HSPA8 dissociates from LAMP2A-bound substrate

Stable Identifier
Reaction [dissociation]
Homo sapiens
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Intracellular proteins are targeted for proteolytic degradation in lysosome with the aid of chaperones. Heat shock cognate 71 kDa protein (HSPA8) acts as the constitutive chaperone that binds KFERQ-domain containing substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Post-binding, HSPA8 is released from the complex to allow multimerization of LAMP2a and internalization of the substrate (Bandyopadhyay U et al. 2008). Experiments confirming this binding were performed on rat models.

Literature References
PubMed ID Title Journal Year
29626215 The coming of age of chaperone-mediated autophagy

Kaushik, S, Cuervo, AM

Nat. Rev. Mol. Cell Biol. 2018
18644871 The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane

Bandyopadhyay, U, Kaushik, S, Varticovski, L, Cuervo, AM

Mol. Cell. Biol. 2008
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