The G protein alpha chaperone and guanine-nucleotide exchange factor RIC-8 regulates cilia morphogenesis in Caenorhabditis elegans sensory neurons

• DOI: 10.1371/journal.pgen.1011015
• Publication Date: 2023-11-01T17:49:39Z
• Authors: Christina M. Camp...; Hayley McMahon; Inna Nechipurenko
• Keywords: Ciliogenesis; Intraflagellar Transport; Basal body; Chaperone (clinical)

Heterotrimeric G (αβγ) proteins are canonical transducers of G-protein-coupled receptor (GPCR) signaling and play critical roles in communication between cells their environment. Many GPCRs heterotrimeric localize to primary cilia modulate morphology via mechanisms that not well understood. Here, we show RIC-8, a cytosolic guanine nucleotide exchange factor (GEF) chaperone for Gα protein subunits, shapes membrane subset Caenorhabditis elegans sensory neurons. Consistent with its role ciliogenesis, C . RIC-8 localizes different neuron types. Using domain mutagenesis, demonstrate while the GEF function alone is sufficient, both Gα-interacting motifs required morphogenesis. We identify ODR-3 as client functions same genetic pathway another component non-canonical AGS-3 shape morphology. Notably, despite defects AWC morphology, ags-3 null mutants exhibit normal chemotaxis toward benzaldehyde unlike odr-3 mutant animals. Collectively, our findings describe novel evolutionarily conserved RIC-8-AGS-3-ODR-3 morphogenesis uncouple ciliogenesis olfaction.