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The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.

p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding

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Itakura, Eisuke, Mizushima, Noboru·2011·Journal of Cell Biology

Abstract

Autophagy is an intracellular degradation process by which cytoplasmic contents are degraded in the lysosome. In addition to nonselective engulfment of cytoplasmic materials, the autophagosomal membrane can selectively recognize specific proteins and organelles. It is generally believed that the major selective substrate (or cargo receptor) p62 is recruited to the autophagosomal membrane through interaction with LC3. In this study, we analyzed loading of p62 and its related protein NBR1 and found that they localize to the endoplasmic reticulum (ER)–associated autophagosome formation site independently of LC3 localization to membranes. p62 colocalizes with upstream autophagy factors such as ULK1 and VMP1 even when autophagosome formation is blocked by wortmannin or FIP200 knockout. Self-oligomerization of p62 is essential for its localization to the autophagosome formation site. These results suggest that p62 localizes to the autophagosome formation site on the ER, where autophagosomes are nucleated. This process is similar to the yeast cytoplasm to vacuole targeting pathway.

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Metadata

Authors
Itakura, E., & Mizushima, N.
Venue
Journal of Cell Biology
Published
2011-01-10
Volume
192
Issue
1
Pages
17-27
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2078013685
Cited by
416
References
64
FWCI
25.93
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. https://app.cochat.ai/papers/10.1083/jcb.201009067
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Itakura, E., & Mizushima, N. (2011). p62 targeting to the autophagosome formation site requires self-oligomerization but not LC3 binding. Journal of Cell Biology. https://doi.org/10.1083/jcb.201009067

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