4.6 Review

Oligomerization of Selective Autophagy Receptors for the Targeting and Degradation of Protein Aggregates

Journal

CELLS
Volume 10, Issue 8, Pages -

Publisher

MDPI
DOI: 10.3390/cells10081989

Keywords

receptors; autophagy; proteasome; ubiquitin; p62; Dsk2; Cue5; TAX1BP1

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Funding

  1. National Key R&D Program of China [2017YFA0506300]

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This article summarizes the mechanisms of action of receptors in selective protein aggregate autophagy and recent research progress, with a particular focus on how oligomerization of receptors affects pathway determinants and promotes phase separation.
The selective targeting and disposal of solid protein aggregates are essential for cells to maintain protein homoeostasis. Autophagy receptors including p62, NBR1, Cue5/TOLLIP (CUET), and Tax1-binding protein 1 (TAX1BP1) proteins function in selective autophagy by targeting ubiquitinated aggregates through ubiquitin-binding domains. Here, we summarize previous beliefs and recent findings on selective receptors in aggregate autophagy. Since there are many reviews on selective autophagy receptors, we focus on their oligomerization, which enables receptors to function as pathway determinants and promotes phase separation.

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