Permanent URL to this publication: http://dx.doi.org/10.5167/uzh-31228
Krikin, V; Lamark, T; Sou, Y S; et al; Theurillat, J P (2009). A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Molecular Cell, 33(4):505-516.
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Autophagy is a catabolic process where cytosolic cellular components are delivered to the lysosome for degradation. Recent studies have indicated the existence of specific receptors, such as p62, which link ubiquitinated targets to autophagosomal degradation pathways. Here we show that NBR1 (neighbor of BRCA1 gene 1) is an autophagy receptor containing LC3- and ubiquitin (Ub)-binding domains. NBR1 is recruited to Ub-positive protein aggregates and degraded by autophagy depending on an LC3-interacting region (LIR) and LC3 family modifiers. Although NBR1 and p62 interact and form oligomers, they can function independently, as shown by autophagosomal clearance of NBR1 in p62-deficient cells. NBR1 was localized to Ub-positive inclusions in patients with liver dysfunction, and depletion of NBR1 abolished the formation of Ub-positive p62 bodies upon puromycin treatment of cells. We propose that NBR1 and p62 act as receptors for selective autophagosomal degradation of ubiquitinated targets.
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|Item Type:||Journal Article, not refereed, original work|
|Communities & Collections:||04 Faculty of Medicine > University Hospital Zurich > Institute of Surgical Pathology|
|Dewey Decimal Classification:||610 Medicine & health|
|Date:||26 February 2009|
|Deposited On:||12 Mar 2010 15:22|
|Last Modified:||05 Apr 2016 13:57|
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