The DOI matches its Crossref record; 46 of the 46 references it cites were found in a registry or an index.
p62/SQSTM 1 functions as a signaling hub and an autophagy adaptor
Abstract
p62/SQSTM 1 is a stress‐inducible cellular protein that is conserved among metazoans but not in plants and fungi. p62/SQSTM 1 has multiple domains that mediate its interactions with various binding partners and it serves as a signaling hub for diverse cellular events such as amino acid sensing and the oxidative stress response. In addition, p62/SQSTM 1 functions as a selective autophagy receptor for degradation of ubiqutinated substrates. In the present review, we describe the current knowledge about p62 with regard to mammalian target of rapamycin complex 1 activation, the Keap1–Nrf2 pathway and selective autophagy.
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Self-citationSelective autophagy mediated by autophagic adapter proteins
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The Dual Roles of NRF2 in Cancer
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Mechanistic insights into selective autophagy pathways: lessons from yeast
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Autophagy, Inflammation, and Immune Dysfunction in the Pathogenesis of Pancreatitis
Gukovskaya, A. S., Gukovsky, I., Algül, H., & Habtezion, A. (2017) · Gastroenterology · doi:10.1053/j.gastro.2017.08.071 · Cited by 357
Human Astrocytes Transfer Aggregated Alpha-Synuclein via Tunneling Nanotubes
Rostami, J., Holmqvist, S., Lindström, V., Sigvardson, J., Westermark, G. T., Ingelsson, M., Bergström, J., Roybon, L., & Erlandsson, A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.0983-17.2017 · Cited by 339
TRIM21 Ubiquitylates SQSTM1/p62 and Suppresses Protein Sequestration to Regulate Redox Homeostasis
Pan, J.-A., Sun, Y., Jiang, Y.-P., Bott, A. J., Jaber, N., Dou, Z., Yang, B., Chen, J.-S., Catanzaro, J. M., Du, C., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.007 · Cited by 265
Metadata
- Authors
- Katsuragi, Y., Ichimura, Y., & Komatsu, M.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2015-10-16
- Volume
- 282
- Issue
- 24
- Pages
- 4672-4678
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W2177646965
- Cited by
- 788
- References
- 46
- FWCI
- 47.70
- Type
- journal article
- Language
- en
- Open access
- closed
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