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Mitochondrial Protein Sorting

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Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
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Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
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Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70 chaperones are targetted to TOM20-TOM22 receptor complexes.
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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...

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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...

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Related Experiment Video

Updated: May 22, 2026

Mitochondrial Preparation from Microglia for Glycan Analysis

Mitochondrial Preparation from Microglia for Glycan Analysis

Published on: May 30, 2025

Multiple proteins with essential mitochondrial functions have glycosylated isoforms.

Amanda R Burnham-Marusich¹, Patricia M Berninsone

¹Biology Department, University of Nevada Reno, 1664 N. Virginia St., MS-314, Reno, NV 89557, USA. amanda.marusich@gmail.com

|May 9, 2012

Summary

Glycosylation, a common protein modification, is rarely reported in mitochondria. This study found evidence of glycosylated mitochondrial proteins, suggesting a potential regulatory role in mitochondrial and extra-mitochondrial functions.

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Area of Science:

Biochemistry
Molecular Biology
Cellular Biology

Background:

Glycosylation is a common post-translational modification for nucleocytosolic and secreted proteins.
Glycosylated mitochondrial proteins are infrequently reported, suggesting a gap in understanding protein modification within this organelle.

Purpose of the Study:

To investigate the presence and potential significance of glycosylation in mitochondrial proteins.
To explore whether glycosylation impacts mitochondrial protein function or localization.

Main Methods:

Utilized lectin chromatography on bovine heart tissue to isolate and detect glycoproteins.
Focused on identifying low-abundance glycoforms of nuclear-encoded proteins with known mitochondrial functions.

Main Results:

Detected low-abundance glycoforms of key mitochondrial proteins, including pyruvate dehydrogenase E1α, NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, ADP/ATP translocase, ATP synthase d, and oligomycin sensitivity-conferring protein.
Observed that ATP synthase d and oligomycin sensitivity-conferring protein, identified as glycosylated, were also previously detected at the plasma membrane.

Conclusions:

Glycosylation of classical mitochondrial proteins may be more prevalent than previously assumed.
Glycosylation could serve as an uncharacterized regulatory mechanism for mitochondrial proteins, influencing their function both within mitochondria and in extra-mitochondrial locations.