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Ulrich lab - Institute for Biochemistry

Redox-Regulated Relocalization of Get3 and its Chaperone Clients into Stress-Induced Foci

Various stress conditions or metabolic challenges can cause ATP depletion, protein unfolding and potentially toxic protein aggregation, associated with the onset and progression of diseases and premature ageing. Stress-induced chaperones serve as fast-reacting and highly dynamic components of the proteostasis network to prevent protein aggregation. In yeast, the oxidative activation of the cytosolic protein Get3 as an ATP-independent chaperone protects cells against ATP-depleting stress conditions. Under these conditions, Get3 relocates into defined punctate structures, where it presumably sequesters aggregation-prone proteins. Here, we study how Get3 foci formation is regulated, which client proteins are sequestered into these foci and how they are released upon stress recovery. We also explore stress- and age-dependent relocalization of stress-sensing chaperones and their tissue-specific role in C. elegans.

Lara Knaup

PhD students since June 2023

EMail: lknaup[at]

"I completed my Bachelor's and Master's degree in Human Biology at the University of Greifswald. In my dissertation in the laboratory of Jun. Prof. Ulrich, I am working on a stress and redox regulated chaperone and would like to better understand the underlying mechanism as well as the associated relocalization and its interaction partners."

Shayan Motiei

PhD Students since December 2023

EMail: smotiei[at]

"I received my bachelors degree in biochemistry from HHU Düsseldorf and my master degree in biological sciences from Universtiy of Cologne. In December 2023, I joined the Ulrich lab and began my PhD journey. I am investigating the role of a redox-regulated chaperone, ASNA-1, in the nematode worm C. elegans. The primary focus of my project is to elucidate the role of ASNA-1 as a hub connecting redox and protein homeostasis during aging and under stress conditions."