Multiple proteins with essential mitochondrial functions have glycosylated isoforms.

Mitochondrion
Amanda R Burnham-Marusich, Patricia M Berninsone

Abstract

Nucleocytosolic and secreted proteins are commonly glycosylated. However, reports of glycosylated mitochondrial proteins are rare. Using lectin chromatography on bovine heart, we detected low-abundance glycoforms of nuclear-encoded proteins with well-established mitochondrial function: pyruvate dehydrogenase E1α, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, ADP/ATP translocase, ATP synthase d and oligomycin sensitivity-conferring protein. Notably, the latter two have been previously detected at the plasma membrane. Our findings indicate that glycosylation of classic mitochondrial proteins may be more common than previously appreciated. We discuss the implication that glycosylation could represent an unexplored mechanism for regulating these proteins' functions within mitochondria or at extra-mitochondrial locations.

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Citations

Sep 10, 2013·Biochemistry. Biokhimii︠a︡·G Ya Wiederschain
Oct 22, 2013·International Journal of Molecular Sciences·Xiaojin WangLin Liu
May 3, 2014·International Journal of Molecular Sciences·Manuela AntonielGiovanna Lippe
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Jun 23, 2018·Frontiers in Neuroscience·Paula A Q Videira, Margarida Castro-Caldas
Aug 14, 2021·Proceedings of the National Academy of Sciences of the United States of America·Hongjie GuoStephen M Beverley

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