Hspa8:Lamp2 multimers depolymerizes to monomers

Stable Identifier
R-RNO-9626254
Type
Reaction [transition]
Species
Rattus norvegicus
Compartment
ReviewStatus
5/5
General
SVG |   | PPTX  | SBGN
Hspa8:Lamp2 multimers depolymerizes to monomers
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 (Lamp2). Subsequently, Lamp2 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 Lamp2 multimers in the lysosomal membrane. This induces the disassembly of the multimeric complex into monomeric units (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
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Orthologous Events
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