Authors

Gargi Mahapatra, Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine
Ashwathy Varughese, Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine
Qinqin Ji, Chemistry Department, Brown University
Icksoo Lee, Center for Molecular Medicine and Genetics, Wayne State University School of Medicine
Jenney Liu, Center for Molecular Medicine and Genetics, Wayne State University School of Medicine
Asmita Vaishnav, Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine
Christopher Sinkler, Center for Molecular Medicine and Genetics, Wayne State University School of Medicine
Alexandr A. Kapralov, Center for Free Radical and Antioxidant Health, University of Pittsburgh
Carlos T. Moraes, Department of Neurology, University of Miami Schoool of Medicine
Thomas H. Sanderson, Department of Emergency Medicine, Wayne State University School of Medicine
Timothy L. Stemmler, Department of Pharmaceutical Sciences, Wayne State University School of Medicine
Lawrence I. Grossman, Center for Molecular Medicine and Genetics, Wayne State University School of Medicine
Valerian E. Kagan, Center for Free Radical and Antioxidant Health, University of Pittsburgh
Joseph S. Brunzelle, Life Sciences Collaborative Access Team, Northwestern University, Center for Synchrotron Research
Arthur R. Salomon, Life Sciences Collaborative Access Team, Northwestern University, Center for Synchrotron Research
Brian FP Edwards, Department of Biochemistry and Molecular Biology, Wayne State University School of MedicineFollow
Maik Hüttemann, Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine

Document Type

Article

Abstract

Mammalian cytochrome c (Cytc) plays a key role in cellular life and death decisions, functioning as an electron carrier in the electron transport chain and as a trigger of apoptosis when released from the mitochondria. However, its regulation is not well understood. We show that the major fraction of Cytc iso- lated from kidneys is phosphorylated on Thr28, leading to a par- tial inhibition of respiration in the reaction with cytochrome c oxidase. To further study the effect of Cytc phosphorylation in vitro, we generated T28E phosphomimetic Cytc, revealing supe- rior behavior regarding protein stability and its ability to degrade reactive oxygen species compared with wild-type un- phosphorylated Cytc. Introduction of T28E phosphomimetic Cytc into Cytc knock-out cells shows that intact cell respiration, mitochondrial membrane potential (����m), and ROS levels are reduced compared with wild type. As we show by high resolu- tion crystallography of wild-type and T28E Cytc in combination with molecular dynamics simulations, Thr28 is located at a cen- tral position near the heme crevice, the most flexible epitope of the protein apart from the N and C termini. Finally, in silico prediction and our experimental data suggest that AMP kinase, which phosphorylates Cytc on Thr28 in vitro and colocalizes with Cytc to the mitochondrial intermembrane space in the kid- ney, is the most likely candidate to phosphorylate Thr28 in vivo. We conclude that Cytc phosphorylation is mediated in a tissue- specific manner and leads to regulation of electron transport chain flux via “controlled respiration,” preventing ����m hyperpolarization, a known cause of ROS and trigger of apoptosis.

Disciplines

Biochemistry | Molecular Biology

Comments

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