Biology subjects

Odehnalova, K.

Publications and source records attributed to Odehnalova, K..

2 recordsLinked to original sources

bioRxiv2026

ESCRT proteins organise stress-induced organelle contact between endoplasmic reticulum and Golgi

ESCRT proteins remodel membranes at many cell organelles, including the endoplasmic reticulum (ER). Here, we investigate whether ESCRTs in budding yeast participate in stress-induced ER reorganisation. We find that ER stress triggers the formation of tubular ER subdomains that recruit various ESCRT proteins. Recruitment of the major ESCRT-III protein Snf7 is mediated by the ESCRT-associated protein Bro1, a homologue of human ALIX, in a manner that is mechanistically distinct from Bro1 function at endosomes. ESCRT-containing ER subdomains are derived from ceramide-rich ER exit sites and form contacts with the Golgi. Furthermore, Bro1 helps to concentrate the tethering and lipid transfer protein Tcb3, a homologue of human extended synaptotagmins, at these organelle contacts and contributes to cellular fitness when lipid metabolism is perturbed. These results indicate that specialised ER exit sites can be repurposed for contacting the Golgi directly and uncover ESCRTs as organisers of stress-inducible ER-Golgi contacts that help maintain cell homeostasis.

cell biology↗

bioRxiv2025

Dynamic Organellar Mapping in yeast reveals extensive protein localization changes during ER stress

Sophisticated techniques are available for systematic studies of yeast cell biology. However, it remains challenging to investigate protein subcellular localization changes on a proteome-wide scale. Here, we apply Dynamic Organellar Maps (DOMs) by label-free mass spectrometry to detect localization changes of native, untagged proteins during endoplasmic reticulum (ER) stress. We find that hundreds of proteins shift between cellular compartments. For example, we show that numerous secretory pathway proteins accumulate in the ER, thus defining the extent and selectivity of ER retention of misfolded proteins. Furthermore, we identify candidate cargo proteins of the ER reflux pathway, determine constituents of reticulon clusters that segregate from the remainder of the ER and provide evidence for altered nuclear pore complex composition and nuclear import. These findings uncover protein relocalization as a major aspect of cellular reorganization during ER stress and establish DOMs as a powerful discovery tool in yeast.

cell biology↗