Peroxisomal ACBD4 interacts with VAPB and promotes ER-peroxisome associations

Costello, Joseph L.; Castro, Inês G.; Schrader, Tina A.; Islinger, Markus; Schrader, Michael

doi:10.1080/15384101.2017.1314422

Cited by 73 publications

(74 citation statements)

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“…In mammals, the ER has the most abundant contact sites for peroxisomes (more than 90% of peroxisomes contact the ER) followed by mitochondria (~ 20%) and LDs (~ 20%) . Recently, two independent groups identified the tethers between the ER and peroxisomes in mammals (Fig B). The ER tethers are the vesicle‐associated membrane protein (VAMP)‐associated proteins (VAPs), which are implicated in tethering several different MCSs .…”

Section: Introductionmentioning

confidence: 99%

Peroxisome biogenesis, membrane contact sites, and quality control

et al. 2018

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Peroxisomes are conserved organelles of eukaryotic cells with important roles in cellular metabolism, human health, redox homeostasis, as well as intracellular metabolite transfer and signaling. We review here the current status of the different co‐existing modes of biogenesis of peroxisomal membrane proteins demonstrating the fascinating adaptability in their targeting and sorting pathways. While earlier studies focused on peroxisomes as autonomous organelles, the necessity of the ER and potentially even mitochondria as sources of peroxisomal membrane proteins and lipids has come to light in recent years. Additionally, the intimate physical juxtaposition of peroxisomes with other organelles has transitioned from being viewed as random encounters to a growing appreciation of the expanding roles of such inter‐organellar membrane contact sites in metabolic and regulatory functions. Peroxisomal quality control mechanisms have also come of age with a variety of mechanisms operating both during biogenesis and in the cellular response to environmental cues.

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Section: Introductionmentioning

confidence: 99%

Peroxisome biogenesis, membrane contact sites, and quality control

et al. 2018

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“…Consequently, all TA proteins are imported in membranes posttranslationally (Chio et al ., ; Costello et al ., ; ). In addition to mitochondria, TA proteins are components of other membrane‐bound organelles, such as the endoplasmic reticulum (ER), peroxisomes, and in plants, the outer membrane of plastids (Kriechbaumer et al ., ; Chio et al ., ; Costello et al ., ; ). Altogether, TA proteins represent 3–5% of the eukaryotic membrane proteome (Hegde and Keenan, ).…”

Section: Introductionmentioning

confidence: 99%

“…Subtle changes in the properties of the C‐tail anchor can mistarget mitochondrial TA proteins to the cytosol or ER (Kuroda et al ., ; Borgese et al ., ; Hwang et al ., ; Henderson et al ., ). Particularly, interplay between the tail charge and TMD hydrophobicity appeared to be critical to control the correct targeting of TA proteins into the cellular organelles including ER, mitochondria and peroxisome (Costello et al ., ; ).…”

Section: Introductionmentioning

confidence: 99%

“…They are based on the interaction of TA proteins with (i) the signal recognition particle (SRP‐assisted insertion), (ii) the Hsc70/Hsp40 system of chaperones, (iii) targeting and insertion via the Guided Entry of TA protein (GET) pathway (Abell et al ., ; ; Schuldiner et al ., ; Rabu et al ., ; Brkljacic et al ., ; Colombo and Fasana, ; Chio et al ., ; Costello et al ., ; ) and (iv) the recently discovered SRP‐independent pathway (SND) that can partially substitute for the SRP and GET pathways (Aviram et al ., ; Casson et al ., ). The characteristic feature of the yeast ER proteins is a higher hydrophobicity of the TMD in comparison to the mitochondrial TA proteins, although this feature is not clearly different in human cells (Costello et al ., ; ). The sorting of TA proteins into peroxisomes is based on their recognition by the import receptor Pex19.…”

Section: Introductionmentioning

confidence: 99%

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Targeting of tail‐anchored proteins to Trichomonas vaginalis hydrogenosomes

Rada

Makki

Žárský

et al. 2019

Molecular Microbiology

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Summary Tail‐anchored (TA) proteins are membrane proteins that are found in all domains of life. They consist of an N‐terminal domain that performs various functions and a single transmembrane domain (TMD) near the C‐terminus. In eukaryotes, TA proteins are targeted to the membranes of mitochondria, the endoplasmic reticulum (ER), peroxisomes and in plants, chloroplasts. The targeting of these proteins to their specific destinations correlates with the properties of the C‐terminal domain, mainly the TMD hydrophobicity and the net charge of the flanking regions. Trichomonas vaginalis is a human parasite that has adapted to oxygen‐poor environment. This adaptation is reflected by the presence of highly modified mitochondria (hydrogenosomes) and the absence of peroxisomes. The proteome of hydrogenosomes is considerably reduced; however, our bioinformatic analysis predicted 120 putative hydrogenosomal TA proteins. Seven proteins were selected to prove their localization. The elimination of the net positive charge in the C‐tail of the hydrogenosomal TA4 protein resulted in its dual localization to hydrogenosomes and the ER, causing changes in ER morphology. Domain mutation and swap experiments with hydrogenosomal (TA4) and ER (TAPDI) proteins indicated that the general principles for specific targeting are conserved across eukaryotic lineages, including T. vaginalis; however, there are also significant lineage‐specific differences.

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“…Tethering complexes that connect the endoplasmic reticulum (ER) to peroxisomes have been described in cells of several species. In mammalian cells, the ER‐resident VAMP‐associated proteins A (VAPA) and B (VAPB) interact with the tail‐anchored peroxisomal membrane proteins acyl‐CoA binding domain proteins 4 (ACBD4) and 5 (ACBD5) to form a MCS involved in peroxisome maintenance and lipid homeostasis …”

Section: Introductionmentioning

confidence: 99%

Determinants of the assembly, integrity and maintenance of the endoplasmic reticulum‐peroxisome tether

Knoblach

Rachubinski

2019

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Organelle tethering and intercommunication are crucial for proper cell function. We previously described a tether between peroxisomes and the endoplasmic reticulum (ER) that acts in peroxisome population control in the yeast, Saccharomyces cerevisiae. Components of this tether are Pex3p, an integral membrane protein of both peroxisomes and the ER and Inp1p, a connector that links peroxisomes to the ER. Here, we report the analysis of random Inp1p mutants that enabled identification of regions in Inp1p required for the assembly and maintenance of the ER‐peroxisome tether. Interaction analysis between Inp1p mutants and known Inp1p‐binding proteins demonstrated that Pex3p and Inp1p do not constitute the sole components of the ER‐peroxisome tether. Deletion of these Inp1p interactors whose steady‐state localization is outside of ER‐peroxisome tethers affected peroxisome dynamics. Our findings are consistent with the presence of regulatory cues that act on ER‐peroxisome tethers and point to the existence of membrane contact sites between peroxisomes and organelles other than the ER.

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Peroxisomal ACBD4 interacts with VAPB and promotes ER-peroxisome associations

Cited by 73 publications

References 40 publications

Peroxisome biogenesis, membrane contact sites, and quality control

Peroxisome biogenesis, membrane contact sites, and quality control

Targeting of tail‐anchored proteins to Trichomonas vaginalis hydrogenosomes

Determinants of the assembly, integrity and maintenance of the endoplasmic reticulum‐peroxisome tether

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