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Details on Person Intracellular proteins are targeted for proteolytic degradat...
| Class:Id | Summation:9624152 |
|---|---|
| _displayName | Intracellular proteins are targeted for proteolytic degradat... |
| _timestamp | 2019-01-07 11:53:06 |
| created | [InstanceEdit:9624150] Varusai, Thawfeek, 2018-10-08 |
| modified | [InstanceEdit:9624163] Varusai, Thawfeek, 2018-10-08 [InstanceEdit:9634155] Varusai, Thawfeek, 2019-01-07 |
| 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 KFERQ-domain containing substrates in the cytosol. Consequently, the Hspa8:Substrate complex translocates from cytosol to lysosomal membrane where it binds to Lysosome-associated membrane glycoprotein 2 (LAMP2a). Subsequently, HSPA8 is released and Heat shock protein HSP 90 binds to the lysosomal luminal end of LAMP2a. Binding of HSP90 stabilizes LAMP2 to multimerize into a 700 kDa complex (Bandyopadhyay U et al. 2008). This facilitates the internalization of substrate into the lumen. Experiments confirming this binding were performed on rat models. |
| (summation) | [Polymerisation:9624158] Substrate:LAMP2a:HSP90 polymerizes [Homo sapiens] |
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