Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible photoreceptor degeneration.

ABSTRACT: In response to environmental, developmental, and pathological stressors, cells engage homeostatic pathways to maintain their function. Among these pathways, the Unfolded Protein Response protects cells from the accumulation of misfolded proteins in the ER. Depending on ER stress levels, the ER-resident Fic protein catalyzes AMPylation or de-AMPylation of BiP, the major ER chaperone and regulator of the Unfolded Protein Response. This work elucidates the importance of the reversible AMPylation of BiP in maintaining the Drosophila visual system in response to stress. After 72 hr of constant light, photoreceptors of fic-null and AMPylation-resistant BiP^T366A mutants, but not wild-type flies, display loss of synaptic function, disintegration of rhabdomeres, and

SUBMITTER: Moehlman AT 

PROVIDER: S-EPMC6066327 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature