SLC25A29

Last update 08 May 2025

Basic Info

Synonyms

C14orf69, CACT-like, Carnitine/acylcarnitine translocase-like

+ [10]

Introduction

Mitochondrial transporter of arginine, lysine, homoarginine, methylarginine and, to a much lesser extent, ornithine and histidine (PubMed:19287344, PubMed:24652292). Does not transport carnitine nor acylcarnitines (PubMed:24652292). Functions by both counter-exchange and uniport mechanisms (PubMed:24652292). Plays a physiological role in the import of basic amino acids into mitochondria for mitochondrial protein synthesis and amino acid degradation (PubMed:19287344, PubMed:24652292).

100 Clinical Results associated with SLC25A29

100 Translational Medicine associated with SLC25A29

0 Patents (Medical) associated with SLC25A29

Literatures (Medical) associated with SLC25A29

01 Jun 2022·Biochimica et Biophysica Acta (BBA) - BioenergeticsQ2 · BIOLOGY

Praseodymium trivalent ion is an effective inhibitor of mitochondrial basic amino acids and carnitine/acylcarnitine carriers

Q2 · BIOLOGY

Article

Author: Nicolotti, Orazio ; Giangregorio, Nicola ; Tonazzi, Annamaria ; Gambacorta, Nicola ; Incampo, Giovanna ; Palmieri, Luigi ; Pacifico, Concetta

We herein report the identification of the lantanide praseodymium trivalent ion Pr³⁺ as inhibitor of mitochondrial transporters for basic amino acids and phylogenetically related carriers belonging to the Slc25 family. The inhibitory effect of Pr³⁺ has been tested using mitochondrial transporters reconstituted into liposomes being effective in the micromolar range, acting as a competitive inhibitor of the human basic amino acids carrier (BAC, Slc25A29), the human carnitine/acylcarnitine carrier (CAC, Slc25A20). Furthermore, we provide computational evidence that the complete inhibition of the transport activity of the recombinant proteins is due to the Pr³⁺ coordination to key acidic residues of the matrix salt bridge network. Besides being used as a first choice stop inhibitor for functional studies in vitro of mitochondrial carriers reconstituted in proteoliposomes, Pr³⁺ might also represent a useful tool for structural studies of the mitochondrial carrier family.

01 Jan 2021·Computational and Structural Biotechnology Journal

Structural determinants of ligands recognition by the human mitochondrial basic amino acids transporter SLC25A29. Insights from molecular dynamics simulations of the c-state

Article

Author: Polticelli, Fabio ; Pasquadibisceglie, Andrea

In mitochondria, metabolic processes require the trafficking of solutes and organic molecules, such as amino acids. This task is accomplished by the Mitochondrial Carrier Family members (also known as SLC25), among which the SLC25A29 is responsible for the translocation of basic amino acids. In this regard, nitric oxide levels originated by the arginine mitochondrial catabolism have been shown to strongly affect cancer cells' metabolic status. Furthermore, the metabolic disease saccharopinuria has been linked to a mitochondrial dysregulation caused by a toxic intermediate of the lysine catabolism. In both cases, a reduction of the activity of SLC25A29 has been shown to ameliorate these pathological conditions. However, no detailed structural data are available on SLC25A29. In the present work, molecular modelling, docking and dynamics simulations have been employed to analyse the structural determinants of ligands recognition by SLC25A29 in the c-state. Results confirm and reinforce earlier predictions that Asn73, Arg160 and Glu161, and Arg257 represent the ligand contact points I, II, and III, respectively, and that Arg160, Trp204 and Arg257 form a stable interaction, likely critical for ligand binding and translocation. These results are discussed in view of the experimental data available for SLC25A29 and other homologous carriers of the same family.

01 May 2018·OncogeneQ1 · MEDICINE

Elevated mitochondrial SLC25A29 in cancer modulates metabolic status by increasing mitochondria-derived nitric oxide

Q1 · MEDICINE

Article

Author: Gu, Junzhong ; Xu, Hao ; Gu, Yuchun ; Yin, Le ; Wang, Qinyi ; Liang, Shenghui ; Wu, Lida ; Zhao, Chao ; Zhang, Huiyuan

Warburg effect has been recognized as a hallmark of cancer cells for many years, but its modulation mechanism remains a great focus. Our current study found a member of solute carrier family 25 (SLC25A29), the main arginine transporter on mitochondria, significantly elevated in various cancer cells. Knockout of SLC25A29 by CRISPR/Cas9 inhibited proliferation and migration of cancer cells both in vitro and in vivo. SLC25A29-knockout cells also showed an altered metabolic status with enhanced mitochondrial respiration and reduced glycolysis. All of above impacts could be reversed after rescuing SLC25A29 expression in SLC25A29-knockout cells. Arginine is transported into mitochondria partly for nitric oxide (NO) synthesis. Deletion of SLC25A29 resulted in severe decrease of NO production, indicating that the mitochondria is a significant source of NO. SLC25A29-knockout cells dramatically altered the variation of metabolic processes, whereas addition of arginine failed to reverse the effect, highlighting the necessity of transporting arginine into mitochondria by SLC25A29. In conclusion, aberrant elevated SLC25A29 in cancer functioned to transport more arginine into mitochondria, improved mitochondria-derived NO levels, thus modulated metabolic status to facilitate increased cancer progression.

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SLC25A29

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