Metabolism and function of mitochondrial cardiolipin

Ren, Mindong; Phoon, Colin K.L.; Schlame, Michael

doi:10.1016/j.plipres.2014.04.001

Cited by 270 publications

(272 citation statements)

References 198 publications

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“…For 186 instance, UPS1 controls the transfer of phosphatidic acid (PA) from the outer to the inner 187 membrane, where PA is channeled into a chain of enzymatic reactions resulting in the 188 production of cardiolipin (CL) [65,66,69]. susceptibility of TRIAP1-deficient cells to lethal stimuli [71,74]. Of note, TRIAP1 was 201 initially identified as a TP53-responsive anti-apoptotic protein that was induced in conditions 202 of sub-lethal genotoxic stress [70,75] as well as a TP53 antagonist at the level of cell cycle 203 regulation [76].…”

Section: Mitochondrial Lipid Homeostasis 180mentioning

confidence: 99%

Mitochondrial Proteins Containing Coiled-Coil-Helix-Coiled-Coil-Helix (CHCH) Domains in Health and Disease

Modjtahedi

Tokatlidis

Dessen

et al. 2016

Trends in Biochemical Sciences

110

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Members of the coiled-coil-helix-coiled-coil-helix (CHCH) domain-containing protein family that carry (CX 9 C) type motifs are imported into the mitochondrion with the help of the disulfide relay-dependent MIA import pathway. These evolutionary-conserved proteins are emerging as new cellular factors that control mitochondrial respiration, redox regulation, lipid homeostasis or membrane ultrastructure and dynamics. Here, we discuss recent insights on the activity of known (CX 9 C) motif-carrying proteins in mammals and review current data implicating the MIA40/CHCHD4 import machinery in the regulation of their mitochondrial import. Recent findings and the identification of disease-associated mutations in specific (CX 9 C) motif-carrying proteins have highlighted members of this family of proteins as potential therapeutic targets in a variety of human disorders.

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Section: Mitochondrial Lipid Homeostasis 180mentioning

confidence: 99%

Mitochondrial Proteins Containing Coiled-Coil-Helix-Coiled-Coil-Helix (CHCH) Domains in Health and Disease

Modjtahedi

Tokatlidis

Dessen

et al. 2016

Trends in Biochemical Sciences

110

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“…Alteration in its acyl chain composition and peroxidation of cardiolipin have been proposed to show different effects in tissues-dependent manner. 33,34) Precise mechanisms to explain the biphasic regulation of CerK and/or C1P formation by cardiolipin including specificity of molecular forms of cardiolipin remain to be elucidated.…”

Section: Discussionmentioning

confidence: 99%

“…Alterations of cardiolipin in cells have been shown to be involved in various pathological conditions including ischemia, hypothyroism, Barth syndrome, and aging, etc. 33,34) Also, CerK and C1P appear to be involved in ischemia and neurodegenerative diseases. 41,42) Possible interactions between cardiolipin and CerK/C1P should be determined physiologically and pathologically.…”

Section: Regulation Of Cerk Activity By Cardiolipin In Cellsmentioning

confidence: 99%

Effects of Glycerophospholipids on Ceramide Kinase Activity: Cardiolipin-Affected Cellular Formation of Ceramide-1-phosphate

Matsuzaki

Takahashi

Nakamura

et al. 2016

Biological & Pharmaceutical Bulletin

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Ceramide kinase (CerK) and ceramide-1-phosphate (C1P) are involved in various cellular functions, while regulation of the enzyme activity has not been well elucidated. We herein investigated the effects of several glycerophospholipids on human recombinant CerK activity with CaCl 2 and MgCl 2 by measuring the formation of fluorescent labeled C1P in vitro. CerK activities were 44.1 11.4 (pmol/µg/min) with vehicle, 137 29 with 2 mM CaCl 2 , and 144 32 with 2 mM MgCl 2 in the glycerol/albumin buffer. The addition of glycerophospholipids such as phosphatidylcholine, phosphatidylinositol (PI), PI 4,5-bisphosphate (PI(4,5)P 2 ), and phosphatidic acid had no effect on CerK activity with CaCl 2 , although PI(4,5)P 2 and phosphatidic acid bound to CerK in the lipid-protein overlay assay. The addition of cardiolipin (diphosphatidylglycerol) at concentrations up to 0.1 µM increased, whereas those more than 1 µM decreased CerK activity with CaCl 2 /MgCl 2 . In the lipid-protein overlay assay, cardiolipin bound to CerK and CerK lacking pleckstrin homology (PH) domain, but not PH domain of CerK, in CaCl 2 -independent manner. Cardiolipin also bound to CerK in the multilamellar vesicle binding assay. A deviation from the normal range of cellular cardiolipin, both the decrease by phospholipase D6 expression and increase by an exogenous addition of the lipid, negatively regulated C1P formation in intact HepG2 cells. Our results revealed that cardiolipin bound to CerK and regulated the formation of C1P in vitro and in cells.Key words ceramide kinase; cardiolipin; glycerophospholipid Ceramide kinase (CerK) produces ceramide-1-phosphate (C1P) through the phosphorylation of ceramide, and the cloning and functional characterization of this enzyme were successfully achieved by Drs. Kohama and Spiegel's group.

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“…Another important class of redox signaling molecules are cardiolipins, which are virtually exclusively localized in the inner mitochondrial membrane (Ren et al, 2014). Most cardiolipin species have four unsaturated acyl chains that are oxidation-sensitive.…”

Section: Mitochondria As Redox Signaling Nodesmentioning

confidence: 99%

Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation

2017

Frontiers Research Topics

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Metabolism and function of mitochondrial cardiolipin

Cited by 270 publications

References 198 publications

Mitochondrial Proteins Containing Coiled-Coil-Helix-Coiled-Coil-Helix (CHCH) Domains in Health and Disease

Mitochondrial Proteins Containing Coiled-Coil-Helix-Coiled-Coil-Helix (CHCH) Domains in Health and Disease

Effects of Glycerophospholipids on Ceramide Kinase Activity: Cardiolipin-Affected Cellular Formation of Ceramide-1-phosphate

Molecular Mechanisms and Physiological Significance of Organelle Interactions and Cooperation

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