GO_REF:0000033

Annotation inferences using phylogenetic trees

IBA annotations for MKS complex membership and cilium assembly are supported by phylogenetic conservation across ciliated organisms

GO_REF:0000043

Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping

GO_REF:0000117

Electronic Gene Ontology annotations created by ARBA machine learning models

PMID:18337471

Functional redundancy of the B9 proteins and nephrocystins in Caenorhabditis elegans ciliogenesis

C. elegans B9 proteins (including MKS-1/XBX-7) form a complex at the base of cilia

"the C. elegans B9 proteins form a complex that localizes to the base of cilia"
B9 proteins function redundantly with nephrocystins in ciliogenesis

"the B9 proteins function redundantly with the nephrocystins to regulate the formation and/or maintenance of cilia and dendrites in the amphid and phasmid ciliated sensory neurons"
Single B9 mutants have no overt ciliary defects

"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"
Combined B9/nphp mutations cause severe ciliary and dendrite defects

"the B9 proteins function redundantly with the nephrocystins to regulate the formation and/or maintenance of cilia and dendrites in the amphid and phasmid ciliated sensory neurons"

PMID:19208769

Functional interactions between the ciliopathy-associated Meckel syndrome 1 (MKS1) protein and two novel MKS1-related (MKSR) proteins

MKS-1, MKSR-1, and MKSR-2 localize to transition zones/basal bodies

"All Caenorhabditis elegans B9-domain-containing proteins, MKS-1 and MKS-1-related proteins 1 and 2 (MKSR-1, MKSR-2), localize to transition zones/basal bodies of sensory cilia"
Their subcellular localization is largely co-dependent

"Their subcellular localization is largely co-dependent, pointing to a functional relationship between the proteins"
B9 domain is found exclusively in this family of three proteins

"this domain occurs exclusively within a family of three proteins distributed widely in ciliated organisms"
Single, double, and triple mks/mksr mutants lack overt ciliary structure defects

"single, double and triple C. elegans mks/mksr mutants do not display overt defects in ciliary structure, intraflagellar transport or chemosensation"
Genetic interactions between mks/mksr mutants affect 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"

PMID:21422230

MKS and NPHP modules cooperate to establish basal body/transition zone membrane associations and ciliary gate function during ciliogenesis

MKS-1 is part of the MKS module at the transition zone

"the conserved C. elegans B9 domain (MKS-1, MKSR-1, and MKSR-2), MKS-3/TMEM67, MKS-5/RPGRIP1L, MKS-6/CC2D2A, NPHP-1, and NPHP-4 proteins exhibit essential, collective functions at the transition zone (TZ)"
MKS and NPHP modules cooperate for basal body/TZ membrane associations

"Specifically, MKS/MKSR/NPHP proteins establish basal body/TZ membrane attachments before or coinciding with intraflagellar transport-dependent axoneme extension"
MKS module includes MKS-1, MKSR-1, MKSR-2, MKS-3, MKS-5, MKS-6

"the conserved C. elegans B9 domain (MKS-1, MKSR-1, and MKSR-2), MKS-3/TMEM67, MKS-5/RPGRIP1L, MKS-6/CC2D2A, NPHP-1, and NPHP-4 proteins exhibit essential, collective functions at the transition zone (TZ)"
These proteins establish the ciliary gate during ciliogenesis

"uncover a unified role for eight TZ-localized proteins in basal body anchoring and establishing a ciliary gate during ciliogenesis"
B9 domains are structurally related to C2 domains

"B9 domains of MKS-1, MKSR-1, and MKSR-2 may be structurally related to C2 domains of RGRIP1L/MKS-5 and CC2D2A/MKS-6"

PMID:26595381

TMEM107 recruits ciliopathy proteins to subdomains of the ciliary transition zone and causes Joubert syndrome

TMEM-107 organizes recruitment of MKS-1 to the transition zone

"nematode TMEM-107 occupies an intermediate layer of the TZ-localized MKS module by organizing recruitment of the ciliopathy proteins MKS-1, TMEM-231 (JBTS20) and JBTS-14 (TMEM237)"
MKS module proteins occupy distinct subdomains within the TZ

"This work expands the MKS module of ciliopathy-causing TZ proteins associated with diffusion barrier formation and provides insight into TZ subdomain architecture"
MKS module membrane proteins are immobile at the TZ

"MKS module membrane proteins are immobile and super-resolution microscopy in worms and mammalian cells reveals periodic localizations within the TZ"

file:worm/mks-1/mks-1-deep-research-falcon.md

Deep research report on mks-1