Figure 2.
Figure 2. SLC-36.1 is a putative lysosomal amino acid transporter. (A) Topology models of C. elegans SLC-36.1 and H. sapiens SLC36A1. (B) Alignment of the amino acid transporter domains of C. elegans SLC-36.1, human SLC36A1-4, rat LYAAT-1, fly Path, and yeast AVT4. Identical residues are shaded in black, and similar ones in gray. The conserved H57, G66, and L68 are indicated in orange, yellow, and green, respectively. The blue star indicates the unconserved Ser 69. The mutation site in slc-36(yq84) mutants (P130L) is indicated in pink. (C) Quantification (mean ± SEM) of embryonic vacuoles in N2 and slc-36.1(yq110) and slc-36.1(yq110) mutants carrying the indicated transgenes. 15 embryos at the 1.5-fold stage were scored for each strain. Three independent transgenic lines were analyzed for each transgene. *, P < 0.05; **, P < 0.01; ***, P < 0.001. Black asterisks indicate comparisons between nontransgene and each SLC-36.1 transgenic line. Red asterisks indicate comparisons of transgenes between WT and mutant SLC-36.1 transgenic lines. (D) Quantification (mean ± SEM) of embryo lethality in N2, slc-36.1 and laat-1 single mutants and laat-1;slc-36.1 double mutants without or with supplementation of amino acids. 250 or more embryos were analyzed for each genotype. Indicated amino acids were supplied at 100 mM each, and data shown are derived from 10 independent experiments. Data are from three (non–amino acid supplementation group) or 10 (amino acid supplementation group) independent experiments. **, P < 0.01; ***, P < 0.001. (E) Colocalization of mCh::SLC-36.1 with LAAT-1::GFP in embryos (top) and adult hypodermis (bottom). Arrows and arrowheads indicate phagosomes and lysosomes, respectively. Boxed regions are magnified (2×) in insets. Bars, 2 µm. (F) Colocalization of mCh::SLC-36.1 carrying H57A, G66A, and or L68S mutations (red) with LAAT-1::GFP (green) in embryos (top) and adult hypodermis (bottom). Lysosomes are indicated by arrowheads. Insets show magnified (2×) views of boxed regions with mCh, GFP, and merged panels. Bars, 2 µm.

SLC-36.1 is a putative lysosomal amino acid transporter. (A) Topology models of C. elegans SLC-36.1 and H. sapiens SLC36A1. (B) Alignment of the amino acid transporter domains of C. elegans SLC-36.1, human SLC36A1-4, rat LYAAT-1, fly Path, and yeast AVT4. Identical residues are shaded in black, and similar ones in gray. The conserved H57, G66, and L68 are indicated in orange, yellow, and green, respectively. The blue star indicates the unconserved Ser 69. The mutation site inslc-36(yq84) mutants (P130L) is indicated in pink.(C) Quantification (mean ± SEM) of embryonic vacuoles in N2 and slc-36.1(yq110) andslc-36.1(yq110) mutants carrying the indicated transgenes. 15 embryos at the 1.5-fold stage were scored for each strain. Three independent transgenic lines were analyzed for each transgene. *, P < 0.05; **, P < 0.01; ***, P < 0.001. Black asterisks indicate comparisons between nontransgene and each SLC-36.1 transgenic line. Red asterisks indicate comparisons of transgenes between WT and mutant SLC-36.1 transgenic lines. (D) Quantification (mean ± SEM) of embryo lethality in N2,slc-36.1 and laat-1 single mutants and laat-1;slc-36.1 double mutants without or with supplementation of amino acids. 250 or more embryos were analyzed for each genotype. Indicated amino acids were supplied at 100 mM each, and data shown are derived from 10 independent experiments. Data are from three (non–amino acid supplementation group) or 10 (amino acid supplementation group) independent experiments. **, P < 0.01; ***, P < 0.001. (E) Colocalization of mCh::SLC-36.1 with LAAT-1::GFP in embryos (top) and adult hypodermis (bottom). Arrows and arrowheads indicate phagosomes and lysosomes, respectively. Boxed regions are magnified (2×) in insets. Bars, 2 µm.(F) Colocalization of mCh::SLC-36.1 carrying H57A, G66A, and or L68S mutations (red) with LAAT-1::GFP (green) in embryos (top) and adult hypodermis (bottom). Lysosomes are indicated by arrowheads. Insets show magnified (2×) views of boxed regions with mCh, GFP, and merged panels. Bars, 2 µm.

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