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. 1997 Dec 29;139(7):1775–1783. doi: 10.1083/jcb.139.7.1775

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(A) Deletions of the NH₂-terminal domain of iso-1. WT represents the wild-type sequence. The Δ numbers represent the number of NH₂-terminal amino acids deleted in each construct. The amino acid sequence (single letter code) of the relevant portion of the NH₂-terminal domain is indicated at the top with numbers designating the amino acid position starting with the initiating methionine at position 1. (B) Confocal laser scanning microscopy of L. enriettii promastigotes expressing epitope-tagged deletion constructs Δ20, Δ25, and Δ30. Stable cell lines transfected with pX63Hyg.Δ20, pX63Hyg.Δ25, or pX63Hyg.Δ30 were stained with a 1:500 dilution of the anti-GLUT2 antibody and a 1:200 dilution of FITC-conjugated secondary antibody and examined by confocal microscopy. Each micrograph represents a single 0.5-μm section through each field.

(A) Deletions of the NH₂-terminal domain of iso-1. WT represents the wild-type sequence. The Δ numbers represent the number of NH₂-terminal amino acids deleted in each construct. The amino acid sequence (single letter code) of the relevant portion of the NH₂-terminal domain is indicated at the top with numbers designating the amino acid position starting with the initiating methionine at position 1. (B) Confocal laser scanning microscopy of L. enriettii promastigotes expressing epitope-tagged deletion constructs Δ20, Δ25, and Δ30. Stable cell lines transfected with pX63Hyg.Δ20, pX63Hyg.Δ25, or pX63Hyg.Δ30 were stained with a 1:500 dilution of the anti-GLUT2 antibody and a 1:200 dilution of FITC-conjugated secondary antibody and examined by confocal microscopy. Each micrograph represents a single 0.5-μm section through each field.