RGD Reference Report - Chaperone-assisted selective autophagy is essential for muscle maintenance. - Rat Genome Database

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Chaperone-assisted selective autophagy is essential for muscle maintenance.

Authors: Arndt, V  Dick, N  Tawo, R  Dreiseidler, M  Wenzel, D  Hesse, M  Furst, DO  Saftig, P  Saint, R  Fleischmann, BK  Hoch, M  Hohfeld, J 
Citation: Arndt V, etal., Curr Biol. 2010 Jan 26;20(2):143-8. doi: 10.1016/j.cub.2009.11.022. Epub 2010 Jan 7.
RGD ID: 10448947
Pubmed: PMID:20060297   (View Abstract at PubMed)
DOI: DOI:10.1016/j.cub.2009.11.022   (Journal Full-text)

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.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
ATP hydrolysis activity enablesIDA 10448947PMID:20060297MGI 

Objects Annotated

Genes (Rattus norvegicus)
Hspa8  (heat shock protein family A (Hsp70) member 8)


Additional Information