Abstract
PP2Ce: Fat and stressed out?
Highlights
In 2008, a group from Merck & Co reported the development of an alternative approach to classical forward genetics for dissecting complex disease traits [1]
Fast forward to 2013, and in this issue of Molecular Metabolism, Lu et al. report a detailed characterization of the protein product of Ppm1l, which they christened ‘protein phosphatase 2C on endoplasmic reticulum’ or PP2Ce [2]. They propose that PP2Ce is a specific phosphatase for inositol requiring-protein 1 (IRE1), a serine/threonine protein kinase that alters gene expression as a response to endoplasmic reticulum based stress signals
In ER stress signaling, three sentinel proteins, IRE1, ATF6, and PERK detect a deficiency in ER function and via their signaling pathways enable the cell to adapt to metabolic perturbation and/or altered secretory requirements, in an attempt to restore homeostasis (Figure 1)
Summary
In 2008, a group from Merck & Co reported the development of an alternative approach to classical forward genetics for dissecting complex disease traits [1]. They propose that PP2Ce is a specific phosphatase for inositol requiring-protein 1 (IRE1), a serine/threonine protein kinase that alters gene expression as a response to endoplasmic reticulum based stress signals. In ER stress signaling, three sentinel proteins, IRE1, ATF6, and PERK detect a deficiency in ER function and via their signaling pathways enable the cell to adapt to metabolic perturbation and/or altered secretory requirements, in an attempt to restore homeostasis (Figure 1) (reviewed by [3]).
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