Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...

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...

Porin Insertion in the Outer Mitochondrial Membrane

Porin Insertion in the Outer Mitochondrial Membrane

Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...

Structure of Porins

Structure of Porins

Mitochondria, chloroplasts, and gram-negative bacteria have transmembrane, beta-barrel proteins called porins to mediate the free diffusion of ions and metabolites across the membrane. Mitochondrial porin precursors contain conserved amino acid sequences called beta signals at their C-terminal. Beta signals have a motif of PoXGXXHyXHy (Po-Polar, X-Any amino acid, G-Glycine, Hy-LargeHydrophobic), which are crucial for precursor recognition to initiate precursor assembly. Beta-barrel...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Plasma Metabolomics Reveals a Shared Metabolomic Profile in Experimental and Human Chronic Kidney Disease.

Toxins·2026

Same author

Dual pharmacological targeting of coactivator-associated arginine methyltransferase 1 (CARM1) and salt inducible kinase (SIK) drives ketogenesis in both hepatocytes and mice.

British journal of pharmacology·2026

Same author

Impaired insulin signaling limits osteogenic potential of bone marrow stromal cells in type 2 diabetes.

European journal of endocrinology·2026

Same author

Reshaping the progranulin/sortilin interaction for targeted degradation of extracellular proteins.

Cell chemical biology·2026

Same author

Energy metabolism alteration and gene expression reprogramming in a cell model of high fat load non-alcoholic fatty liver disease.

BMC gastroenterology·2026

Same author

Restoration of Interaction Between Fatty Acid Oxidation and Electron Transport Chain Proteins In Vitro by Addition of Recombinant VLCAD.

Biomedicines·2026

Search research articles

Related Experiment Video

Updated: Mar 17, 2026

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Published on: June 2, 2023

Proteomics of human mitochondria.

Johan Palmfeldt¹, Peter Bross¹

¹Research Unit for Molecular Medicine, Department of Clinical Medicine, Aarhus University and Aarhus University Hospital, Palle Juul-Jensens Boulevard 99, DK-8200 Aarhus, Denmark.

|July 23, 2016

Summary

Mitochondrial proteomics, using advanced mass spectrometry, reveals insights into human diseases and aging. New methods improve analysis of limited human samples, aiding disease modeling and research.

Keywords:

Mass spectrometry Mitochondrial diseases Mitochondrial medicine Mitochondrial proteins Proteomics

More Related Videos

Preparation of Mitochondria from Ovarian Cancer Tissues and Control Ovarian Tissues for Quantitative Proteomics Analysis

Preparation of Mitochondria from Ovarian Cancer Tissues and Control Ovarian Tissues for Quantitative Proteomics Analysis

Published on: November 18, 2019

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Related Experiment Videos

Last Updated: Mar 17, 2026

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Author Spotlight: Two-Step Tag-Free Isolation of Mitochondria for Improved Protein Discovery and Quantification

Published on: June 2, 2023

Preparation of Mitochondria from Ovarian Cancer Tissues and Control Ovarian Tissues for Quantitative Proteomics Analysis

Preparation of Mitochondria from Ovarian Cancer Tissues and Control Ovarian Tissues for Quantitative Proteomics Analysis

Published on: November 18, 2019

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Measurement of Protein Import Capacity of Skeletal Muscle Mitochondria

Published on: January 7, 2022

Area of Science:

Biochemistry
Molecular Biology
Genomics

Background:

Mitochondria are crucial in cellular function and disease pathogenesis.
Proteomics has advanced significantly with sensitive mass spectrometry.
Mitochondrial dysfunction is implicated in aging and various diseases.

Purpose of the Study:

To review recent progress in human mitochondrial proteomics.
To discuss challenges and advancements in analyzing human samples.
To highlight the role of proteomics in understanding mitochondrial disease.

Main Methods:

Advanced mass spectrometry techniques for protein identification and quantification.
Bioinformatics and database utilization for proteomic data analysis.
Development of patient-specific cellular models using induced pluripotent stem cells.

Main Results:

Catalog of human mitochondrial proteins is expanding.
Proteins with dual localization are identified.
Proteomic analyses link mitochondrial proteins to inherited and complex diseases.

Conclusions:

Proteomics is vital for understanding mitochondrial roles in health and disease.
Technological advancements are overcoming sample limitations.
Future research will leverage proteomics for novel therapeutic strategies.