High impact information on eat-4

• Using the electropharyngeograms, we show that gamma-aminobutyric acid is not likely to be the M3 neurotransmitter, that synaptic transmission is present but abnormal in mutants lacking synaptotagmin, and that worms mutant in the eat-4 gene are defective for M3 function or transmission [1].
• In mutants lacking a voltage-dependent calcium channel (unc-2) or a vesicular glutamate transporter (VGLUT; eat-4), the abundance of GLR-1 in the ventral nerve cord was increased [2].
• Similarly, the amplitude of glutamate-evoked currents in ventral cord interneurons was increased in eat-4 VGLUT mutants compared with wild-type controls [2].
• The phenotypes of eat-4 mutants and the cell biology of the EAT-4 protein were critical in the identification of this protein as the vesicular glutamate transporter (3, 4) [3].
• Mutations in the unc-36 and eat-4 genes are partially neuroprotective, which indicates that endogenous signaling modulates the severity of the neurotoxic effects of Galphas [4].

Biological context of eat-4

• The same transgene rescues pharyngeal activity defects and both the habituation and dishabituation deficits seen in the eat-4 worms [5].

Anatomical context of eat-4

• Finally, we have tested long-term memory for habituation training in a strain of worms with a mutation in a vesicular glutamate transporter in the sensory neurons that transduce tap (eat-4) [6].

References