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    Area of Science:

    • Cell Biology
    • Developmental Biology
    • Genetics

    Background:

    • Ankyrin repeat-containing proteins Inversin (INVS) and ANKS6, along with NEK8 kinase, are implicated in tissue patterning and organ physiology.
    • The dynamic assembly and functional states of the Inversin complex remain poorly understood.

    Approach:

    • Utilized hyperactive alleles in *C. elegans* to investigate the Inversin complex's activation mechanism.
    • Employed genome engineering to tag nematode homologs of INVS (MLT-4) and NEK8 (NEKL-2) with RFP.
    • Applied optogenetics to stimulate and inhibit dimerization of MLT-4 and NEKL-2.

    Key Points:

    • Dimerization of the Inversin complex activates its function, leading to gain-of-function phenotypes.
    • Monomerization of fluorescent tags suppressed the observed hyperactive phenotype.
    • Optogenetically induced dimerization mimicked a constitutively active Inversin complex.
    • Dimerization of NEKL-2 rescued a lethal MLT-4 mutant, highlighting the functional requirement of the dimeric state.

    Conclusions:

    • The Inversin complex exists in at least two distinct functional states: an active dimer and an inactive monomer.
    • Dynamic switching between these states regulates the output of the Inversin complex, controlling tissue patterning and organ physiology.