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Mitochondrial Protein Posttranslational Modification Analysis

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Cellular metabolism is closely related to the pathophysiology of the disease. As an integral part of normal cellular function, mitochondria are essential for maintaining and regulating the metabolic functions of cells and organs. Mitochondrial dysfunction can lead to a variety of diseases, such as cardiovascular disease, diabetes and metabolic syndrome, neurodegeneration, cancer, and aging. Multiple post-translational protein modifications (PTMs) are located in mitochondria, including phosphorylation, acetylation, and O-GlcNAcylation. These modifications are responsive to nutrient availability and redox conditions, and can act in protein-protein interactions to modify a variety of mitochondrial functions.

Mitochondrial Protein Posttranslational Modification Analysis

Mitochondrial PTM features

  • Recently, the discovery that reversible PTMs of mitochondrial proteins are involved in regulating core metabolic processes has attracted great interest
  • Protein PTMs in mitochondria are abundant and diverse
  • Many mitochondrial PTMs have been found to be involved in mitochondrial energy metabolism, signal transduction pathways, metabolism, autophagy, apoptosis, and tissue response to ischemic injury.

Specific PTMs of mitochondrial proteins

  • Mitochondrial protein phosphorylation

Protein phosphorylation is one of the most well-known PTMs that occur in all domains of life. Increasing evidence suggests that phosphorylation may also play an important role in the regulation of tissue-specific mitochondrial function and pathophysiology.

  • Mitochondrial protein acetylation

Protein acetylation in mitochondria has been found to play an important regulatory role in the regulation of energy metabolism, oxidative stress response, mitophagy, and other mitochondrial processes. Abnormal levels of mitochondrial protein acetylation have been reported to contribute to diseases associated with metabolic inflexibility.

  • Mitochondrial protein O-GlcNAcylation

O-GlcNAcylation is composed of O-linked beta-N-acetylglucosamine (O-GlcNAc) attached to Ser/Thr residues and is nutrient-sensitive and reversible PTM for cell signaling. This modification in mitochondria is as extensive and diverse as phosphorylation and appears to be intricately linked to phosphorylation, playing an interrelated role in pathological states.

With advanced mass spectrometry (MS) system and strong analysis capabilities, Creative Proteomics provides mitochondrial protein modification analysis service. We are committed to helping researchers identify new target proteins and facilitate the discovery and study of mitochondrial protein modification mechanisms.

Our services include the following list, but are not limited to:

Given the fundamental role of mitochondria in cellular energy provision and regulation of cellular metabolic homeostasis and the strong association of mitochondrial dysregulation with the disease, mitochondrial protein modifications may continue to provide clues to functional significance. Our mitochondrial protein modification analysis service can facilitate the discovery of modifiable mitochondrial targets for metabolic modulation therapies. If you need more information? Or want to work with us? Drop us a line and someone from our team will get back to you shortly.


  1. Stram, Amanda R., and R. Mark Payne. "Post-translational modifications in mitochondria: protein signaling in the powerhouse." Cellular and molecular life sciences 73 (2016): 4063-4073.

* For Research Use Only. Not for use in diagnostic procedures.

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