Goalpha regulates olfactory adaptation by antagonizing Gqalpha-DAG signaling in Caenorhabditis elegans.

ABSTRACT: The heterotrimeric G protein G(o) is abundantly expressed in the mammalian nervous system and modulates neural activities in response to various ligands. However, G(o)'s functions in living animals are less well understood. Here, we demonstrate that GOA-1 G(o)alpha has a fundamental role in olfactory adaptation in Caenorhabditis elegans. Impairment of GOA-1 G(o)alpha function and excessive activation of EGL-30 G(q)alpha cause a defect in adaptation to AWC-sensed odorants. These pathways antagonistically modulate olfactory adaptation in AWC chemosensory neurons. Wild-type animals treated with phorbol esters and double-mutant animals of diacylglycerol (DAG) kinases, dgk-3; dgk-1, also have a defect in adaptation, suggesting that elevated DAG signals disrupt normal adaptation. Constitutively

SUBMITTER: Matsuki M 

PROVIDER: S-EPMC1347976 | biostudies-literature | 2006 Jan

REPOSITORIES: biostudies-literature