On the mechanism and functional significance of the ADP/ATP carrier (AAC) dimerization

Moiseeva, Vera; Murugova, T. N.; Vangeli, I. M.; Byvshev, I. M.; Ravaud, Stéphanie; Simonyan, Ruben A.; Gordeliy, Valentin; Pebay‐Peyroula, Eva; Yaguzhinsky, L. S.

doi:10.1134/s1990747817040079

Cited by 1 publication

(2 citation statements)

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“…More specifically, among proton transporters of the MCF, there has not been a consensus on the functional molecular forms of AAC [21][22][23], UCP [11,18,21,24] and phosphate carrier (PIC) [20,21,25]. It has been suggested that AAC forms either a monomer [21] or a dimer [22], or both [26] in the membrane. Out of six molecules of cardiolipin (CL) that are bound to subunits of dimeric AAC, two are thought to sit at the dimer interface and act as a "glue" between the monomeric subunits [22].…”

Section: Structure Of Mcf Membersmentioning

confidence: 99%

“…Furthermore, it has been suggested that CL might have a role in cross-talk between AAC subunits in the dimer [22]. Moiseeva et al [26] showed that external factors (such as tonicity of the mitochondria or incubation at 4 • C) can influence the oligomerization of AAC [26]. PICs are also proposed to function either as a monomer [21] or dimer [25].…”

Section: Structure Of Mcf Membersmentioning

confidence: 99%

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Uncoupling Proteins and Regulated Proton Leak in Mitochondria

Ardalan

Smith

Jelokhani-Niaraki

2022

IJMS

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Higher concentration of protons in the mitochondrial intermembrane space compared to the matrix results in an electrochemical potential causing the back flux of protons to the matrix. This proton transport can take place through ATP synthase complex (leading to formation of ATP) or can occur via proton transporters of the mitochondrial carrier superfamily and/or membrane lipids. Some mitochondrial proton transporters, such as uncoupling proteins (UCPs), transport protons as their general regulating function; while others are symporters or antiporters, which use the proton gradient as a driving force to co-transport other substrates across the mitochondrial inner membrane (such as phosphate carrier, a symporter; or aspartate/glutamate transporter, an antiporter). Passage (or leakage) of protons across the inner membrane to matrix from any route other than ATP synthase negatively impacts ATP synthesis. The focus of this review is on regulated proton transport by UCPs. Recent findings on the structure and function of UCPs, and the related research methodologies, are also critically reviewed. Due to structural similarity of members of the mitochondrial carrier superfamily, several of the known structural features are potentially expandable to all members. Overall, this report provides a brief, yet comprehensive, overview of the current knowledge in the field.

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