HSPA8:LAMP2a multimers depolymerizes to monomers

Stable Identifier
R-HSA-9626256
Type
Reaction [transition]
Species
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

Bandyopadhyay, U, Kaushik, S, Varticovski, L, Cuervo, AM

Mol. Cell. Biol. 2008
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