Ca2+-regulated mitochondrial carriers of ATP-Mg2+/Pi: evolutionary insights in protozoans
EntityUAM. Departamento de Biología Molecular
10.1016/j.bbamcr.2021.119038Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1868.7 (2021): 119038
Funded byThis work has been funded by a grant from the Spanish Ministry of Science SAF2017-82560-R (to AdelA), and by an institutional grant from the Fundación Ramón Areces to the Centro de Biología Molecular Severo Ochoa (CBMSO)
ProjectGobierno de España. SAF2017-82560-R
SubjectsATP transport; Calcium; Evolution; Mitochondria; Mitochondrial carrier; Protozoan; Biología y Biomedicina / Biología
Rights© 2021 The Authors
Esta obra está bajo una licencia de Creative Commons Reconocimiento-NoComercial-SinObraDerivada 4.0 Internacional.
In addition to its uptake across the Ca2+ uniporter, intracellular calcium signals can stimulate mitochondrial metabolism activating metabolite exchangers of the inner mitochondrial membrane belonging to the mitochondrial carrier family (SLC25). One of these Ca2+-regulated mitochondrial carriers (CaMCs) are the reversible ATP-Mg2+/Pi transporters, or SCaMCs, required for maintaining optimal adenine nucleotide (AdN) levels in the mitochondrial matrix representing an alternative transporter to the ADP/ATP translocases (AAC). This CaMC has a distinctive Calmodulin-like (CaM-like) domain fused to the carrier domain that makes its transport activity strictly dependent on cytosolic Ca2+ signals. Here we investigate about its origin analysing its distribution and features in unicellular eukaryotes. Unexpectedly, we find two types of ATP-Mg2+/Pi carriers, the canonical ones and shortened variants lacking the CaM-like domain. Phylogenetic analysis shows that both SCaMC variants have a common origin, unrelated to AACs, suggesting in turn that recurrent losses of the regulatory module have occurred in the different phyla. They are excluding variants that show a more limited distribution and less conservation than AACs. Interestingly, these truncated variants of SCaMC are found almost exclusively in parasitic protists, such as apicomplexans, kinetoplastides or animal-patogenic oomycetes, and in green algae, suggesting that its lost could be related to certain life-styles. In addition, we find an intricate structural diversity in these variants that may be associated with their pathogenicity. The consequences on SCaMC functions of these new SCaMC-b variants are discussed
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