PMID:10887089

Citation	Gunther, CV, Georgi, LL and Riddle, DL (2000) A Caenorhabditis elegans type I TGF beta receptor can function in the absence of type II kinase to promote larval development. Development 127:3337-47
Abstract	The daf-4 gene encodes a type II bone morphogenetic protein receptor in Caenorhabditis elegans that regulates dauer larva formation, body size and male tail patterning. The putative type I receptor partner for DAF-4 in regulating dauer larva formation is DAF-1. Genetic tests of the mechanism of activation of these receptors show that DAF-1 can signal in the absence of DAF-4 kinase activity. A daf-1 mutation enhances dauer formation in a daf-4 null background, whereas overexpression of daf-1 partially rescues a daf-4 mutant. DAF-1 alone cannot fully compensate for the loss of DAF-4 activity, indicating that nondauer development normally results from the activities of both receptors. DAF-1 signaling in the absence of a type II kinase is unique in the type I receptor family. The activity may be an evolutionary remnant, owing to daf-1's origin near the type I/type II divergence, or it may be an innovation that evolved in nematodes. daf-1 and daf-4 promoters both mediated expression of green fluorescent protein in the nervous system, indicating that a DAF-1/DAF-4 receptor complex may activate a neuronal signaling pathway. Signaling from a strong DAF-1/DAF-4 receptor complex or a weaker DAF-1 receptor alone may provide larvae with more precise control of the dauer/nondauer decision in a range of environmental conditions.
Links	PubMed
Keywords	Activin Receptors, Type I; Amino Acid Sequence; Animals; Caenorhabditis elegans/embryology; Caenorhabditis elegans/physiology; Caenorhabditis elegans Proteins; Gene Expression; Helminth Proteins/chemistry; Helminth Proteins/genetics; Helminth Proteins/metabolism; Larva; Models, Molecular; Molecular Sequence Data; Mutation; Phenotype; Phosphorylation; Protein Conformation; Protein-Serine-Threonine Kinases/metabolism; Protein-Serine-Threonine Kinases/physiology; Receptors, Cell Surface/chemistry; Receptors, Cell Surface/genetics; Receptors, Cell Surface/metabolism; Receptors, Transforming Growth Factor beta/chemistry; Receptors, Transforming Growth Factor beta/genetics; Receptors, Transforming Growth Factor beta/metabolism; Receptors, Transforming Growth Factor beta/physiology; Sequence Homology, Amino Acid; Signal Transduction; Structure-Activity Relationship; Transgenes
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