Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
A map of the interactome network of the metazoan C. elegans.
Functional redundancy of the B9 proteins and nephrocystins in Caenorhabditis elegans ciliogenesis.
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The C. elegans B9 proteins (MKS-1/MKSR-1/MKSR-2) form a complex at the base of cilia and function redundantly with the nephrocystins (nph-1/nph-4); B9-gene mutations do not overtly affect cilia unless combined with a nph mutation.
"Mutations in the B9 genes do not overtly affect cilia formation unless they are in combination with a mutation in nph-1 or nph-4"
Empirically controlled mapping of the Caenorhabditis elegans protein-protein interactome network.
Functional interactions between the ciliopathy-associated Meckel syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR) proteins.
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The B9 domain defines a family of three proteins (MKS-1, MKSR-1, MKSR-2) in ciliated organisms; all three localize co-dependently to transition zones/basal bodies of C. elegans sensory cilia. Double mks/mksr mutants show an increased-lifespan phenotype due to abnormal insulin-IGF-I signaling.
"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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MKSR-1/B9D1 localizes to the ciliary transition zone and is a member of the MKS/MKSR module (with MKS-1, MKSR-2, MKS-3, MKS-6); the mksr-1;nphp-4 double mutant disrupts TZ membrane anchoring and Y-links.
"Phenotypes nearly identical to mks-6;nphp-4 mutants were observed in the mksr-1;nphp-4 strain"
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MKSR-1 is required for the transition-zone localization of other MKS-module proteins (MKS-6 and MKS-3), restricting MKS-3 to the TZ membrane.
"MKSR-1, MKSR-2, and MKS-5 restrict MKS-3 to the TZ membrane"
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MKSR-1 contributes to ciliary-gate function; in mksr-1 mutants the normally-excluded membrane proteins TRAM-1a and RPI-2 accumulate inside cilia.
"accumulates within cilia of mksr-1, mksr-2, mks-5, mks-6, nphp-1, and nphp-4 mutants"
TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome.
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TMEM-107 organizes recruitment of MKS-module ciliopathy proteins to subdomains of the ciliary transition zone; MKS-module membrane proteins are immobile and periodically arranged within the TZ.
"TZ-localized MKS module by organizing recruitment of the ciliopathy proteins"