A C-terminal domain regulates plasma membrane localization of podocin.

<p>A. Immunofluorescence for a transiently expressed, Flag-tagged truncation of podocin (podocin^1–285) reveals increased plasma membrane localization in comparison with podocin wild type in HeLa-cells (b and a respectively). B. Schematic representation of constructs consisting of the extracellular domain of CD16 and the transmembrane domain of CD7 fused to different parts of podocin. C. Immunofluorescence using anti-CD16 antibody showed primarily membranous staining patterns for CD-16-7-* and CD16-7-podocin^1–285 (a, b). In contrast, immunofluorescence for CD16-7-podocin^286–385 revealed multiple vesicular structures (c), thereby proving analogous localization of CD16-fusion constructs and V5/Flag-tagged constructs.