Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
A polycystic kidney-disease gene homologue required for male mating behaviour in C. elegans.
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lov-1 was identified as a gene required for male mating behavior, specifically response to hermaphrodite contact and vulva location.
"Here we identify a gene, lov-1 (for location of vulva), that is required for two male sensory behaviours: response and vulva location."
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LOV-1 is expressed in male-specific sensory neurons: ray neurons, hook neurons, and head cephalic (CEM) neurons.
"lov-1 is expressed in adult males in sensory neurons of the rays, hook and head"
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LOV-1 is homologous to human PKD1 polycystin.
"LOV-1 is the closest C. elegans homologue of PKD1"
The Caenorhabditis elegans autosomal dominant polycystic kidney disease gene homologs lov-1 and pkd-2 act in the same pathway.
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lov-1 and pkd-2 act in the same genetic pathway for mating behavior.
"pkd-2;lov-1 double mutants are no more severe than either of the single mutants, indicating that lov-1 and pkd-2 act together"
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LOV-1::GFP and PKD-2::GFP colocalize in cilia and cell bodies of male-specific neurons.
"LOV-1::GFP and PKD-2::GFP are expressed in the same male-specific sensory neurons and are concentrated in cilia and cell bodies"
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lov-1 is not required for cilia structure.
"the cilia of lov-1 and pkd-2 single mutants and of lov-1;pkd-2 double mutants are normal as judged by electron microscopy"
Towards understanding the polycystins.
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LOV-1 and PKD-2 localize to sensory neuron endings and may function as mechanosensors or chemosensors.
"Expression analysis localized LOV-1 and PKD-2 to the ends of sensory neurons in male tails and to the tips of CEM neurons in the head, consistent with functions as chemo- or mechanosensors"
ATP-2 interacts with the PLAT domain of LOV-1 and is involved in Caenorhabditis elegans polycystin signaling.
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ATP-2 physically interacts with LOV-1 PLAT domain and this interaction is conserved.
"ATP-2, the beta subunit of the ATP synthase, physically associates with the LOV-1 PLAT domain and that this interaction is evolutionarily conserved"
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ATP-2, LOV-1, and PKD-2 act in the same signaling pathway.
"atp-2, lov-1, and pkd-2 act in the same molecular pathway"
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ATP synthase components colocalize with LOV-1 and PKD-2 in cilia.
"ATP-2 and other ATP synthase components colocalize with LOV-1 and PKD-2 in cilia"
Casein kinase II and calcineurin modulate TRPP function and ciliary localization.
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CK2 regulatory subunit (KIN-10) binds LOV-1 and modulates PKD-2 ciliary localization.
"We identified the regulatory subunit of the serine-threonine casein kinase II (CK2) as a binding partner of LOV-1 and human PC-1"
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Phosphorylation regulates PKD-2 ciliary localization.
"A dynamic phosphorylation-dephosphorylation cycle may represent a mechanism for modulating TRPP activity, cellular sensation, and ciliary protein localization"
STAM and Hrs down-regulate ciliary TRP receptors.
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STAM-1A interacts with LOV-1 and directs LOV-1/PKD-2 for lysosomal degradation.
"signal transduction adaptor molecule STAM-1A interacts with C. elegans LOV-1 (PC1), and that STAM functions with hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs) on early endosomes to direct the LOV-1-PKD-2 complex for lysosomal degradation"
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LOV-1 localizes to both ciliary base and cilium proper.
"In a stam-1 mutant, both LOV-1 and PKD-2 improperly accumulate at the ciliary base"
Deep research report on lov-1