Hspa8 dissociates from Lamp2a-bound substrate

Stable Identifier
R-RNO-9622832
Type
Reaction [dissociation]
Species
Rattus norvegicus
Compartment
ReviewStatus
5/5
General
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Hspa8 dissociates from Lamp2a-bound substrate
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 a KFERQ-domain containing substrate in the cytosol. Consequently, the substrate:Hspa8 complex translocates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (Lamp2). Post-binding, Hspa8 is released from the complex to allow multimerization of Lamp2 and internalization of the substrate (Bandyopadhyay U et al. 2008).
Literature References
PubMed ID Title Journal Year
18644871 The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane

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

Mol. Cell. Biol. 2008
29626215 The coming of age of chaperone-mediated autophagy

Cuervo, AM, Kaushik, S

Nat. Rev. Mol. Cell Biol. 2018
Participants
Orthologous Events
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