HSPA8 binds substrate

Stable Identifier
R-HSA-9615721
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Intracellular proteins are targeted for proteolytic degradation in the lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds substrate proteins in the cytosol. HSPA8 recognizes a motif based on the charge of the amino acids (Chiang H et al. 1989, Dice JF et al. 1990). This allows the motif to have multiple sequence possibilities and also create a motif through post-translational modifications such as phosphorylation and acetylation. Once bound with HSPA8, the substrates are targeted to the lysosome or endosome.

Literature References
PubMed ID Title Journal Year
25961502 Degradation of lipid droplet-associated proteins by chaperone-mediated autophagy facilitates lipolysis

Kaushik, S, Cuervo, AM

Nat. Cell Biol. 2015
2799391 A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins

Chiang, HL, Terlecky, SR, Plant, CP, Dice, JF

Science 1989
2204156 Peptide sequences that target cytosolic proteins for lysosomal proteolysis

Dice, JF

Trends Biochem. Sci. 1990
Participants
Participant Of
Inferred From
Authored
Reviewed
Created
Cite Us!