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Unfolded substrate in Lamp2 multimeric complex binds Hspa8
Stable Identifier
R-RNO-9625173
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
lysosomal lumen
,
lysosomal membrane
ReviewStatus
5/5
General
SBML
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BioPAX
Level 2
Level 3
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SBGN
Intracellular proteins are targeted for proteolytic degradation in the 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 and translocates to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (Lamp2). Subsequently, Hspa8 is released and Heat shock protein Hsp90 binds to the lysosomal luminal end of Lamp2. The Lamp2 complex then multimerizes and stabilizes. Now, the substrate unfolds and binds to Hspa8 in the lysosomal lumen (Agarraberes FA et al. 1997, Cuervo AM et al. 1997). Subsequently, the substrate is internalized and degraded in the lumen.
Literature References
PubMed ID
Title
Journal
Year
9151685
An intralysosomal hsp70 is required for a selective pathway of lysosomal protein degradation
Dice, JF
,
Agarraberes, FA
,
Terlecky, SR
J. Cell Biol.
1997
9038169
A population of rat liver lysosomes responsible for the selective uptake and degradation of cytosolic proteins
Dice, JF
,
Cuervo, AM
,
Knecht, E
J. Biol. Chem.
1997
Participants
Input
Hspa8 [lysosomal lumen]
(Rattus norvegicus)
Lamp2 multimer complex: Gfap [lysosomal membrane]
(Rattus norvegicus)
Output
Hspa8:Lamp2 multimeric complex [lysosomal membrane]
(Rattus norvegicus)
Orthologous Events
Unfolded substrate in LAMP2a multimeric complex binds HSPA8 (Homo sapiens)
Authored
Varusai, TM (2019-11-08)
Reviewed
Metzakopian, E (2019-02-22)
Created
Varusai, TM (2018-10-19)
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