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Hspa8 dissociates from Lamp2a-bound substrate
Stable Identifier
R-RNO-9622832
Type
Reaction [dissociation]
Species
Rattus norvegicus
Compartment
cytosol
,
lysosomal membrane
ReviewStatus
5/5
General
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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 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
Input
Hspa8:Rnase1:Lamp2 [lysosomal membrane]
(Rattus norvegicus)
Output
Hspa8 [cytosol]
(Rattus norvegicus)
Rnase1:Lamp2 [lysosomal membrane]
(Rattus norvegicus)
Orthologous Events
HSPA8 dissociates from LAMP2A-bound substrate (Homo sapiens)
Authored
Varusai, TM (2019-11-08)
Reviewed
Metzakopian, E (2019-02-22)
Created
Varusai, TM (2018-10-02)
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