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https://hdl.handle.net/2440/83397
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Type: | Journal article |
Title: | Chaperone-assisted selective autophagy is essential for muscle maintenance |
Author: | Arndt, V. Dick, N. Tawo, R. Dreiseidler, M. Wenzel, D. Hesse, M. Furst, D. Saftig, P. Saint, R. Fleischmann, B. Hoch, M. Hohfeld, J. |
Citation: | Current Biology, 2010; 20(2):143-148 |
Publisher: | Dell Press |
Issue Date: | 2010 |
ISSN: | 0960-9822 1879-0445 |
Department: | Division of the Deputy Vice-Chancellor and Vice-President (Research) |
Statement of Responsibility: | Verena Arndt, Nikolaus Dick, Riga Tawo, Michael Dreiseidler, Daniela Wenzel, Michael Hesse, Dieter O. Fürst, Paul Saftig, Robert Saint, Bernd K. Fleischmann, Michael Hoch, and Jörg Höhfeld |
Abstract: | How are biological structures maintained in a cellular environment that constantly threatens protein integrity? Here we elucidate proteostasis mechanisms affecting the Z disk, a protein assembly essential for actin anchoring in striated muscles, which is subjected to mechanical, thermal, and oxidative stress during contraction [1]. Based on the characterization of the Drosophila melanogaster cochaperone Starvin (Stv), we define a conserved chaperone machinery required for Z disk maintenance. Instead of keeping Z disk proteins in a folded conformation, this machinery facilitates the degradation of damaged components, such as filamin, through chaperone-assisted selective autophagy (CASA). Stv and its mammalian ortholog BAG-3 coordinate the activity of Hsc70 and the small heat shock protein HspB8 during disposal that is initiated by the chaperone-associated ubiquitin ligase CHIP and the autophagic ubiquitin adaptor p62. CASA is thus distinct from chaperone-mediated autophagy, previously shown to facilitate the ubiquitin-independent, direct translocation of a client across the lysosomal membrane [2]. Impaired CASA results in Z disk disintegration and progressive muscle weakness in flies, mice, and men. Our findings reveal the importance of chaperone-assisted degradation for the preservation of cellular structures and identify muscle as a tissue that highly relies on an intact proteostasis network, thereby shedding light on diverse myopathies and aging. |
Keywords: | Proteins Cellbio Humdisease |
Rights: | ©2010 Elsevier Ltd All rights reserved |
DOI: | 10.1016/j.cub.2009.11.022 |
Published version: | http://dx.doi.org/10.1016/j.cub.2009.11.022 |
Appears in Collections: | Aurora harvest 4 Genetics publications |
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