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WBPicture0000008627DescriptionFigure 5. Ce-DAB-1 associates with Ce-LRP-1 and Ce-LRP-2 and with Golgi components. (A,B) The Ce-DAB-1 PTB domain (residues 1-252) shows interaction with the intracellular domains of both Ce-LRP-1 (residues 4595-4753) and Ce-LRP-2 (C-terminal 81 residues) by yeast two-hybrid assay. β-Galactosidase activity (replicates; A) and growth in the absence of histidine (B). (C) Potential binding sites in Ce-LRP-1 (underlined amino acids indicate those that match the consensus binding site for the PTB domains of mammalian Dab1 and Dab2). (D) The Ce-DAB-1 PTB domain interacts with an FXNPXY motiffrom residues 4653-4658. Substitution of Tyr 4658 with alanine reduces interaction between the Ce-DAB-1 PTB domain and the intracellular domain of Ce-LRP-1. (E) Subcellular localization of Ce-DAB-1 expressed in tissue culture cells. NIH3T3 (WGA) and HeLa cells (gamma-adaptin) were transfected to express Ce-DAB-1 and processed for indirect immunofluorescence with antibodies to gamma-adaptin subunit AP-1, Ce-DAB-1, and directly labeled WGA. Note that there are two HeLa cells in the image shown. (F) Ce-DAB-1::GFP is present in punctate structures within P6.p daughters. Indirect immunofluorescence of qaEx4003 [Ce-dab-1::Ce-DAB-1::GFP; unc-119(+)]; unc-119(e2498) animals with antibodies to LET-23 (left) and Ce-DAB-1::GFP (anti-GFP; center) and merged images (right) are shown. Images are single 0.2-μm confocal planes through P6.p after one division.
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AcknowledgmentTemplateWormBase wishes to thank <Journal_URL> for permission to reproduce figures from this article. Please note that this material may be protected by copyright. Reprinted from <Journal_URL>, <Article_URL>. Copyright (<Publication_year>) with permission from <Publisher_URL>.
Publication_year2003
Article_URLDOIid10.1101/gad.1136103
Journal_URLGenes&Development
Publisher_URLColdSpringHarborLabPress
ReferenceWBPaper00006219