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
TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome.
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The MKS-module membrane proteins of the ciliary transition zone are immobile and periodically arranged within the TZ, and TMEM-107 organizes recruitment of MKS-module ciliopathy proteins.
"TZ-localized MKS module by organizing recruitment of the ciliopathy proteins"
A Screen for Modifiers of Cilia Phenotypes Reveals Novel MKS Alleles and Uncovers a Specific Genetic Interaction between osm-3 and nphp-4.
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A novel mks-2 allele (yhw128) was recovered as an enhancer of nphp-4; mks-2 single mutants show no overt dye-filling defect, but nphp-4;mks-2 double mutants are strongly Dyf, demonstrating MKS/NPHP-module redundancy.
"there was no overt defect in dye uptake in mks-1(yhw146) or mks-2(yhw128) mutants"
MKS5 and CEP290 Dependent Assembly Pathway of the Ciliary Transition Zone.
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MKS-2 is a core MKS-module TZ protein required for the transition-zone localization of the peripheral protein TMEM-218.
"TMEM-218 is no longer present at the TZ in the mks-2 MKS module mutant"
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The core MKS-module TZ proteins (including MKS-2) are required for ciliary gate function, restricting entry of membrane-associated TRAM-1a into cilia.
"restricting the inappropriate entry of membrane-associated TRAM-1a into cilia"
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MKS-2 localization to the TZ depends on the upstream assembly factor MKS-5, and MKS-2 mislocalizes in the cep-290 mutant.
"MKS-5 as a critical assembly factor for all known MKS module proteins tested thus far"