Use of the ND evidence code for Gene Ontology (GO) terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Functional characterization of the C. elegans nephrocystins NPHP-1 and NPHP-4 and their role in cilia and male sensory behaviors.
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NPHP-1 localizes to ciliated sensory endings of dendrites
"GFP-tagged NPHP-1 and NPHP-4 proteins localize to ciliated sensory endings of dendrites and colocalize with PKD-2 in male-specific sensory cilia."
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NPHP-1 and NPHP-4 colocalize with PKD-2 in male-specific sensory cilia
"GFP-tagged NPHP-1 and NPHP-4 proteins localize to ciliated sensory endings of dendrites and colocalize with PKD-2 in male-specific sensory cilia."
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nphp-1;nphp-4 double mutant males are response defective
"nphp-1; nphp-4 double, but not single, mutant males are response defective."
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NPHP-1 and NPHP-4 play redundant roles in ciliary sensory signal transduction
"We propose that NPHP-1 and NPHP-4 proteins play important and redundant roles in facilitating ciliary sensory signal transduction."
The Caenorhabditis elegans nephrocystins act as global modifiers of cilium structure.
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NPHP-1 and NPHP-4 localize to ciliary transition zones
"GFP-tagged NPHP-1 and NPHP-4 proteins localize to the ciliary TZ, with NPHP-1 requiring the presence of NPHP-4 for TZ localization"
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NPHP-1 requires NPHP-4 for TZ localization
"GFP-tagged NPHP-1 and NPHP-4 proteins localize to the ciliary TZ, with NPHP-1 requiring the presence of NPHP-4 for TZ localization"
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NPHP-1 and NPHP-4 regulate ciliary access of IFT machinery and signaling molecules
"We propose that NPHP-1 and NPHP-4 act globally at the TZ to regulate ciliary access of the IFT machinery, axonemal structural components, and signaling molecules"
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Loss of NPHP-1 and NPHP-4 causes changes in localization of specific ciliary components
"In conclusion, loss of both NPHP-1 and NPHP-4 but not NPHP-1 alone leads to the abnormal ciliary localization of the IFT-B polypeptide OSM-6, the OSM-3-kinesin, and the BBS proteins BBS-7 and BBS-8."
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nphp-1 mutants have stunted or misshaped CEM cilia
"In nphp-1 mutants, CEM cilia are stunted or misshaped"
Functional interactions between the ciliopathy-associated Meckel syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR) proteins.
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MKS/MKSR proteins localize to transition zones/basal bodies of sensory cilia
"MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1, MKSR-2), localize to transition zones/basal bodies of sensory cilia"
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Genetic interactions between mks/mksr mutants manifest as increased lifespan due to abnormal insulin-IGF-I signaling
"we find genetic interactions between all double mks/mksr mutant combinations, manifesting as an increased lifespan phenotype, which is due to abnormal insulin-IGF-I signaling"
MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis.
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NPHP-1 and NPHP-4 localize to the transition zone
"Using fluorescently tagged proteins, we detect MKS/MKSR/NPHP proteins in a region corresponding to the TZ (adjacent to where IFT proteins concentrate at the TFs/BB)."
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NPHP-1 and NPHP-4 are part of the NPHP module
"we group MKS-1, MKSR-1, MKSR-2, MKS-3, and MKS-6 into an MKS/MKSR module and NPHP-1 and NPHP-4 into an NPHP module"
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NPHP and MKS modules cooperate for BB/TZ membrane associations
"MKS/MKSR/NPHP proteins establish basal body/TZ membrane attachments before or coinciding with intraflagellar transport-dependent axoneme extension"
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TZ proteins establish a ciliary gate that restricts protein accumulation in cilia
"the two modules restrict inappropriate accumulation of membrane-associated proteins inside cilia"
Ciliopathy proteins establish a bipartite signaling compartment in a C. elegans thermosensory neuron.
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Ciliopathy proteins including nephronophthisis proteins localize to the ciliary base
"proteins associated with Bardet-Biedl syndrome (BBS), Meckel syndrome and nephronophthisis at its base"
TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome.
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TMEM-107 functions redundantly with NPHP-4 to regulate cilium integrity
"nematode TMEM-107 occupies an intermediate layer of the TZ-localized MKS module by organizing recruitment of the ciliopathy proteins"
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TZ proteins organize recruitment of ciliopathy proteins
"nematode TMEM-107 occupies an intermediate layer of the TZ-localized MKS module by organizing recruitment of the ciliopathy proteins"
A Conserved Role for Girdin in Basal Body Positioning and Ciliogenesis.
Expression and phenotype analysis of the nephrocystin-1 and nephrocystin-4 homologs in Caenorhabditis elegans.
Deep research report on nphp-1