The diversity of ACBD proteins – From lipid binding to protein modulators and organelle tethers

Islinger, Markus; Costello, Joseph L.; Kors, Suzan; Soupène, Eric; Levine, Timothy P.; Kuypers, Frans A.; Schrader, Michael

doi:10.1016/j.bbamcr.2020.118675

Cited by 36 publications

(56 citation statements)

References 184 publications

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“…4 ). The coordination of fatty acyl-CoA distribution within the cells has been proposed to involve, in part, acyl-CoA-binding domain-containing proteins (ACBDs) [ 211 ]. There are seven family members, including ACBD1, also known as acyl-CoA binding protein, yet little is known about the specific roles of the ACBDs in the regulation of fatty acyl-CoA metabolizing processes [ 212 ].…”

Section: Tumor Fatty Acid Metabolism Pathways and Their Role In Cancementioning

confidence: 99%

The diversity and breadth of cancer cell fatty acid metabolism

2021

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Tumor cellular metabolism exhibits distinguishing features that collectively enhance biomass synthesis while maintaining redox balance and cellular homeostasis. These attributes reflect the complex interactions between cell-intrinsic factors such as genomic-transcriptomic regulation and cell-extrinsic influences, including growth factor and nutrient availability. Alongside glucose and amino acid metabolism, fatty acid metabolism supports tumorigenesis and disease progression through a range of processes including membrane biosynthesis, energy storage and production, and generation of signaling intermediates. Here, we highlight the complexity of cellular fatty acid metabolism in cancer, the various inputs and outputs of the intracellular free fatty acid pool, and the numerous ways that these pathways influence disease behavior.

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Section: Tumor Fatty Acid Metabolism Pathways and Their Role In Cancementioning

confidence: 99%

The diversity and breadth of cancer cell fatty acid metabolism

2021

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“…The authors suggested that the ACBD2/ECI2 protein complex facilitates tethering of peroxisomes with mitochondria by interacting simultaneously with both the mitochondrial (through N-terminal targeting signal) and peroxisomal (through C-terminal targeting signal) protein import machinery ( Fan et al, 2016 ). To further verify this mechanism of tether formation additional studies are required ( Islinger et al, 2020 ).…”

Section: Metabolite Transport Between Organellesmentioning

confidence: 99%

Peroxisomal Metabolite and Cofactor Transport in Humans

Chornyi

IJlst

Roermund

et al. 2021

Front. Cell Dev. Biol.

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Peroxisomes are membrane-bound organelles involved in many metabolic pathways and essential for human health. They harbor a large number of enzymes involved in the different pathways, thus requiring transport of substrates, products and cofactors involved across the peroxisomal membrane. Although much progress has been made in understanding the permeability properties of peroxisomes, there are still important gaps in our knowledge about the peroxisomal transport of metabolites and cofactors. In this review, we discuss the different modes of transport of metabolites and essential cofactors, including CoA, NAD+, NADP+, FAD, FMN, ATP, heme, pyridoxal phosphate, and thiamine pyrophosphate across the peroxisomal membrane. This transport can be mediated by non-selective pore-forming proteins, selective transport proteins, membrane contact sites between organelles, and co-import of cofactors with proteins. We also discuss modes of transport mediated by shuttle systems described for NAD+/NADH and NADP+/NADPH. We mainly focus on current knowledge on human peroxisomal metabolite and cofactor transport, but also include knowledge from studies in plants, yeast, fruit fly, zebrafish, and mice, which has been exemplary in understanding peroxisomal transport mechanisms in general.

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“…The acyl-coenzyme A (CoA)-binding domain proteins ACBD5 and ACBD4 act as tethers to mediate peroxisome-ER MCSs, through the binding of their FFAT-like motif to VAP proteins in the ER membrane [ [149] , [150] , [151] ]. Both proteins belong to the large ACBD family, whose members are involved in lipid-binding, cellular signalling, lipid metabolic pathways and controlling energy regulation, and are found in eukaryotes and prokaryotes [ 152 ]. In addition to their FFAT-like motifs, peroxisomal ACBD4 and ACBD5 possess an acyl-CoA binding domain at the N-terminus (exposed to the cytosol), a coiled-coil region and a C-terminal transmembrane domain.…”

Section: Peroxisome-organelle Interactions and Their Physiological Rementioning

confidence: 99%

“…3 ). Once at the ER membrane, PI(4)P can be hydrolysed to PI by the ER-resident phosphatase Sac1 [ 224 ], while PI(4)P is regenerated at the TGN by PI(4)-kinases such as PI4KIIIβ, which is recruited to the TGN membrane by the Golgi protein ACBD3 [ 152 , 227 ]. Coupled together, this maintains the PI(4)P concentration gradient between the TGN and ER, both ensuring the directionality of cholesterol transport and establishing the difference in membrane composition that is required for downstream signalling and function [ 225 ].…”

Section: Golgi-organelle Interactions and Their Physiological Relevanmentioning

confidence: 99%

Maintaining social contacts: The physiological relevance of organelle interactions

Silva

DiGiovanni

Kumar

et al. 2020

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

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Membrane-bound organelles in eukaryotic cells form an interactive network to coordinate and facilitate cellular functions. The formation of close contacts, termed “membrane contact sites” (MCSs), represents an intriguing strategy for organelle interaction and coordinated interplay. Emerging research is rapidly revealing new details of MCSs. They represent ubiquitous and diverse structures, which are important for many aspects of cell physiology and homeostasis. Here, we provide a comprehensive overview of the physiological relevance of organelle contacts. We focus on mitochondria, peroxisomes, the Golgi complex and the plasma membrane, and discuss the most recent findings on their interactions with other subcellular organelles and their multiple functions, including membrane contacts with the ER, lipid droplets and the endosomal/lysosomal compartment.

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The diversity of ACBD proteins – From lipid binding to protein modulators and organelle tethers

Cited by 36 publications

References 184 publications

The diversity and breadth of cancer cell fatty acid metabolism

The diversity and breadth of cancer cell fatty acid metabolism

Peroxisomal Metabolite and Cofactor Transport in Humans

Maintaining social contacts: The physiological relevance of organelle interactions

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