HSPA8 dissociates from LAMP2A-bound substrate

Stable Identifier
R-HSA-9622840
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
cytosol, lysosomal membrane
ReviewStatus
5/5
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HSPA8 dissociates from LAMP2A-bound substrate
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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
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
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Hspa8 dissociates from Lamp2a-bound substrate (Rattus norvegicus)
Authored
Varusai, TM  (2019-02-21)
Reviewed
Metzakopian, E  (2019-02-22)
Created
Varusai, TM  (2018-10-02)
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