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Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...

Mitochondrial Protein Sorting

Mitochondrial Protein Sorting

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.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...

The Inner Mitochondrial Membrane

The Inner Mitochondrial Membrane

The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria. In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...

Mitochondrial Precursor Proteins

Mitochondrial Precursor Proteins

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.
Most of the mitochondrial...

Energy to Drive Translocation

Energy to Drive Translocation

Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...

Protein Transport into the Inner Mitochondrial Membrane

Protein Transport into the Inner Mitochondrial Membrane

Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...

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Related Experiment Video

Updated: Mar 16, 2026

Rapid Isolation of the Mitoribosome from HEK Cells

Rapid Isolation of the Mitoribosome from HEK Cells

Published on: October 4, 2018

PARL: The mitochondrial rhomboid protease.

Marco Spinazzi¹, Bart De Strooper²

¹VIB Center for the Biology of Disease, O&N4 Herestraat 49 box 602, 3000, Leuven, Belgium; KU Leuven Center for Human Genetics, O&N4 Herestraat 49 box 602, 3000, Leuven, Belgium.

Seminars in Cell & Developmental Biology

|August 10, 2016

Summary

The rhomboid family protein PARL is crucial for cell homeostasis. This review examines PARL

Keywords:

Cell death Metabolism Mitochondria PARL Protease Rhomboid

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Last Updated: Mar 16, 2026

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Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

The rhomboid family consists of evolutionarily conserved intramembrane proteases.
Mitochondrion-localized rhomboid (PARL in mammals) is vital for cellular homeostasis.
Genetic ablation of PARL leads to severe phenotypes across species.

Purpose of the Study:

To review the functions and substrates of PARL and its orthologues.
To highlight controversies and uncertainties regarding PARL's roles.
To discuss PARL's potential involvement in diseases like type II diabetes and Parkinson's disease.

Main Methods:

Literature review of existing studies on PARL and its orthologues.
Analysis of proposed substrates and their biological relevance.
Comparative analysis across different species (mammals, yeast, Drosophila).

Main Results:

Several substrates have been proposed for PARL, but significant controversy remains.
PARL's precise functions and mechanisms of action are not fully elucidated.
Evidence suggests a conserved role for PARL in maintaining mitochondrial function and cell viability.

Conclusions:

PARL and its orthologues are essential for cell homeostasis.
Further research is needed to resolve controversies surrounding PARL substrates and functions.
PARL may represent a therapeutic target for neurodegenerative and metabolic diseases.