The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy

Mónika Lippai, P. Lőw

Research output: Contribution to journalArticle

148 Citations (Scopus)

Abstract

The ubiquitin-proteasome system and autophagy were long viewed as independent, parallel degradation systems with no point of intersection. By now we know that these degradation pathways share certain substrates and regulatory molecules and show coordinated and compensatory function. Two ubiquitin-like protein conjugation pathways were discovered that are required for autophagosome biogenesis: the Atg12-Atg5-Atg16 and Atg8 systems. Autophagy has been considered to be essentially a nonselective process, but it turned out to be at least partially selective. Selective substrates of autophagy include damaged mitochondria, intracellular pathogens, and even a subset of cytosolic proteins with the help of ubiquitin-binding autophagic adaptors, such as p62/SQSTM1, NBR1, NDP52, and Optineurin. These proteins selectively recognize autophagic cargo and mediate its engulfment into autophagosomes by binding to the small ubiquitin-like modifiers that belong to the Atg8/LC3 family.

Original languageEnglish
Article number832704
JournalBioMed Research International
Volume2014
DOIs
Publication statusPublished - 2014

Fingerprint

Ubiquitins
Autophagy
Ubiquitin
Degradation
Mitochondria
Pathogens
Proteasome Endopeptidase Complex
Substrates
Proteins
Molecules
Autophagosomes

ASJC Scopus subject areas

  • Immunology and Microbiology(all)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Medicine(all)

Cite this

The role of the selective adaptor p62 and ubiquitin-like proteins in autophagy. / Lippai, Mónika; Lőw, P.

In: BioMed Research International, Vol. 2014, 832704, 2014.

Research output: Contribution to journalArticle

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