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HSPA8 binds LAMP2a multimers
Stable Identifier
R-HSA-9626253
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 binds LAMP2a multimers (Homo sapiens)
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The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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 and triggers their disassembly. Interestingly, substrate bound HSPA8 do not have this effect on LAMP2a (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 [cytosol]
(Homo sapiens)
LAMP2a multimer complex [lysosomal lumen]
(Homo sapiens)
Output
HSPA8:LAMP2a multimers [cytosol]
(Homo sapiens)
Participates
as an event of
Chaperone Mediated Autophagy (Homo sapiens)
Inferred From
Hspa8 binds Lamp2 multimers (Rattus norvegicus)
Authored
Varusai, TM (2019-02-21)
Reviewed
Metzakopian, E (2019-02-22)
Created
Varusai, TM (2018-10-26)
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