A Surveillance Pathway Monitors the Fitness of the Endoplasmic Reticulum to Control Its Inheritance

SummaryThe endoplasmic reticulum (ER) plays an essential role in the production of lipids and secretory proteins. Because the ER cannot be generated de novo, it must be faithfully transmitted or divided at each cell division. Little is known of how cells monitor the functionality of the ER during the cell cycle or how this regulates inheritance. We report here that ER stress in S. cerevisiae activates the MAP kinase Slt2 in a new ER stress surveillance (ERSU) pathway, independent of the unfolded protein response. Upon ER stress, ERSU alters the septin complex to delay ER inheritance and cytokinesis. In the absence of Slt2 kinase, the stressed ER is transmitted to the daughter cell, causing the death of both mother and daughter cells. Furthermore, Slt2 is activated via the cell surface receptor Wsc1 by a previously undescribed mechanism. We conclude that the ERSU pathway ensures inheritance of a functional ER.

Graphical AbstractFigure optionsDownload high-quality image (86 K)Download as PowerPoint slideHighlights▸ Cells monitor the functionality of the endoplasmic reticulum during the cell cycle ▸ Endoplasmic eeticulum (ER) stress is recognized by a ER surveillance (ERSU) pathway ▸ ERSU induces delayed cortical ER inheritance and cytokinesis in response to ER stress ▸ ERSU signaling is essential for generation of viable progeny during ER stress