C. elegans Brat homologs regulate PAR protein-dependent polarity and asymmetric cell division.
The evolutionary conserved PAR proteins control polarization and asymmetric division in many organisms. Recent work in Caenorhabditis elegans demonstrated that nos-3 and fbf-1/2 can suppress par-2(it5ts) lethality, suggesting that they participate in cell polarity by regulating the function of the anterior PAR-3/PAR-6/PKC-3 proteins. In Drosophila embryos, Nanos and Pumilio are homologous to NOS-3 and FBF-1/2 respectively and control cell polarity by forming a complex with the tumor suppressor Brat to inhibit Hunchback mRNA translation. In this study, we investigated the possibility that Brat could control cell polarity and asymmetric cell division in C. elegans. We found that disrupting four of the five C. elegans Brat homologs (Cebrats) individually results in suppression of par-2(it5ts) lethality, indicating that these genes are involved in embryonic polarity. Two of the Cebrats, ncl-1 and nhl-2, partially restore the localization of PAR proteins at the cortex. While mutations in the four Cebrat genes do not severely impair polarity, they display polarity-associated defects. Surprisingly, these defects are absent from nos-3 mutants. Similarly, while nos-3 controls PAR-6 protein levels, this is not the case for any of the Cebrats. Our results, together with results from Drosophila, indicate that Brat family members function in generating cellular asymmetries and suggest that, in contrast to Drosophila embryos, the C. elegans homologs of Brat and Nanos could participate in embryonic polarity via distinct mechanisms.
Hyenne
Vincent
V
Cell Division and Differentiation Laboratory, Institute of Research in Immunology and Cancer, Université de Montréal, C.P. 6128, Succ Centre-ville Montréal, QC Canada H3C 3J7. Vincent.hyenne@umontreal.ca
Desrosiers
Marianne
M
Labbé
Jean-Claude
JC
D000818:Animals; D015153:Blotting, Western; D017173:Caenorhabditis elegans / Q000196:embryology*; D029742:Caenorhabditis elegans Proteins / Q000235:genetics / Q000378:metabolism*; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism; D002455:Cell Division / Q000502:physiology*; D016764:Cell Polarity / Q000502:physiology*; D019295:Computational Biology; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D004330:Drosophila; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism*; D019084:Fluorescent Antibody Technique, Indirect; D016013:Likelihood Functions; D008957:Models, Genetic; D009154:Mutation / Q000235:genetics; D010802:Phylogeny; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism
D029742:Caenorhabditis elegans Proteins; D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D029721:Drosophila Proteins; C515528:Nos-3 protein, C elegans; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C412783:brat protein, Drosophila; C111448:ncl-1 protein, C elegans; C512642:par-6 protein, C elegans