Membrane localization of the NlpC/P60 family protein EGL-26 correlates with regulation of vulval cell morphogenesis in Caenorhabditis elegans

• Published in: Developmental biology Vol. 308; no. 1; pp. 196 - 205
• Main Authors: Estes, Kathleen A., Kalamegham, Rasika, Hanna-Rose, Wendy
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.08.2007
• Subjects: Acyltransferases - genetics; Acyltransferases - metabolism; Animals; Animals, Genetically Modified; Base Sequence; Caenorhabditis elegans - genetics; Caenorhabditis elegans - growth & development; Caenorhabditis elegans - metabolism; Caenorhabditis elegans Proteins - genetics; Caenorhabditis elegans Proteins - metabolism; DNA Primers - genetics; DNA, Helminth - genetics; Female; Gene Expression Regulation, Developmental; Genes, Helminth; Hrasls3; LRAT; Membranes - metabolism; Morphogenesis; Mutagenesis, Site-Directed; Mutation; Organogenesis; Palmitoyltransferase; Signal Transduction; Tubulogenesis; Vulva - cytology; Vulva - growth & development; Vulva - metabolism; Morphogenesis; LRAT; Palmitoyltransferase; Hrasls3; Tubulogenesis; Organogenesis
• ISSN: 0012-1606; 1095-564X
• DOI: 10.1016/j.ydbio.2007.05.020

Vulval morphogenesis in Caenorhabditis elegans generates a stack of toroidal cells enclosing a tubular lumen. Mutation of egl-26 is associated with malformation of vulF, the most dorsal toroid in the stack, resulting in a blocked lumen and an egg-laying defect. Here we present evidence that vulF retains the expected gene expression pattern, functions in signaling to the uterus and retains proper polarity when egl-26 is mutated, all suggesting that mutation of egl-26 specifically results in aberrant morphogenesis as opposed to abnormal fate specification. Recent computational analysis indicates that EGL-26, which was previously characterized as novel, belongs to the LRAT (lecithin retinol acyltransferase) subfamily of the NlpC/P60 superfamily of catalytic proteins. Via site-directed mutagenesis, we demonstrate a requirement of the putative catalytic residues for EGL-26 function in vivo. We also show that mutation of conserved serine 275 perturbs the apical membrane localization and the function of the EGL-26 protein. Additional mutagenesis of this residue suggests that EGL-26 attains its membrane localization via a mechanism distinct from that of LRAT.