; Microtubule-Associated Proteins - metabolism; Mitochondria - ultrastructure; Mitochondrial Proteins - chemistry; Mitochondrial Proteins - genetics; Mitochondrial Proteins - metabolism; Mutation; Phosphopeptides - chemistry; Phosphorylation; Phosphoserine - metabolism; Recombinant Fusion Proteins - isolation & purification; Recombinant Fusion Proteins - metabolism; Sequence Deletion

Mitochondria in cells comprise a tubulovesicular reticulum shaped by dynamic fission and fusion events. The multimeric dynamin-like GTPase Drp1 is a critical protein mediating mitochondrial division. It harbors multiple motifs including GTP-binding, middle, and GTPase effector (GED) domains that are...