MassIVE MSV000086558

Partial Public PXD022932

GNPS - Impaired phosphatidylethanolamine metabolism activates a reversible stress response that detects and resolves mutant mitochondrial precursors

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Description

For decades, the endoplasmic reticulum (ER)-resident tri-methylation pathway of phosphatidylcholine production that is fed by phosphatidylethanolamine (PE) made in the mitochondrion, served as a phospholipid trafficking paradigm. Recently, the strict mitochondrial localization of the enzyme that makes PE in the mitochondrion, phosphatidylserine decarboxylase 1 (Psd1), was questioned. Since a dual localization of Psd1 to the ER would have far-reaching implications, we initiated our study to independently re-assess the subcellular distribution of Psd1. Our results support the unavoidable conclusion that the vast majority, if not all, of functional Psd1 resides in the mitochondrion. Through our efforts, we discovered that mutant forms of Psd1 that impair a self-processing step needed for it to become functional, are dually localized to the ER when expressed in a PE-limiting environment. We conclude that severely impaired cellular PE metabolism provokes an ER-assisted adaptive response that is capable of identifying and resolving nonfunctional mitochondrial precursors. [doi:10.25345/C5K19J] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: endoplasmic reticulum phosphatidylethanolamine mitochondria Psd1 metabolism self-processing

Contact

Principal Investigators:
(in alphabetical order) 		Steven M. Claypool, Johns Hopkins University School of Medicine, USA
Submitting User: Jon_Trinidad
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GNPS content goes here (MSV000086558 [task=36c473a4ae3949e083c4a15aa087f6ae])
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