The EFF-1A Cytoplasmic Domain Influences Hypodermal Cell Fusions in C. elegans But Is Not Dependent on 14-3-3 Proteins

PloS One
Jessica H Shinn-ThomasWilliam A Mohler

Abstract

Regulatory and biophysical mechanisms of cell-cell fusion are largely unknown despite the fundamental requirement for fused cells in eukaryotic development. Only two cellular fusogens that are not of clear recent viral origin have been identified to date, both in nematodes. One of these, EFF-1, is necessary for most cell fusions in Caenorhabditis elegans. Unregulated EFF-1 expression causes lethality due to ectopic fusion between cells not developmentally programmed to fuse, highlighting the necessity of tight fusogen regulation for proper development. Identifying factors that regulate EFF-1 and its paralog AFF-1 could lead to discovery of molecular mechanisms that control cell fusion upstream of the action of a membrane fusogen. Bioinformatic analysis of the EFF-1A isoform's predicted cytoplasmic domain (endodomain) previously revealed two motifs that have high probabilities of interacting with 14-3-3 proteins when phosphorylated. Mutation of predicted phosphorylation sites within these motifs caused measurable loss of eff-1 gene function in cell fusion in vivo. Moreover, a human 14-3-3 isoform bound to EFF-1::GFP in vitro. We hypothesized that the two 14-3-3 proteins in C. elegans, PAR-5 and FTT-2, may regulate either localiz...Continue Reading

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Citations

Jul 30, 2016·Small GTPases·Ksenia Smurova, Benjamin Podbilewicz
Apr 3, 2019·The Journal of Cell Biology·Nicolas G BrukmanLeonid V Chernomordik
May 9, 2021·Scientific Reports·Sneha L KoneruMichalis Barkoulas

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Methods Mentioned

BETA
PCR
transgenic
dissection
fluorescence microscopy
confocal microscopy
transgenically
Assay

Software Mentioned

Image J
NetPhos
KinasePhos
MetaMorph
ImageJ
Zeiss
Minimotif Miner ( MnM

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