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

Pingdewinde N. Sam, Elizabeth Calzada, Michelle Grace Acoba, Tian Zhao, Yasunori Watanabe, Anahita Nejatfard, Jonathan C. Trinidad, Timothy E. Shutt, Sonya E. Neal, Steven M. Claypool

Research output: Contribution to journalArticlepeer-review

Abstract

Phosphatidylethanolamine (PE) made in mitochondria has long been recognized as an important precursor for phosphatidylcholine production that occurs in the endoplasmic reticulum (ER). 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.

Original languageEnglish (US)
Article number102196
JournaliScience
Volume24
Issue number3
DOIs
StatePublished - Mar 19 2021

Keywords

  • Cell Biology
  • Molecular Physiology
  • Proteomics

ASJC Scopus subject areas

  • General

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