2. Academic Validation
  3. Sideroflexins enable mitochondrial transport of polar neutral amino acids

Sideroflexins enable mitochondrial transport of polar neutral amino acids

  • bioRxiv. 2025 Jul 2:2025.06.18.660357. doi: 10.1101/2025.06.18.660357.
Samuel Block 1 2 3,  Fangtao Chi 1,  Paul C Rosen 2,  S Sebastian Pineda 4 5 6 7,  Alicia M Darnell 1 2 8,  Keene L Abbott 1 2,  Izabella A Pena 6 9,  Myriam Heiman 6 9,  Ömer H Yilmaz 1 2 10 11,  Nora Kory 3 7 12,  Matthew G Vander Heiden 1 2 7 12
Affiliations

Affiliations

  • 1 David H. Koch Institute for Integrative Cancer Research, MIT, Cambridge, MA, USA.
  • 2 Department of Biology, MIT, Cambridge, MA, USA.
  • 3 Department of Molecular Metabolism, Harvard T.H. Chan School of Public Health, Boston, MA, USA.
  • 4 Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
  • 5 Computer Science and Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
  • 6 Picower Institute for Learning and Memory, MIT, Cambridge, MA, USA.
  • 7 Broad Institute of MIT and Harvard, Cambridge, MA 02141, USA.
  • 8 Department of Pharmacology and Cancer Biology, Duke University School of Medicine, Durham, NC, USA.
  • 9 Department of Brain and Cognitive Sciences, MIT, Cambridge, MA, USA.
  • 10 Department of Pathology, Massachusetts General Hospital and Harvard Medical School, Boston, MA, USA.
  • 11 Department of Pathology, Beth Israel Deaconess Hospital and Harvard Medical School, Boston, MA, USA.
  • 12 Dana-Farber Cancer Institute, Boston, MA, USA.
PMID: 40631095 DOI: 10.1101/2025.06.18.660357
Abstract

Mitochondria contribute to compartmentalized metabolism in eukaryotic cells, supporting key enzymatic reactions for cell function and energy homeostasis. However, this compartmentalization necessitates regulated metabolite transport across mitochondrial membranes. Although many transport proteins have been identified, several mitochondrial amino acid transporters remain largely uncharacterized. Using CRISPR-Cas9-mediated candidate transporter knockouts coupled with assessment of metabolite transport via a mitochondrial swelling assay, we identify SFXN1, previously characterized for its role in mitochondrial serine transport, as a protein that mediates mitochondrial transport of a range of Other polar neutral Amino acids including proline, glycine, threonine, taurine, hypotaurine, β-alanine, and γ-aminobutyric acid (GABA). Furthermore, the SFXN1 paralogues SFXN2 and SFXN3 partially complement loss of SFXN1 to enable glycine transport, while SFXN2 and SFXN5 partially complement loss of SFXN1 to enable GABA transport. Altogether, these data suggest that sideroflexins facilitate the transport of polar neutral Amino acids across the inner mitochondrial membrane.

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