Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of Brain Injury

Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of... Mitochondria are complex organelles that undergo constant fusion and fission in order to adapt to the ever-changing cellular environment. The fusion/fission proteins, localized in the inner and outer mitochondrial membrane, play critical roles under pathological conditions such as acute brain injury and neurodegenerative diseases. Post-translational modifications of these proteins tightly regulate their function and activity, ultimately impacting mitochondrial dynamics and their efficiency to generate ATP. The individual post-translational modifications that are known to affect mitochondrial dynamics include SUMOylation, ubiquitination, phosphorylation, S-nitrosylation, acetylation, O-linked N-acetyl-glucosamine glycosylation, ADP-ribosylation, and proteolytic cleavage. Under stress or pathologic conditions, several of these modifications are activated leading to a complex regulatory mechanism that shifts the state of the mitochondrial network. The main goal is to accommodate and adapt the cellular bioenergetics metabolism to the energetic demand of the new extra- and/or intracellular environment. Understanding the complex relationship between these modifications on fusion and fission proteins in particular pathologic stress or diseases can provide new promising therapeutic targets and treatment approaches. Here, we discuss the specific post-translational modifications of mitochondrial fusion/fission proteins under pathologic conditions and their impact on mitochondrial dynamics. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Translational Stroke Research Springer Journals

Significance of Mitochondrial Protein Post-translational Modifications in Pathophysiology of Brain Injury

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Publisher
Springer US
Copyright
Copyright © 2017 by Springer Science+Business Media, LLC
Subject
Biomedicine; Neurosciences; Neurology; Cardiology; Neurosurgery; Vascular Surgery
ISSN
1868-4483
eISSN
1868-601X
D.O.I.
10.1007/s12975-017-0569-8
Publisher site
See Article on Publisher Site

Abstract

Mitochondria are complex organelles that undergo constant fusion and fission in order to adapt to the ever-changing cellular environment. The fusion/fission proteins, localized in the inner and outer mitochondrial membrane, play critical roles under pathological conditions such as acute brain injury and neurodegenerative diseases. Post-translational modifications of these proteins tightly regulate their function and activity, ultimately impacting mitochondrial dynamics and their efficiency to generate ATP. The individual post-translational modifications that are known to affect mitochondrial dynamics include SUMOylation, ubiquitination, phosphorylation, S-nitrosylation, acetylation, O-linked N-acetyl-glucosamine glycosylation, ADP-ribosylation, and proteolytic cleavage. Under stress or pathologic conditions, several of these modifications are activated leading to a complex regulatory mechanism that shifts the state of the mitochondrial network. The main goal is to accommodate and adapt the cellular bioenergetics metabolism to the energetic demand of the new extra- and/or intracellular environment. Understanding the complex relationship between these modifications on fusion and fission proteins in particular pathologic stress or diseases can provide new promising therapeutic targets and treatment approaches. Here, we discuss the specific post-translational modifications of mitochondrial fusion/fission proteins under pathologic conditions and their impact on mitochondrial dynamics.

Journal

Translational Stroke ResearchSpringer Journals

Published: Sep 21, 2017

References

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