Faculty Opinions recommendation of The mimivirus genome encodes a mitochondrial carrier that transports dATP and dTTP.

2007 ◽  
Author(s):  
Eduardo Rial
Keyword(s):  
Mitochondrial Carrier

scholarly journals Antioxidant Synergy of Mitochondrial Phospholipase PNPLA8/iPLA2γ with Fatty Acid–Conducting SLC25 Gene Family Transporters

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 678
Author(s):  
Martin Jabůrek ◽  
Pavla Průchová ◽  
Blanka Holendová ◽  
Alexander Galkin ◽  
Petr Ježek
Keyword(s):  
Lipid Peroxidation ◽  
Unsaturated Fatty Acids ◽  
Second Messengers ◽  
Redox Status ◽  
Mitochondrial Uncoupling ◽  
Mitochondrial Carrier ◽  
Mitochondrial Superoxide ◽  
Redox Activation ◽  
Mitochondrial Carrier Family ◽  
Alternatively Activated

Patatin-like phospholipase domain-containing protein PNPLA8, also termed Ca2+-independent phospholipase A2γ (iPLA2γ), is addressed to the mitochondrial matrix (or peroxisomes), where it may manifest its unique activity to cleave phospholipid side-chains from both sn-1 and sn-2 positions, consequently releasing either saturated or unsaturated fatty acids (FAs), including oxidized FAs. Moreover, iPLA2γ is directly stimulated by H2O2 and, hence, is activated by redox signaling or oxidative stress. This redox activation permits the antioxidant synergy with mitochondrial uncoupling proteins (UCPs) or other SLC25 mitochondrial carrier family members by FA-mediated protonophoretic activity, termed mild uncoupling, that leads to diminishing of mitochondrial superoxide formation. This mechanism allows for the maintenance of the steady-state redox status of the cell. Besides the antioxidant role, we review the relations of iPLA2γ to lipid peroxidation since iPLA2γ is alternatively activated by cardiolipin hydroperoxides and hypothetically by structural alterations of lipid bilayer due to lipid peroxidation. Other iPLA2γ roles include the remodeling of mitochondrial (or peroxisomal) membranes and the generation of specific lipid second messengers. Thus, for example, during FA β-oxidation in pancreatic β-cells, H2O2-activated iPLA2γ supplies the GPR40 metabotropic FA receptor to amplify FA-stimulated insulin secretion. Cytoprotective roles of iPLA2γ in the heart and brain are also discussed.

scholarly journals The mitochondrial carrier SFXN1 is critical for complex III integrity and cellular metabolism

Cell Reports ◽  
2021 ◽  
Vol 34 (11) ◽  
pp. 108869
Author(s):  
Michelle Grace Acoba ◽  
Ebru S. Selen Alpergin ◽  
Santosh Renuse ◽  
Lucía Fernández-del-Río ◽  
Ya-Wen Lu ◽  
...  
Keyword(s):  
Cellular Metabolism ◽  
Complex Iii ◽  
Mitochondrial Carrier

Thermoregulation: What Role for UCPs in Mammals and Birds?

2005 ◽  
Vol 25 (3-4) ◽  
pp. 227-249 ◽  
Author(s):  
Julien Mozo ◽  
Yalin Emre ◽  
Frederic Bouillaud ◽  
Daniel Ricquier ◽  
Francois Criscuolo
Keyword(s):  
Adipose Tissue ◽  
Heat Generation ◽  
Cold Exposure ◽  
Mitochondrial Respiration ◽  
Physiological Function ◽  
Mitochondrial Carrier ◽  
Brown Adipose ◽  
Mitochondrial Carrier Family ◽  
Cell Energy ◽  
Avian Ucp

Mammals and birds are endotherms and respond to cold exposure by the means of regulatory thermogenesis, either shivering or non-shivering. In this latter case, waste of cell energy as heat can be achieved by uncoupling of mitochondrial respiration. Uncoupling proteins, which belong to the mitochondrial carrier family, are able to transport protons and thus may assume a thermogenic function. The mammalian UCP1 physiological function is now well understood and gives to the brown adipose tissue the capacity for heat generation. But is it really the case for its more recently discovered isoforms UCP2 and UCP3? Additionally, whereas more and more evidence suggests that non-shivering also exists in birds, is the avian UCP also involved in response to cold exposure? In this review, we consider the latest advances in the field of UCP biology and present putative functions for UCP1 homologues.

scholarly journals Presence of a Member of the Mitochondrial Carrier Family in Hydrogenosomes: Conservation of Membrane-Targeting Pathways between Hydrogenosomes and Mitochondria

2000 ◽  
Vol 20 (7) ◽  
pp. 2488-2497 ◽  
Author(s):  
Sabrina D. Dyall ◽  
Carla M. Koehler ◽  
Maria G. Delgadillo-Correa ◽  
Peter J. Bradley ◽  
Evelyn Plümper ◽  
...  
Keyword(s):  
Trichomonas Vaginalis ◽  
Protein Targeting ◽  
Phylogenetic Analyses ◽  
Eukaryotic Cell ◽  
Membrane Targeting ◽  
Carrier Proteins ◽  
Mitochondrial Carrier ◽  
Mitochondrial Carrier Family ◽  
Targeting Signal ◽  
Mitochondrial Carrier Proteins

ABSTRACT A number of microaerophilic eukaryotes lack mitochondria but possess another organelle involved in energy metabolism, the hydrogenosome. Limited phylogenetic analyses of nuclear genes support a common origin for these two organelles. We have identified a protein of the mitochondrial carrier family in the hydrogenosome ofTrichomonas vaginalis and have shown that this protein, Hmp31, is phylogenetically related to the mitochondrial ADP-ATP carrier (AAC). We demonstrate that the hydrogenosomal AAC can be targeted to the inner membrane of mitochondria isolated from Saccharomyces cerevisiae through the Tim9-Tim10 import pathway used for the assembly of mitochondrial carrier proteins. Conversely, yeast mitochondrial AAC can be targeted into the membranes of hydrogenosomes. The hydrogenosomal AAC contains a cleavable, N-terminal presequence; however, this sequence is not necessary for targeting the protein to the organelle. These data indicate that the membrane-targeting signal(s) for hydrogenosomal AAC is internal, similar to that found for mitochondrial carrier proteins. Our findings indicate that the membrane carriers and membrane protein-targeting machinery of hydrogenosomes and mitochondria have a common evolutionary origin. Together, they provide strong evidence that a single endosymbiont evolved into a progenitor organelle in early eukaryotic cells that ultimately give rise to these two distinct organelles and support the hydrogen hypothesis for the origin of the eukaryotic cell.

Computational studies of the mitochondrial carrier family SLC25. Present status and future perspectives

2021 ◽  
Vol 0 (0) ◽  
Author(s):  
Andrea Pasquadibisceglie ◽  
Fabio Polticelli
Keyword(s):  
Transport Mechanism ◽  
Experimental Studies ◽  
Intermembrane Space ◽  
Mitochondrial Carrier ◽  
Mitochondrial Homeostasis ◽  
The Matrix ◽  
Mitochondrial Carrier Family ◽  
Mitochondrial Intermembrane Space ◽  
Computational Analyses

Abstract The members of the mitochondrial carrier family, also known as solute carrier family 25 (SLC25), are transmembrane proteins involved in the translocation of a plethora of small molecules between the mitochondrial intermembrane space and the matrix. These transporters are characterized by three homologous domains structure and a transport mechanism that involves the transition between different conformations. Mutations in regions critical for these transporters’ function often cause several diseases, given the crucial role of these proteins in the mitochondrial homeostasis. Experimental studies can be problematic in the case of membrane proteins, in particular concerning the characterization of the structure–function relationships. For this reason, computational methods are often applied in order to develop new hypotheses or to support/explain experimental evidence. Here the computational analyses carried out on the SLC25 members are reviewed, describing the main techniques used and the outcome in terms of improved knowledge of the transport mechanism. Potential future applications on this protein family of more recent and advanced in silico methods are also suggested.

scholarly journals The calcium-dependent ATP-Mg/Pi mitochondrial carrier is a target of glucose-induced calcium signalling in Saccharomyces cerevisiae

2005 ◽  
Vol 392 (3) ◽  
pp. 537-544 ◽  
Author(s):  
Santiago Cavero ◽  
Javier Traba ◽  
Araceli Del Arco ◽  
Jorgina Satrústegui
Keyword(s):  
Calcium Binding ◽  
Mitochondrial Protein ◽  
Calcium Signalling ◽  
Cytosolic Calcium ◽  
Calcium Signal ◽  
Transport Activity ◽  
Wild Type ◽  
Binding Motifs ◽  
Mitochondrial Carrier ◽  
Calcium Dependent

Sal1p is a mitochondrial protein that belongs to the SCaMC (short calcium-binding mitochondrial carrier) subfamily of mitochondrial carriers. The presence of calcium-binding motifs facing the extramitochondrial space allows the regulation of the transport activity of these carriers by cytosolic calcium and provides a new mechanism to transduce calcium signals in mitochondria without the requirement of calcium entry in the organelle. We have studied its transport activity, finding that it is a carboxyatractyloside-resistant ATP-Mg carrier. Mitochondria from a disruption mutant of SAL1 have a 50% reduction in the uptake of ATP. We have also found a clear stimulation of ATP-transport activity by calcium, with an S0.5 of approx. 30 μM. Our results also suggest that Sal1p is a target of the glucose-induced calcium signal which is non-essential in wild-type cells, but becomes essential for transport of ATP into mitochondria in yeast lacking ADP/ATP translocases.

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