Regulation of Respiration and Apoptosis by Cytochrome c Threonine 58 Phosphorylation

Author:

Wan Junmei,Kalpage Hasini A.,Vaishnav Asmita,Liu Jenney,Lee Icksoo,Mahapatra Gargi,Turner Alice A.,Zurek Matthew P.,Ji Qinqin,Moraes Carlos T.,Recanati Maurice-Andre,Grossman Lawrence I.,Salomon Arthur R.,Edwards Brian F. P.,Hüttemann MaikORCID

Abstract

AbstractCytochromec(Cytc) is a multifunctional protein, acting as an electron carrier in the electron transport chain (ETC), where it shuttles electrons frombc1complex to cytochromecoxidase (COX), and as a trigger of type II apoptosis when released from the mitochondria. We previously showed that Cytcis regulated in a highly tissue-specific manner: Cytcisolated from heart, liver, and kidney is phosphorylated on Y97, Y48, and T28, respectively. Here, we have analyzed the effect of a new Cytcphosphorylation site, threonine 58, which we mapped in rat kidney Cytcby mass spectrometry. We generated and overexpressed wild-type, phosphomimetic T58E, and two controls, T58A and T58I Cytc; the latter replacement is found in human and testis-specific Cytc.In vitro, COX activity, caspase-3 activity, and heme degradation in the presence of H2O2were decreased with phosphomimetic Cytccompared to wild-type. Cytc-knockout cells expressing T58E or T58I Cytcshowed a reduction in intact cell respiration, mitochondrial membrane potential (∆Ψm), ROS production, and apoptotic activity compared to wild-type. We propose that, under physiological conditions, Cytcis phosphorylated, which controls mitochondrial respiration and apoptosis. Under conditions of stress Cytcphosphorylations are lost leading to maximal respiration rates, ∆Ψmhyperpolarization, ROS production, and apoptosis.

Funder

U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

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