TY - JOUR
T1 - Membrane localization of the NlpC/P60 family protein EGL-26 correlates with regulation of vulval cell morphogenesis in Caenorhabditis elegans
AU - Estes, Kathleen A.
AU - Kalamegham, Rasika
AU - Hanna-Rose, Wendy
N1 - Funding Information:
Some nematode strains used in this work were provided by the Caenorhabditis Genetics Center, which is funded by the National Institutes of Health National Center for Research Resources. The egl-26(tm1244) deletion allele was produced and kindly provided by Shohei Mitani and the National Bioresource Project for the Nematode (Tokyo Women's Medical University). We thank Kenneth J. Kemphues for kindly providing anti-PAR-6 antibody. We thank Chris Malone and members of the Hanna-Rose lab for critical reading of the manuscript and acknowledge Kimberly Clemens for help with localization experiments. This research was supported by March of Dimes Foundation award #5-FY01-518 and American Heart Association award # 0555530U.
PY - 2007/8/1
Y1 - 2007/8/1
N2 - 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.
AB - 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.
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U2 - 10.1016/j.ydbio.2007.05.020
DO - 10.1016/j.ydbio.2007.05.020
M3 - Article
C2 - 17560977
AN - SCOPUS:34447646161
SN - 0012-1606
VL - 308
SP - 196
EP - 205
JO - Developmental Biology
JF - Developmental Biology
IS - 1
ER -