| created | [InstanceEdit:9625192] Varusai, Thawfeek, 2018-10-19 |
| dbId | 9625198 |
| displayName | Intracellular proteins are targeted for proteolytic degradat... |
| modified | [InstanceEdit:9634155] Varusai, Thawfeek, 2019-01-07 |
| schemaClass | Summation |
| text | 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. Consequently, the substrate:HSPA8 complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (Lamp2). Subsequently, Hspa8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of Lamp2. This Lamp2 complex then multimerizes into a 700 kDa entity and is stabilized by the binding of Glial fibrillary acidic protein (Gfap) (Bandyopadhyay U et al. 2010). Subsequently, the substrate is unfolded and internalized into the lumen. |
| (summation) |
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