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TitleStructural and biochemical comparison of the FLVCR and CTL membrane protein families in eukaryotes.
Journal, issue, pagesLife Sci Alliance, Vol. 9, Issue 7, Year 2026
Publish dateMay 11, 2026
AuthorsLynette Nel / Jan H Driller / Ronja Driller / Kelly M Frain / Bjørn P Pedersen /
PubMed AbstractThe organic cation choline is essential for eukaryotic metabolism. Recently, the feline leukemia virus subgroup C receptor-related (FLVCR, SLC49) family was demonstrated as central for basal choline ...The organic cation choline is essential for eukaryotic metabolism. Recently, the feline leukemia virus subgroup C receptor-related (FLVCR, SLC49) family was demonstrated as central for basal choline transport, questioning the role of the choline transporter-like (CTL, SLC44) family in this capacity. Here, we use oocytes to confirm that FLVCR1 (SLC49A1) and FLVCR2 (SLC49A2) proteins are choline transporters. CTL1 (SLC44A1) does not transport choline under the same conditions, supported by other CTL proteins, CherI and PNS1, which also display no choline transport activity. We present the atomic structures of FLVCR2, CTL1, and PNS1. The 3.4 Å cryo-EM structure of FLVCR2 has choline in the binding pocket. The 3.3 Å cryo-EM structure of CTL1 and the 2.7 Å crystal structure of PNS1 reveal an unusual protein fold, weakly related to the mitochondrial carrier family (SLC25). The unusual fold appears incompatible with transmembrane transport and implies a different and, so far, unknown function for CTL proteins. Our results support FLVCR proteins as choline transporters and suggest a nontransport role for CTL proteins.
External linksLife Sci Alliance / PubMed:42114998 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.73 - 3.39 Å
Structure data

50252

9qu3

EMDB-50252: Human choline transporter-like protein 1 (hCTL1/SLC44A1) in LMNG
PDB-9qu3: Cryo-EM structure of the human choline transporter-like protein hCTL1 in LMNG
Method: EM (single particle) / Resolution: 3.3 Å

53371

9qu4

EMDB-53371, PDB-9qu4:
Cryo-EM structure of the inward-open choline-bound state of choline/ethanolamine transporter FLVCR2
Method: EM (single particle) / Resolution: 3.39 Å

PDB-9f63:
Crystal structure of Saccharomyces cerevisiae pH nine-sensitive protein 1 (PNS1)
Method: X-RAY DIFFRACTION / Resolution: 2.73 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CHT:
CHOLINE ION

Source
  • homo sapiens (human)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsMEMBRANE PROTEIN / Choline transporter-like family / CTL / SLC44 / Choline transporter

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