Contribution of different pathways to the supply of phosphatidylethanolamine and phosphatidylcholine to mitochondrial membranes of the yeast Saccharomyces cerevisiae

Bürgermeister, Maria; Birner-Grünberger, Ruth; Nebauer, Ruth; Daum, Günther

doi:10.1016/j.bbalip.2004.09.007

Cited by 77 publications

(77 citation statements)

References 44 publications

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“…Therefore, to gain further insight into the function of the individual residues of the LGST motif, yeast Psd1p mutants harboring single and combined LGST mutations were expressed in a psd1⌬psd2⌬ strain. In the absence of both Psd1p and Psd2p, yeast are ethanolamine auxotrophs (11,12). Thus, the ability of a mutant Psd1p construct to support growth of a psd1⌬psd2⌬ strain in the absence of ethanolamine reports on its functionality.…”

Section: Characterization Of the Conserved Lgst Motif Of Psd1p-thementioning

confidence: 99%

“…In yeast, two enzymes mediate the production of PE from PS; Psd1p located in the mitochondrion (7)(8)(9), and Psd2p, a resident of endosomes (10). Yeast without PSD1 and PSD2 cannot grow unless supplemented with ethanolamine, which feeds production of PE via the cytidine diphosphate (CDP)-ethanolamine pathway (11)(12)(13). Although Psd2p is unique to yeast, Psd1p is an essential protein in mammals and has been evolutionarily conserved from bacteria to yeast to metazoans (14).…”

mentioning

confidence: 99%

“…It further suggests that mechanisms to import PE produced in the ER into the mitochondrion are either lacking or inefficient. Indeed, PE produced by the CDP-ethanolamine pathway is poorly incorporated into mitochondrial membranes (11,12,17). The absence of Psd1p in yeast or mammalian cells affects mitochondrial morphology, impairs cell growth, and diminishes respiratory capacity (18 -20).…”

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confidence: 99%

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Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Onguka¹,

Calzada²,

Ogunbona³

et al. 2015

Journal of Biological Chemistry

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Background: Autocatalytic processing is required for Psd1p function. Molecular requirements for Psd1p autocatalysis are largely undefined. Results: Psd1p autocatalysis occurs in yeast mutants lacking its substrate or mitochondrial-specific lipids. Furthermore, Psd1p re-directed to the endoplasmic reticulum undergoes autocatalysis and is functional in vivo. Conclusion: Psd1p autocatalysis does not require its substrate or mitochondrial-specific lipids, proteins, or co-factors. Significance: Once membrane-embedded, Psd1p is autocatalytically self-sufficient.

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Section: Characterization Of the Conserved Lgst Motif Of Psd1p-thementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Onguka¹,

Calzada²,

Ogunbona³

et al. 2015

Journal of Biological Chemistry

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“…1A). Under these growth conditions, PC was synthesized by methylation of PE that is predominantly produced by Psd2 (38). Thus, it is crucial for the yeast cells to maintain certain amounts of PC/PE, although the ratio can vary drastically.…”

Section: Depletion Of Pc Impairs Protein Transport Into the Innermentioning

confidence: 99%

“…The CL biosynthesis pathway consists of multiple steps (30 -34), whereas PE is produced by decarboxylation of phosphatidylserine by the phosphatidylserine decarboxylase 1 (Psd1) (35)(36)(37). In yeast, Psd1 is the major source of cellular PE under standard growth conditions (38). However, further sources for cellular PE exist.…”

mentioning

confidence: 99%

Phosphatidylcholine Affects Inner Membrane Protein Translocases of Mitochondria

Schuler¹,

Bartolomeo

Mårtensson

et al. 2016

Journal of Biological Chemistry

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Two protein translocases transport precursor proteins into or across the inner mitochondrial membrane. The presequence translocase (TIM23 complex) sorts precursor proteins with a cleavable presequence either into the matrix or into the inner membrane. The carrier translocase (TIM22 complex) inserts multispanning proteins into the inner membrane. Both protein import pathways depend on the presence of a membrane potential, which is generated by the activity of the respiratory chain. The non-bilayer-forming phospholipids cardiolipin and phosphatidylethanolamine are required for the activity of the respiratory chain and therefore to maintain the membrane potential for protein import. Depletion of cardiolipin further affects the stability of the TIM23 complex. The role of bilayer-forming phospholipids like phosphatidylcholine (PC) in protein transport into the inner membrane and the matrix is unknown. Here, we report that import of presequence-containing precursors and carrier proteins is impaired in PC-deficient mitochondria. Surprisingly, depletion of PC does not affect stability and activity of respiratory supercomplexes, and the membrane potential is maintained. Instead, the dynamic TIM23 complex is destabilized when the PC levels are reduced, whereas the TIM22 complex remains intact. Our analysis further revealed that initial precursor binding to the TIM23 complex is impaired in PC-deficient mitochondria. We conclude that reduced PC levels differentially affect the TIM22 and TIM23 complexes in mitochondrial protein transport.Mitochondria fulfill essential functions for the survival of the cell like energy conversion to produce ATP, synthesis of amino acids, lipids, and heme, as well as the generation of iron-sulfur clusters. They contain about 1000 proteins in yeast and 1500 proteins in humans (1, 2). More than 99% of the mitochondrial proteins are synthesized as precursors on cytosolic ribosomes. Mitochondria contain a sophisticated system of protein translocases to import precursor proteins (3-9). The translocase of the outer membrane (TOM 3 complex) forms the general entry gate for most precursor proteins. After passage of the TOM channel, distinct protein translocases sort the preproteins into the different subcompartments: the outer and inner membrane as well as the two aqueous compartments, the matrix and intermembrane space.The majority of mitochondrial proteins are sorted into the inner membrane and the matrix. Two inner membrane-bound protein complexes mediate protein import. The presequence translocase (also termed TIM23 complex) transports precursor proteins with a cleavable presequence into the inner membrane and the matrix, whereas the carrier translocase (also termed TIM22 complex) inserts proteins with multiple transmembrane segments into the inner membrane (3-9). The membrane potential across the inner membrane provides the driving force for both protein import pathways and is generated by the activity of the respiratory chain. Presequence-containing preproteins are directly transferred from the ...

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The role of nonbilayer phospholipids in mitochondrial structure and function

2017

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Edited by Wilhelm JustMitochondrial structure and function are influenced by the unique phospholipid composition of its membranes. While mitochondria contain all the major classes of phospholipids, recent studies have highlighted specific roles of the nonbilayer-forming phospholipids phosphatidylethanolamine (PE) and cardiolipin (CL) in the assembly and activity of mitochondrial respiratory chain (MRC) complexes. The nonbilayer phospholipids are cone-shaped molecules that introduce curvature stress in the bilayer membrane and have been shown to impact mitochondrial fusion and fission. In addition to their overlapping roles in these mitochondrial processes, each nonbilayer phospholipid also plays a unique role in mitochondrial function; for example, CL is specifically required for MRC supercomplex formation. Recent discoveries of mitochondrial PE-and CL-trafficking proteins and prior knowledge of their biosynthetic pathways have provided targets for precisely manipulating nonbilayer phospholipid levels in the mitochondrial membranes in vivo. Thus, the genetic mutants of these pathways could be valuable tools in illuminating molecular functions and biophysical properties of nonbilayer phospholipids in driving mitochondrial bioenergetics and dynamics.

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Contribution of different pathways to the supply of phosphatidylethanolamine and phosphatidylcholine to mitochondrial membranes of the yeast Saccharomyces cerevisiae

Cited by 77 publications

References 44 publications

Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Phosphatidylserine Decarboxylase 1 Autocatalysis and Function Does Not Require a Mitochondrial-specific Factor

Phosphatidylcholine Affects Inner Membrane Protein Translocases of Mitochondria

The role of nonbilayer phospholipids in mitochondrial structure and function

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