| Overexpression of Dsk2/dUbqln results in severe developmental defects and lethality in Drosophila melanogaster that can be rescued by overexpression of the p54/Rpn10/S5a proteasomal subunit. | |
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MedLine Citation:
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PMID: 21973017 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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Polyubiquitin receptors execute the targeting of polyubiquitylated proteins to the 26S proteasome. In vitro studies indicate that disturbance of the physiological balance among different receptor proteins impairs the proteasomal degradation of polyubiquitylated proteins. To study the physiological consequences of shifting the in vivo equilibrium between the p54/Rpn10 proteasomal and the Dsk2/dUbqln extraproteasomal polyubiquitin receptors, transgenic Drosophila lines were constructed in which the overexpression or RNAi-mediated silencing of these receptors can be induced. Flies overexpressing Flag-p54 were viable and fertile, without any detectable morphological abnormalities, although detectable accumulation of polyubiquitylated proteins demonstrated a certain level of proteolytic disturbance. Flag-p54 was assembled into the 26S proteasome and could fully complement the lethal phenotype of a p54 null mutant Drosophila line. The overexpression of Dsk2 caused severe morphological abnormalities in the late pupal stages leading to pharate adult lethality, accompanied by a huge accumulation of highly polyubiquitylated proteins. The lethal phenotype of Dsk2 overexpression could be rescued in a double transgenic line coexpressing Flag-Dsk2 and Flag-p54. Although the double transgenic line was viable and fertile, it did not restore the proteolytic defects; the accumulation of the highly polyubiquitylated proteins was even more severe in the double transgenic line. Significant differences were found in the Dsk2-26S proteasome interaction in Drosophila melanogaster as compared with Saccharomyces cerevisiae. In yeast, Dsk2 can interact only with ΔRpn10 proteasomes and not with the wild-type one. In Drosophila Dsk2 does not interact with Δp54 proteasomes, but the interaction can be fully restored by complementing the Δp54 deletion with Flag-p54. Structureddigitalabstract: Dsk2 physically interacts with p54 by pulldown (View Interaction: 1, 2) p54 binds to Dsk2 by pulldown (View interaction). |
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Authors:
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Zoltán Lipinszki; Margit Pál; Olga Nagy; Péter Deák; Eva Hunyadi-Gulyas; Andor Udvardy |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-10-4 |
Journal Detail:
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Title: The FEBS journal Volume: - ISSN: 1742-4658 ISO Abbreviation: - Publication Date: 2011 Oct |
Date Detail:
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Created Date: 2011-10-6 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 101229646 Medline TA: FEBS J Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Journal compilation © 2011 Federation of European Biochemical Societies. |
Affiliation:
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Institute of Biochemistry, Biological Research Centre of the Hungarian Academy of Sciences. H-6701 Szeged, P.O.Box 521. Hungary. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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