The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Ubiquitin signals autophagic degradation of cytosolic proteins and peroxisomes
Open accessAbstract
Autophagy is responsible for nonspecific, bulk degradation of cytoplasmic components. Recent work has revealed also that there is specific, autophagic degradation of polyubiquitinated protein aggregates, whose buildup occurs during neurodegenerative disease. Here, we report that simple mono-ubiquitination of normally long-lived cytoplasmic substrates is sufficient to target these substrates for autophagic degradation in mammalian cells. That is, upon their ubiquitination, both small [i.e., red fluorescent protein (RFP)] and large (i.e., peroxisomes) substrates are efficiently targeted to autophagosomes and then degraded within lysosomes upon autophagosome-lysosome fusion. This targeting requires the ubiquitin-binding protein, p62, and is blocked by the Class III phosphatidylinositol 3-kinase (PI3K) inhibitor, 3-methyladenine (3-MA), or by depletion of the autophagy-related-12 (Atg12) protein homolog. Mammalian cells thus use a common pathway involving ubiquitin and p62 for targeting diverse types of substrates for autophagy.
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Self-citation
Cited by
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609
PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
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Eaten alive: a history of macroautophagy
Yang, Z., & Klionsky, D. J. (2010) · Nature Cell Biology · doi:10.1038/ncb0910-814 · Cited by 2,095
The machinery of macroautophagy
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A Role for Ubiquitin in Selective Autophagy
Kirkin, V., McEwan, D. G., Novak, I., & Dikic, I. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.026 · Cited by 1,239
Metadata
- Authors
- Kim, P. K., Hailey, D. W., Mullen, R. T., & Lippincott-Schwartz, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2008-12-30
- Volume
- 105
- Issue
- 52
- Pages
- 20567-20574
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2129321855
- Cited by
- 532
- References
- 48
- FWCI
- 27.59
- Type
- journal article
- Language
- en
- Open access
- green
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