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Updated: May 24, 2026

Measurements of Physiological Stress Responses in C. Elegans
Published on: May 21, 2020
BiP links TOR signaling to ER stress in Chlamydomonas
1Instituto de Bioquímica Vegetal y Fotosíntesis-Consejo Superior de Investigaciones Científicas, CSIC, Avda. Américo Vespucio, Sevilla, Spain. crespo@ibvf.csic.es
Abstract:
The highly conserved target of rapamycin (TOR) Ser/Thr kinase promotes protein synthesis under favorable growth conditions in all eukaryotes. Downregulation of TOR signaling in the model unicellular green alga Chlamydomonas reinhardtii has recently revealed a link between control of protein synthesis, endoplasmic reticulum (ER) stress and the reversible modification of the BiP chaperone by phosphorylation. Inhibition of protein synthesis by rapamycin or cycloheximide resulted in the phosphorylation of BiP on threonine residues while ER stress induced by tunicamycin or heat shock caused the fast dephosphorylation of the protein. Regulation of BiP function by phosphorylation/dephosphorylation events was proposed in early studies in mammalian cells although no connection to TOR signaling has been established so far. Here I will discuss about the coordinated regulation of BiP modification by TOR and ER stress signals in Chlamydomonas.
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