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

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 293, Issue 15, Pages 5414-5424

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.R117.818237

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Funding

  1. National Institutes of Health from NIA [AG021904, AG031782, AG038072, AG054108]
  2. National Institutes of Health from NINDS [NS100717]
  3. National Institutes of Health from NIDDK [DK098408]
  4. Leducq Network Award [RA15CVD04]
  5. Rainwaters Foundation
  6. Glen Foundation
  7. Backus Foundation

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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.

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