Lysosomes, a meeting point of proteins, chaperones, and proteases

Ana Maria Cuervo, J. Fred Dice

Research output: Contribution to journalArticle

183 Citations (Scopus)

Abstract

Lysosomes, classically considered as nonspecific systems for protein degradation, have recently also been shown to be able selectively to degrade specific intracellular proteins. Here we review this selective pathway of lysosomal protein degradation that involves cytosolic and intralysosomal chaperones and a receptor in the lysosomal membrane. This pathway is highly selective for cytosolic proteins containing a lysosomal targeting signal. The selective lysosomal degradation pathway is active under conditions of nutrient deprivation and plays an important role in the regulation of intracellular protein levels in stress situations. Several physiological and pathological modifications in the activity of this selective lysosomal pathway of protein degradation are discussed.

Original languageEnglish (US)
Pages (from-to)6-12
Number of pages7
JournalJournal of Molecular Medicine
Volume76
Issue number1
StatePublished - 1998
Externally publishedYes

Fingerprint

Lysosomes
Proteolysis
Peptide Hydrolases
Proteins
Food
Membranes
lysosomal proteins

Keywords

  • Lysosomes
  • Membrane transport
  • Molecular chaperones
  • Protein degradation
  • Proteolysis
  • Starvation

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Lysosomes, a meeting point of proteins, chaperones, and proteases. / Cuervo, Ana Maria; Dice, J. Fred.

In: Journal of Molecular Medicine, Vol. 76, No. 1, 1998, p. 6-12.

Research output: Contribution to journalArticle

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