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The ADP/ATP Carrier Protein

The ADP/ATP Carrier Protein

ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...

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...

Electron Carriers

Electron Carriers

Electron carriers can be thought of as electron shuttles. These compounds can easily accept electrons (i.e., be reduced) or lose them (i.e., be oxidized). They play an essential role in energy production because cellular respiration is contingent on the flow of electrons.
Over the many stages of cellular respiration, glucose breaks down into carbon dioxide and water. Electron carriers pick up electrons lost by glucose in these reactions, temporarily storing and releasing them into the electron...

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...

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...

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,...

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Related Experiment Video

Updated: Jun 22, 2026

Fingerprinting Cardiolipin in Leukocytes by Mass Spectrometry for a Rapid Diagnosis of Barth Syndrome

Fingerprinting Cardiolipin in Leukocytes by Mass Spectrometry for a Rapid Diagnosis of Barth Syndrome

Published on: March 23, 2022

Cardiolipin and mitochondrial carriers.

Martin Klingenberg¹

¹Institut für Physiologische Chemie der Universität München, Germany. Klingenberg@med.uni-muenchen.de

Biochimica Et Biophysica Acta

|June 23, 2009

Summary

Cardiolipin (CL) stabilizes mitochondrial carriers like the ADP/ATP carrier (AAC). Disrupting CL binding to AAC impacts mitochondrial function and cell death, highlighting AAC

Area of Science:

Mitochondrial biology
Biochemistry
Cellular physiology

Background:

Cardiolipin (CL) is crucial for mitochondrial carrier protein function and stability.
The ADP/ATP carrier (AAC) is a key mitochondrial transporter that interacts with CL.

Purpose of the Study:

To elucidate the functional and structural roles of cardiolipin (CL) in mitochondrial carrier proteins, particularly the ADP/ATP carrier (AAC).
To investigate the implications of CL binding to AAC in cellular processes like energy transfer and cell death.

Main Methods:

Functional assays in reconstituted vesicles.
Structural analysis using crystallography (CAT-AAC complex).
Spectroscopic techniques including (31)P NMR and ESR for CL binding dynamics.

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Main Results:

CL stabilizes isolated carriers and is essential for transport in reconstituted systems.
AAC binds CL in a graded manner, with structural data showing peripheral CL binding.
CL binding to AAC is linked to energy transfer and can be disrupted by Ca(++) or oxidants, influencing mitochondrial pore transition (MPT) and cell death.
Uncoupling protein 1 (UCP1) shows differential CL binding compared to AAC, suggesting regulatory roles.

Conclusions:

Cardiolipin plays a vital, multifaceted role in the structure and function of mitochondrial carriers, especially AAC.
The interaction between CL and AAC is critical for maintaining mitochondrial integrity and energy homeostasis.
Dysregulation of CL binding to AAC has significant implications for cell fate and mitochondrial dysfunction.