Involvement of contact sites in phosphatidylserine import into liver mitochondria

Ardail, Dominique; Lermé, F.; Louisot, Pierre

doi:10.1016/s0021-9258(18)92926-1

Cited by 96 publications

(11 citation statements)

References 13 publications

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“…A recent study showed that PRELI phospholipids within mitochondria. For example, to be delivered to the site of biosynthesis and function, phospholipids may be transferred from one leaflet to another as well as from the OM to the IM at contact sites where both membranes are positioned closely (Ardail et al, 1991;Epand et al, 2007). Ups proteins may mediate these processes in the IMS.…”

Section: Discussionmentioning

confidence: 99%

Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria

Tamura

Endo

Iijima

et al. 2009

Journal of Cell Biology

155

196

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Cardiolipin, a unique phospholipid composed of four fatty acid chains, is located mainly in the mitochondrial inner membrane (IM). Cardiolipin is required for the integrity of several protein complexes in the IM, including the TIM23 translocase, a dynamic complex which mediates protein import into the mitochondria through interactions with the import motor presequence translocase–associated motor (PAM). In this study, we report that two homologous intermembrane space proteins, Ups1p and Ups2p, control cardiolipin metabolism and affect the assembly state of TIM23 and its association with PAM in an opposing manner. In ups1Δ mitochondria, cardiolipin levels were decreased, and the TIM23 translocase showed altered conformation and decreased association with PAM, leading to defects in mitochondrial protein import. Strikingly, loss of Ups2p restored normal cardiolipin levels and rescued TIM23 defects in ups1Δ mitochondria. Furthermore, we observed synthetic growth defects in ups mutants in combination with loss of Pam17p, which controls the integrity of PAM. Our findings provide a novel molecular mechanism for the regulation of cardiolipin metabolism.

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Section: Discussionmentioning

confidence: 99%

Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria

Tamura

Endo

Iijima

et al. 2009

Journal of Cell Biology

155

196

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“…Particularly, lipid movements can occur via specialized zones of apposition between subcellular membranes. For example, in yeast and in mammalian cells, a movement of phosphatidylserine (PS) from ER to mitochondria inner membrane was clearly demonstrated to occur through specialized region of ER referred to as mitochondria-associated membranes (MAM; Vance, 1990;Ardail et al, 1991;Achleitner et al, 1999). To investigate how DGDG transfers from chloroplast envelope to mitochondria membranes, we surveyed cell structures during the course of adaptation to P i deprivation.…”

Section: Discussionmentioning

confidence: 99%

Phosphate deprivation induces transfer of DGDG galactolipid from chloroplast to mitochondria

Jouhet

Maréchal

Baldan

et al. 2004

The Journal of Cell Biology

243

207

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In many soils plants have to grow in a shortage of phosphate, leading to development of phosphate-saving mechanisms. At the cellular level, these mechanisms include conversion of phospholipids into glycolipids, mainly digalactosyldiacylglycerol (DGDG). The lipid changes are not restricted to plastid membranes where DGDG is synthesized and resides under normal conditions. In plant cells deprived of phosphate, mitochondria contain a high concentration of DGDG, whereas mitochondria have no glycolipids in control cells. Mitochondria do not synthesize this pool of DGDG, which structure is shown to be characteristic of a DGD type enzyme present in plastid envelope. The transfer of DGDG between plastid and mitochondria is investigated and detected between mitochondria-closely associated envelope vesicles and mitochondria. This transfer does not apparently involve the endomembrane system and would rather be dependent upon contacts between plastids and mitochondria. Contacts sites are favored at early stages of phosphate deprivation when DGDG cell content is just starting to respond to phosphate deprivation.

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“…Phospholipid transport between the outer and inner mitochondrial membranes has been proposed to occur, similar to protein transport, at contact sites between mitochondrial inner and outer membranes (Ardail et al, 1991;Simbeni et al, 1991). Experiments with CHO cell mutants have identified a variant with a lesion in PS transport between the outer and inner mitochondrial membranes, but the gene responsible for this defect has yet to be identified (Emoto et al, 1999).…”

Section: Intramitochondrial Lipid Traffickingmentioning

confidence: 99%

Making heads or tails of phospholipids in mitochondria

Osman

Voelker

Langer

2011

Journal of Cell Biology

518

466

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Mitochondria are dynamic organelles whose functional integrity requires a coordinated supply of proteins and phospholipids. Defined functions of specific phospholipids, like the mitochondrial signature lipid cardiolipin, are emerging in diverse processes, ranging from protein biogenesis and energy production to membrane fusion and apoptosis. The accumulation of phospholipids within mitochondria depends on interorganellar lipid transport between the endoplasmic reticulum (ER) and mitochondria as well as intramitochondrial lipid trafficking. The discovery of proteins that regulate mitochondrial membrane lipid composition and of a multiprotein complex tethering ER to mitochondrial membranes has unveiled novel mechanisms of mitochondrial membrane biogenesis.

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Involvement of contact sites in phosphatidylserine import into liver mitochondria

Cited by 96 publications

References 13 publications

Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria

Ups1p and Ups2p antagonistically regulate cardiolipin metabolism in mitochondria

Phosphate deprivation induces transfer of DGDG galactolipid from chloroplast to mitochondria

Making heads or tails of phospholipids in mitochondria

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