Work

Permeability transition in human mitochondria persists in the absence of peripheral stalk subunits of ATP synthase

Year: 2017

Type: article

Abstract: Significance Mitochondria generate the cellular fuel ATP to sustain complex life. Production of ATP depends on the oxidation of energy-rich compounds to produce a chemical potential difference for hydrogen ions, the proton motive force (pmf), across the inner mitochondrial membrane (IMM). Disruption of the IMM, dissipation of the pmf, and cell death occur if the concentration of calcium ions inside mitochondria is sufficiently elevated to open a pore in the IMM. The identity of the pore is disputed. One proposal is that the pore is in the enzyme that makes ATP. Here, we show that proteins in the enzyme’s peripheral stalk are not involved in the formation or regulation of the pore.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1711201114

Authors: Jiuya He, Joe Carroll, Shujing Ding, Ian M. Fearnley, John E. Walker

Institutions: University of Cambridge, MRC Mitochondrial Biology Unit, Medical Research Council

Language: English

Topic: ATP Synthase and ATPases Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: Medical Research Council

Awards: Structure, mechanisms, regulation and assembly of ATP synthase, Investigation of the function of the ER/mitochondria contact sites in cell physiology and disease, G7104851454