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WBPicture0000013140DescriptionFigure 2. epg-7 encodes a protein with similarity to mammalian FIP200 and yeast Atg11 and is degraded by autophagy. (A) Cloning of epg-7. (B) Protein sequence of EPG-7. The molecular lesions in identified mutant alleles are highlighted in red. (C) Schematic structures of EPG-7, FIP200, and Atg11. The coiled-coil domains are highlighted in green. The Atg11 domain is depicted in pink. (D) A large number of SQST-1::GFP aggregates accumulate in epg-7 mutant embryos carrying an epg-7(del Atg11) transgene. (E and F) No SQST-1 aggregates are detected in epg-7 mutants carrying an epg-7::gfp reporter. (E) DAPI image of the embryo shown in F. (G) EPG-7::GFP is weakly expressed and diffusely localized in the cytoplasm in wild-type embryos. (H-I) EPG-7::GFP is expressed in pharyngeal muscles (H, arrow) and cells in the tail region (I) at larval stages. (J) Compared with wild-type animals, levels of EPG-7::GFP are dramatically elevated in epg-4 mutants, but remain unchanged in sqst-1 mutants. (K) The expression level of EPG-7::GFP is dramatically elevated and many EPG-7::GFP aggregates are formed in lgg-1 mutant embryos. (L and M) No EPG-7 aggregates, detected by anti-EPG-7 antibody, are formed in wild-type embryos. (L) DAPI image of the embryo shown in M. (N) Levels of EPG-7 are dramatically elevated and a large number of EPG-7 aggregates are formed in atg-3 mutants. (O) No EPG-7 aggregates are formed in sqst-1 mutant embryos. Bars: (D-G and K-O) 10 um; (H) 10 um; (I) 10 um.
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AcknowledgmentTemplateWormBase thanks <Journal_URL> for permission to reproduce figures from this article. Reprinted from <Article_URL>. Copyright (<Publication_year>) with permission from <Publisher_URL>. The user must not use the Work for commercial purposes. If the user shares, alters, transforms, or builds upon the Work, the user may distribute the resulting work only under the same license the user received from <Publisher_URL>.
Publication_year2013
Article_URLDOIid10.1083/jcb.201209098
Journal_URLTheJournalofCellBiology
Publisher_URLTheRockefellerUniversityPress
ReferenceWBPaper00042170