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https://hdl.handle.net/2440/83397
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dc.contributor.author | Arndt, V. | - |
dc.contributor.author | Dick, N. | - |
dc.contributor.author | Tawo, R. | - |
dc.contributor.author | Dreiseidler, M. | - |
dc.contributor.author | Wenzel, D. | - |
dc.contributor.author | Hesse, M. | - |
dc.contributor.author | Furst, D. | - |
dc.contributor.author | Saftig, P. | - |
dc.contributor.author | Saint, R. | - |
dc.contributor.author | Fleischmann, B. | - |
dc.contributor.author | Hoch, M. | - |
dc.contributor.author | Hohfeld, J. | - |
dc.date.issued | 2010 | - |
dc.identifier.citation | Current Biology, 2010; 20(2):143-148 | - |
dc.identifier.issn | 0960-9822 | - |
dc.identifier.issn | 1879-0445 | - |
dc.identifier.uri | http://hdl.handle.net/2440/83397 | - |
dc.description.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. | - |
dc.description.statementofresponsibility | 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 | - |
dc.language.iso | en | - |
dc.publisher | Dell Press | - |
dc.rights | ©2010 Elsevier Ltd All rights reserved | - |
dc.source.uri | http://dx.doi.org/10.1016/j.cub.2009.11.022 | - |
dc.subject | Proteins | - |
dc.subject | Cellbio | - |
dc.subject | Humdisease | - |
dc.title | Chaperone-assisted selective autophagy is essential for muscle maintenance | - |
dc.type | Journal article | - |
dc.contributor.department | Division of the Deputy Vice-Chancellor and Vice-President (Research) | - |
dc.identifier.doi | 10.1016/j.cub.2009.11.022 | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 4 Genetics publications |
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