Chaperone-mediated autophagy and endosomal microautophagy: Joint by a chaperone

J Biol Chem. 2018 Apr 13;293(15):5414-5424. doi: 10.1074/jbc.R117.818237. Epub 2017 Dec 15.

Abstract

A variety of mechanisms deliver cytosolic materials to the lysosomal compartment for degradation through autophagy. Here, we focus on two autophagic pathways, the chaperone-mediated autophagy and the endosomal microautophagy that rely on the cytosolic chaperone hsc70 for substrate targeting. Although hsc70 participates in the triage of proteins for degradation by different proteolytic systems, the common characteristic shared by these two forms of autophagy is that hsc70 binds directly to a specific five-amino acid motif in the cargo protein for its autophagic targeting. We summarize the current understanding of the molecular machineries behind each of these types of autophagy.

Keywords: autophagy; chaperone; lysosome; membrane protein; protein targeting; selective degradation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Animals
  • Autophagy*
  • Endosomes / genetics
  • Endosomes / metabolism*
  • HSC70 Heat-Shock Proteins / genetics
  • HSC70 Heat-Shock Proteins / metabolism*
  • Humans
  • Proteolysis*

Substances

  • HSC70 Heat-Shock Proteins
  • HSPA8 protein, human