Journal
BIOMOLECULES
Volume 13, Issue 5, Pages -Publisher
MDPI
DOI: 10.3390/biom13050869
Keywords
post-translational modifications; mitochondria; virus-host interactions; mass spectrometry; proteomics; phosphorylation; acylation
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The regulation of mitochondria structure and function is crucial for viral infections. Post-translational modification of mitochondrial proteins plays a critical role in controlling energy metabolism, apoptosis, and immune signaling. Understanding these modifications and their effects is important for the development of therapeutic strategies.
The regulation of mitochondria structure and function is at the core of numerous viral infections. Acting in support of the host or of virus replication, mitochondria regulation facilitates control of energy metabolism, apoptosis, and immune signaling. Accumulating studies have pointed to post-translational modification (PTM) of mitochondrial proteins as a critical component of such regulatory mechanisms. Mitochondrial PTMs have been implicated in the pathology of several diseases and emerging evidence is starting to highlight essential roles in the context of viral infections. Here, we provide an overview of the growing arsenal of PTMs decorating mitochondrial proteins and their possible contribution to the infection-induced modulation of bioenergetics, apoptosis, and immune responses. We further consider links between PTM changes and mitochondrial structure remodeling, as well as the enzymatic and non-enzymatic mechanisms underlying mitochondrial PTM regulation. Finally, we highlight some of the methods, including mass spectrometry-based analyses, available for the identification, prioritization, and mechanistic interrogation of PTMs.
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