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- W2034794811 abstract "Members of the UNC-5 protein family are transmembrane receptors for UNC-6/netrin guidance cues. To analyze the functional roles of different UNC-5 domains, we sequenced mutations in seven severe and three weak alleles of unc-5 in Caenorhabditis elegans. Four severe alleles contain nonsense mutations. Two weak alleles are truncations of the cytodomain, but one is a missense mutation in an extracellular immunoglobulin domain. To survey the function of different regions of UNC-5, wild-type and mutant unc-5::HA transgenes were tested for their ability to rescue the unc-5(e53) null mutant. Our data reveal partial functional requirements for the extracellular domains and identify a portion of the cytoplasmic juxtamembrane (JM) region as essential for rescue of migrations. When nine cytodomain tyrosines, including seven in the JM region, are mutated to phenylalanine, UNC-5 function and tyrosine phosphorylation are largely compromised. When F482 in the JM region of the mutant protein is reverted to tyrosine, UNC-5 tyrosine phosphorylation and in vivo function are largely recovered, suggesting that Y482 phosphorylation is critical to UNC-5 function in vivo. Our data also show that part of the ZU-5 motif is required for UNC-40-independent signaling of UNC-5." @default.
- W2034794811 created "2016-06-24" @default.
- W2034794811 creator A5019065056 @default.
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- W2034794811 creator A5090328187 @default.
- W2034794811 date "2002-11-01" @default.
- W2034794811 modified "2023-10-14" @default.
- W2034794811 title "UNC-5 Function Requires Phosphorylation of Cytoplasmic Tyrosine 482, but Its UNC-40-Independent Functions also Require a Region between the ZU-5 and Death Domains" @default.
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- W2034794811 doi "https://doi.org/10.1006/dbio.2002.0825" @default.
- W2034794811 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12435363" @default.
- W2034794811 hasPublicationYear "2002" @default.
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