The human gene SLC25A17 encodes a peroxisomal transporter of coenzyme A, FAD and NAD+

2012 ◽  
Vol 443 (1) ◽  
pp. 241-247 ◽  
Author(s):  
Gennaro Agrimi ◽  
Annamaria Russo ◽  
Pasquale Scarcia ◽  
Ferdinando Palmieri

The essential cofactors CoA, FAD and NAD+ are synthesized outside the peroxisomes and therefore must be transported into the peroxisomal matrix where they are required for important processes. In the present study we have functionally identified and characterized SLC25A17 (solute carrier family 25 member 17), which is the only member of the mitochondrial carrier family that has previously been shown to be localized in the peroxisomal membrane. Recombinant and purified SLC25A17 was reconstituted into liposomes. Its transport properties and kinetic parameters demonstrate that SLC25A17 is a transporter of CoA, FAD, FMN and AMP, and to a lesser extent of NAD+, PAP (adenosine 3′,5′-diphosphate) and ADP. SLC25A17 functioned almost exclusively by a counter-exchange mechanism, was saturable and was inhibited by pyridoxal 5′-phosphate and other mitochondrial carrier inhibitors. It was expressed to various degrees in all of the human tissues examined. Its main function is probably to transport free CoA, FAD and NAD+ into peroxisomes in exchange for intraperoxisomally generated PAP, FMN and AMP. The present paper is the first report describing the identification and characterization of a transporter for multiple free cofactors in peroxisomes.

Molecules ◽  
2020 ◽  
Vol 25 (10) ◽  
pp. 2417 ◽  
Author(s):  
Luc Rochette ◽  
Alexandre Meloux ◽  
Marianne Zeller ◽  
Gabriel Malka ◽  
Yves Cottin ◽  
...  

The transfer of metabolites through the mitochondrial membranes is a vital process that is highly controlled and regulated by the inner membrane. A variety of metabolites, nucleotides, and cofactors are transported across the inner mitochondrial membrane (IMM) by a superfamily of membrane transporters which are known as the mitochondrial carrier family (MCF) or the solute carrier family 25 (SLC25 protein family). In humans, the MCF has 53 members encoded by nuclear genes. Members of the SLC25 family of transporters, which is the largest group of solute carriers, are also known as mitochondrial carriers (MCs). Because MCs are nuclear-coded proteins, they must be imported into the IMM. When compared with normal cells, the mitochondria of cancer cells exhibit significantly increased transmembrane potentials and a number of their transporters are altered. SLC25 members were identified as potential biomarkers for various cancers. The objective of this review is to summarize what is currently known about the involvement of mitochondrial SLC25 carriers in associated diseases. This review suggests that the SLC25 family could be used for the development of novel points of attack for targeted cancer therapy.


Gene ◽  
2019 ◽  
Vol 705 ◽  
pp. 142-148
Author(s):  
Ping Ren ◽  
Jiankai Wei ◽  
Haiyan Yu ◽  
Bo Dong

Endocrinology ◽  
2002 ◽  
Vol 143 (3) ◽  
pp. 1047-1057 ◽  
Author(s):  
Markus R. John ◽  
Maya Arai ◽  
David A. Rubin ◽  
Kenneth B. Jonsson ◽  
Harald Jüppner

Gene ◽  
2003 ◽  
Vol 314 ◽  
pp. 113-120 ◽  
Author(s):  
G. Vazza ◽  
S. Picelli ◽  
A. Bozzato ◽  
M.L. Mostacciuolo

1998 ◽  
Vol 82 (3-4) ◽  
pp. 147-152 ◽  
Author(s):  
M. Kimura ◽  
Y. Matsuda ◽  
T. Yoshioka ◽  
N. Sumi ◽  
Y. Okano

Biomolecules ◽  
2020 ◽  
Vol 10 (9) ◽  
pp. 1226
Author(s):  
Adriano Nunes-Nesi ◽  
João Henrique F. Cavalcanti ◽  
Alisdair R. Fernie

Although structurally related, mitochondrial carrier family (MCF) proteins catalyze the specific transport of a range of diverse substrates including nucleotides, amino acids, dicarboxylates, tricarboxylates, cofactors, vitamins, phosphate and H+. Despite their name, they do not, however, always localize to the mitochondria, with plasma membrane, peroxisomal, chloroplast and thylakoid and endoplasmic reticulum localizations also being reported. The existence of plastid-specific MCF proteins is suggestive that the evolution of these proteins occurred after the separation of the green lineage. That said, plant-specific MCF proteins are not all plastid-localized, with members also situated at the endoplasmic reticulum and plasma membrane. While by no means yet comprehensive, the in vivo function of a wide range of these transporters is carried out here, and we discuss the employment of genetic variants of the MCF as a means to provide insight into their in vivo function complementary to that obtained from studies following their reconstitution into liposomes.


2018 ◽  
Vol 14 (10) ◽  
pp. 1321-1332 ◽  
Author(s):  
Lili Xiong ◽  
Ran Kang ◽  
Ruofan Ding ◽  
Wenyuan Kang ◽  
Yiming Zhang ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document