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

ABSTRACT: 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 Mapping 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

SUBMITTER: Platzek A 

PROVIDER: S-EPMC12672650 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature