Content and dimensions of the endoplasmic reticulum (ER) are flexible and regulated based on cellular needs, environmental changes or stress. Turnover or degradation of superfluous material is facilitated by selective degradation of the ER via the lysosome (ER-phagy). Malfunction of ER-phagy usually results in disease formation, including neurodegenerative diseases. 

Researchers around the IBC2-based Stolz group were studying the regulation of the ER-phagy machinery, in particular by phosphorylation events. In their latest work published in Nature Communication, the Stolz lab in collaboration with the Heilemann, Grumati, Misra and Dötsch labs identified the kinase CK2 as a central player of ER-phagy that regulates functional ubiquitination events on ER-phagy receptors and the formation of active ER-phagy sites.