Peroxisomal ATP-binding cassette transporters form mainly tetramers

Autor: Quentin Raas, Alexandre M.M. Dias, Catherine Gondcaille, Géraldine Lucchi, Flore Geillon, Caroline Truntzer, Doriane Trompier, Stéphane Savary, Pierre Falson, Patrick Ducoroy, Delphine Pecqueur
Přispěvatelé: Laboratoire Bio-PeroxIL. Biochimie du peroxysome, inflammation et métabolisme lipidique [Dijon] (BIO-PEROXIL), Université de Bourgogne (UB)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Bourgogne Franche-Comté [COMUE] (UBFC), Plate-forme Protéomique CLIPP - Clinical and Innovation Proteomic Platform [Dijon] (CLIPP), Franche-Comté Électronique Mécanique, Thermique et Optique - Sciences et Technologies (UMR 6174) (FEMTO-ST), Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS)-Université de Technologie de Belfort-Montbeliard (UTBM)-Ecole Nationale Supérieure de Mécanique et des Microtechniques (ENSMM)-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie Moléculaire de l'Université de Bourgogne [Dijon] (ICMUB), Université de Bourgogne (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)-Université de Bourgogne (UB)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), Microbiologie moléculaire et biochimie structurale / Molecular Microbiology and Structural Biochemistry (MMSB), Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon-Centre National de la Recherche Scientifique (CNRS), Institut de biologie et chimie des protéines [Lyon] (IBCP), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon
Rok vydání: 2017
Předmět:
0301 basic medicine
Carcinoma
Hepatocellular
Green Fluorescent Proteins
protein assembly
ATP-binding cassette transporter
Calcium-Transporting ATPases
Plasma protein binding
fatty-acid transport
Biology
ATP Binding Cassette Transporter
Subfamily D
ATP Binding Cassette Transporter
Subfamily D
Member 1
Biochemistry
Mass Spectrometry
Cell Line
Protein–protein interaction
protein-protein interaction
Mice
03 medical and health sciences
Adenosine Triphosphate
Tandem Mass Spectrometry
Chlorocebus aethiops
Protein Interaction Mapping
Peroxisomes
Animals
peroxisome
Calcium Signaling
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry
Molecular Biology/Biochemistry [q-bio.BM]
Protein Structure
Quaternary
Molecular Biology
Peroxisomal targeting signal
030102 biochemistry & molecular biology
Liver Neoplasms
Cell Biology
Peroxisome
Rats
Transport protein
Protein Transport
030104 developmental biology
COS Cells
Protein Structure and Folding
ATP-Binding Cassette Transporters
Protein quaternary structure
ABC transporter
Protein Binding
Zdroj: Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2017, 292 (17), pp.6965-6977. ⟨10.1074/jbc.M116.772806⟩
ISSN: 0021-9258
1083-351X
Popis: International audience; ABCD1 and its homolog ABCD2 are peroxisomal ATP-binding cassette (ABC) half-transporters of fatty acyl-CoAs with both distinct and overlapping substrate specificities. Although it is established that ABC half-transporters have at least to dimerize to generate a functional unit, functional equivalents of tetramers (i.e. dimers of full-length transporters) have also been reported. However, oligomerization of peroxisomal ABCD transporters is incompletely understood but is of potential significance because more complex oligomerization might lead to differences in substrate specificity. In this work, we have characterized the quaternary structure of the ABCD1 and ABCD2 proteins in the peroxisomal membrane. Using various biochemical approaches, we clearly demonstrate that both transporters exist as both homo- and heterotetramers, with a predominance of homotetramers. In addition to tetramers, some larger molecular ABCD assemblies were also found but represented only a minor fraction. By using quantitative co-immunoprecipitation assays coupled with tandem mass spectrometry, we identified potential binding partners of ABCD2 involved in polyunsaturated fatty-acid metabolism. Interestingly, we identified calcium ATPases as ABCD2-binding partners, suggesting a role of ABCD2 in calcium signaling. In conclusion, we have shown here that ABCD1 and its homolog ABCD2 exist mainly as homotetramers in the peroxisomal membrane.
Databáze: OpenAIRE
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