The role of ubiquitin in autophagy-dependent protein aggregate processing

Published

Journal Article

The efficient management of misfolded protein aggregates is essential for cell viability and requires 3 interconnected pathways: the molecular chaperone machinery that assists protein folding, the proteasome pathway that degrades misfolded proteins, and the aggresomal pathway that sequesters and delivers toxic protein aggregates to autophagy for clearance. Although autophagy is generally considered as nonselective degradative machinery, growing evidence supports the existence of a selective autophagy that specifically targets protein aggregates for clearance. This "quality control autophagy" is established by specific ubiquitin E3 ligases, autophagic substrate ubiquitination, and specific ubiquitin-binding proteins p62 and HDAC6. In this context, quality control autophagy is similar to the proteasome system and utilizes ubiquitin tags for substrate recognition and processing. Here, I will discuss the recent progress toward understanding the molecular basis of this unique form of ubiquitin-dependent autophagy in protein aggregate clearance and its relevance to disease. © The Author(s) 2010.

Full Text

Duke Authors

Cited Authors

  • Yao, TP

Published Date

  • December 1, 2010

Published In

Volume / Issue

  • 1 / 7

Start / End Page

  • 779 - 786

Electronic International Standard Serial Number (EISSN)

  • 1947-6027

International Standard Serial Number (ISSN)

  • 1947-6019

Digital Object Identifier (DOI)

  • 10.1177/1947601910383277

Citation Source

  • Scopus