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  Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex 1 and the heat-shock protein PBP74

Schwarzer, C., Barnikol-Watanabe, S., Thinnes, F. P., & Hilschmann, N. (2002). Voltage-dependent anion-selective channel (VDAC) interacts with the dynein light chain Tctex 1 and the heat-shock protein PBP74. International Journal of Biochemistry and Cell Biology, 34(9), 1059-1070.

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Schwarzer, C., Autor
Barnikol-Watanabe, Shitsu1, Autor           
Thinnes, F. P.1, Autor
Hilschmann, Norbert1, Autor           
Affiliations:
1Max Planck Institute of Experimental Medicine, Max Planck Society, ou_2173648              

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Schlagwörter: VDAC; porin; Tctex-l; PBP74; two-hybrid system; trafficking; chloride channels
 Zusammenfassung: The voltage-dependent anion-selective channel 1 (VDAC1), i.e. eukaryotic porin, functions as a channel in membranous structures as described for the outer mitochondrial membrane. the cell membrane, endosomes, caveolae, the sarcoplasmatic reticulum, synaptosomes. and post-synaptic density fraction. The identification of VDAC1 interacting proteins may be a promising approach for better understanding the biological context and function of the channel protein. In this study human VDAC1 was used as a bait protein in a two-hybrid screening, which is based on the Sos recruitment system (SRS). hVDAC1 interacts with the dynein light chain Tctex-1 and the heat-shock protein peptide-binding protein 74 (PBP74)/mitochondrial heat-shock protein 70 (mtHSP70)/glucose- regulated protein 75 (GRP75)/mortalin in vivo. Both interactions were confirmed by overlay-assays using recombinant partner proteins and purified hVDAC1. Indirect immunofluorescence on HeLa cells indicates a co-localisation of hVDAC1 with the dynein light chain and the PBP74. In addition, HeLa cells were transfected transiently with enhanced green fluorescent protein (EGFP)-hVDAC1 fusion proteins, which also clearly co-localise with both proteins. The functional relevance of the identified protein interactions was analysed in planar lipid bilayer (PLB) experiments. In these experiments both recombinant binding partners altered the electrophysiological properties of hVDAC1, While rTctex-1 increases the voltage-dependence of hVDAC1 slightly, the rPBP74 drastically minimises the voltage-dependence, indicating a modulation of channel properties in each case. Since the identified proteins are known to be involved in the transport or processing of proteins, the results of this study represent additional evidence of membrane-associated trafficking of the voltage-dependent anion-selective channel 1. (C) 2002 Elsevier Science Ltd. All rights reserved.

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Sprache(n): eng - English
 Datum: 2002-09
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: eDoc: 711991
ISI: 000176802100004
 Art des Abschluß: -

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Titel: International Journal of Biochemistry and Cell Biology
Genre der Quelle: Zeitschrift
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Ort, Verlag, Ausgabe: Exeter, England : Pergamon
Seiten: - Band / Heft: 34 (9) Artikelnummer: - Start- / Endseite: 1059 - 1070 Identifikator: ISSN: 1357-2725
CoNE: https://pure.mpg.de/cone/journals/resource/954927542149