Xenbase Image ID: 172912

Fig. 3. Direct interaction of spectrin βV with membrane phospholipids, but not with ankyrin G. (A) Spectrin-ankyrin interaction. (Left) Purified His-tagged ankyrin G binds to a GST-tagged R14-R15 fragment of spectrin βII (GST-βII R14-R15), but not to GST-tagged R14-R15 fragments of the human spectrin βV (GST-βV R14-R15) or Drosophila spectrin βH (GST-βH R14-R15). (Right) In the reciprocal experiment, the GST-tagged ZU5 domain of ankyrin G (GST-ankyrin ZU5) does not bind to the myc-tagged full-length human spectrin βV. Homodimerization of spectrin βV through its C-terminal region (R29-Cter) was used as a positive control (17). (B) Spectrin-membrane interaction. In a membrane lipid strip assay, the R29-Cter fragment of spectrin βV, but not its actin-binding domain (βV ABD), binds to phosphatidic acid (PA) and phosphatidylinositol 4-monophosphate [PI(4)P]. In the PIP strip assay, the βV R29-Cter peptide binds to PI(3)P, PI(4)P, and PI(5)P, to PI(3,5)P2, and to PI(3,4,5)P3. Image published in: Cortese M et al. (2017) Copyright © 2017. Image reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View

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