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HSPA8:LAMP2a multimers depolymerizes to monomers
Stable Identifier
R-HSA-9626256
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
,
lysosomal membrane
ReviewStatus
5/5
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Autophagy (Homo sapiens)
Chaperone Mediated Autophagy (Homo sapiens)
HSPA8:LAMP2a multimers depolymerizes to monomers (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) transports substrates from the cytosol to the lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of HSPA8. Cytosolic HSPA8 binds with LAMP2a multimers in the lysosomal membrane. This triggers the disassembly of multimeric complexes into monomeric units (Bandyopadhyay U et al. 2008). Experiments confirming this event were performed in rats.
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
Participants
Input
HSPA8:LAMP2a multimers [cytosol]
(Homo sapiens)
Output
HSPA8:LAMP2a multimers [lysosomal membrane]
(Homo sapiens)
Participates
as an event of
Chaperone Mediated Autophagy (Homo sapiens)
Inferred From
Hspa8:Lamp2 multimers depolymerizes to monomers (Rattus norvegicus)
Authored
Varusai, TM (2019-02-21)
Reviewed
Metzakopian, E (2019-02-22)
Created
Varusai, TM (2018-10-26)
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