Fig. 4: Mutation of LAT1-4F2hc complexes to investigate lipid binding, the effects of glycosylation and the influence of the LAT1 C-terminus. | Nature Communications

Fig. 4: Mutation of LAT1-4F2hc complexes to investigate lipid binding, the effects of glycosylation and the influence of the LAT1 C-terminus.

From: The complete assembly of human LAT1-4F2hc complex provides insights into its regulation, function and localisation

Fig. 4

A The phospholipid binding site is at the C-terminus of the LAT1 subunit (light green) and the transmembrane segment of 4F2hc (blue). The head group of interfacial phospholipid interacts with 4F2hc-R183. B Native mass spectra of LAT1-4F2hc with the 4F2hc-R183L mutation. No lipid adduct is observed. The palmitoylated proteoform is labelled with a purple circle. C Structural illustration of non-glycosylated LAT1-4F2hc 4 M mutant with N365D/N381D/N424D/N506D. D Native mass spectra of non-glycosylated LAT1-4F2hc 4 M mutant in 20 µM LMNG. Two endogenous lipid adducts (731.3 ± 2.7 Da and 731.8 ± 4.2 Da) are observed. E Structural illustration of LAT1-4F2hc 4M-ΔC mutant with deletion of LAT1 C-terminal helix (highlighted orange). F Native mass spectra of LAT1-4F2hc 4M-ΔC mutant in LMNG. The absence of lipid adducts means that no endogenous lipids are retained. LMNG adduct peaks are highlighted with asterisks.

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