Journal Article

FZJ-2018-05901

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Phasing out the bad-How SQSTM1/p62 sequesters ubiquitinated proteins for degradation by autophagy

Zaffagnini, G. ; Savova, A. ; Danieli, A. ; Romanov, J. ; Tremel, S. ; Ebner, M. ; Peterbauer, T. ; Sztacho, M. ; Trapannone, R. ; Tarafder, A. K. ; Sachse, C.FZJ* ; Martens, S. (Corresponding author)

2018
Taylor & Francis Abingdon, Oxon

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Please use a persistent id in citations: http://hdl.handle.net/2128/20142  doi:10.1080/15548627.2018.1462079

Abstract: The degradation of misfolded, ubiquitinated proteins is essential for cellular homeostasis. These proteins are primarily degraded by the ubiquitin-proteasome system (UPS) and macroautophagy/autophagy serves as a backup mechanism when the UPS is overloaded. How autophagy and the UPS are coordinated is not fully understood. During the autophagy of misfolded, ubiquitinated proteins, referred to as aggrephagy, substrate proteins are clustered into larger structures in a SQSTM1/p62-dependent manner before they are sequestered by phagophores, the precursors to autophagosomes. We have recently shown that SQSTM1/p62 and ubiquitinated proteins spontaneously phase separate into micrometer-sized clusters in vitro. This enabled us to characterize the properties of the ubiquitin-positive substrates that are necessary for the SQSTM1/p62-mediated cluster formation. Our results suggest that aggrephagy is triggered by the accumulation of substrates with multiple ubiquitin chains and that the process can be inhibited by active proteasomes.

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Contributing Institute(s):

1. Strukturbiologie (ER-C-3)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2018

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Database coverage:
; ; ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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