Use of the ND evidence code for Gene Ontology (GO) terms

Annotation inferences using phylogenetic trees

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

MKS-6/CC2D2A is one of eight TZ proteins that function collectively in ciliogenesis

"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-6 localizes specifically to the ciliary transition zone

"MKS/MKSR and NPHP proteins localize specifically to the ciliary TZ"
Functional interactions between NPHP proteins and MKS-5 or MKS-6 are required for ciliogenesis

"Functional interactions between NPHP proteins and MKS-5 or MKS-6 are required for ciliogenesis"
Joint disruption of MKS module proteins with NPHP-4 causes severe BB/TZ membrane association defects

"Joint disruption of an MKS/MKSR protein and NPHP-4 results in BB/TZ membrane association defects"
MKS-5 acts as a central hub required for docking MKS and NPHP protein modules

"MKS-5 is a central component required for docking/anchoring MKS and NPHP protein modules"
TZ proteins establish a ciliary gate that restricts nonciliary components from the cilium

"establishing a ciliary gate during ciliogenesis, and suggest that disrupting ciliary gate function contributes to phenotypic features of the MKS/NPHP disease spectrum"

PMID:25335890

Ciliopathy proteins establish a bipartite signaling compartment in a C. elegans thermosensory neuron.

TZ proteins localize to the dendrite terminus in AFD neurons

"we reveal the unexpected presence of ciliary transition zone proteins where no canonical transition zone ultrastructure exists"
Ciliary proteins help establish distinct signaling compartments in thermosensory neurons

"ciliary proteins help establish two contiguous, yet distinct cyclic GMP (cGMP) signaling compartments in Caenorhabditis elegans thermosensory AFD neurons"
TZ proteins function in membrane diffusion barrier formation at sites without canonical TZ ultrastructure

"Consistent with a requirement for a membrane diffusion barrier at the subcompartment base, we reveal the unexpected presence of ciliary transition zone proteins where no canonical transition zone ultrastructure exists"

PMID:26595381

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

TMEM-107 organizes recruitment of MKS module proteins to TZ subdomains

"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 are immobile at the TZ and show periodic localization patterns

"MKS module membrane proteins are immobile and super-resolution microscopy in worms and mammalian cells reveals periodic localizations within the TZ"
TZ proteins control ciliary composition through diffusion barrier function

"The transition zone (TZ) ciliary subcompartment is thought to control cilium composition and signalling by facilitating a protein diffusion barrier at the ciliary base"

file:worm/mks-6/mks-6-deep-research-falcon.md

Deep research report on mks-6