Gene Ontology annotation through association of InterPro records with GO terms
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Mutations in ARMC9, which Encodes a Basal Body Protein, Cause Joubert Syndrome in Humans and Ciliopathy Phenotypes in Zebrafish.
Dysfunction of the ciliary ARMC9/TOGARAM1 protein module causes Joubert syndrome.
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Patient-cell perturbations implicate the ARMC9/TOGARAM1 module in ciliary stability.
"Aberrant serum-induced ciliary resorption and
cold-induced depolymerization in ARMC9 and TOGARAM1 patient cell lines suggest a
role for this new JBTS-associated protein module in ciliary stability."
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Disease-associated TOGARAM1 changes can disrupt its ARMC9 interaction.
"TOGARAM1
variants cause JBTS and disrupt TOGARAM1 interaction with ARMC9."
Primary cilia formation requires the Leigh syndrome-associated mitochondrial protein NDUFAF2.
A CRISPR-based screen for Hedgehog signaling provides insights into ciliary function and ciliopathies.
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Tagged ARMC9 shows stimulus-dependent ciliary-tip enrichment in mouse cells, with unresolved tagged-reagent species.
"stimulation of Hh signaling in IMCD3 cells led to redistribution of ARMC9 towards the ciliary tip within 6 hr before a gradual return to its original proximal location"
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Armc9 perturbation alters GLI accumulation without establishing a direct ARMC9 motor or SMO interaction.
"Armc9 mutant NIH-3T3 cells exhibited reduced ciliary accumulation of GLI2 and GLI3 (but not SMO) upon pathway activation"
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Armc9 mutant cells have altered ciliary length and tubulin modification levels.
"cilia from Armc9 mutant cells were short and exhibited reduced levels of acetylated and polyglutamylated tubulin"
A network of interacting ciliary tip proteins with opposing activities imparts slow and processive microtubule growth.
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Distinct ARMC9 interfaces organize interactions with TOGARAM1 and CSPP1 and modulate their microtubule effects.
"ARMC9 can bind to both proteins through two distinct domains and mildly enhance their effects on MT dynamics"
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ARMC9 does not bind microtubules autonomously in the tested conditions.
"ARMC9 does not bind to MTs on its own or in the presence of CEP104 and EB3"
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The ciliary module is a flexible interaction network rather than a fixed-stoichiometry complex.
"we do not think that the five CTM proteins form a stoichiometric complex but rather a flexible interaction network"
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ARMC9 and CCDC66 potentiate slow growth under particular component ratios.
"When the latter are present in excess, the scaffold proteins ARMC9 and CCDC66 can stimulate TOGARAM1-dependent slow growth."