GFAP binds LAMP2a multimer

Stable Identifier
R-HSA-9625197
Type
Reaction [binding]
Species
Homo sapiens
Compartment
lysosomal lumen, lysosomal membrane
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GFAP binds LAMP2a multimer
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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. This LAMP2a 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. Experiments confirming this binding were performed on rat models.

Literature References
PubMed ID Title Journal Year
21282471 Chaperone-mediated autophagy at a glance

Kaushik, S, Bandyopadhyay, U, Sridhar, S, Kiffin, R, Martinez-Vicente, M, Kon, M, Orenstein, SJ, Wong, E, Cuervo, AM

J. Cell. Sci. 2011
20797626 Identification of regulators of chaperone-mediated autophagy

Bandyopadhyay, U, Sridhar, S, Kaushik, S, Kiffin, R, Cuervo, AM

Mol. Cell 2010
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Inferred From
Gfap binds Lamp2 multimer (Rattus norvegicus)
Authored
Varusai, TM  (2019-02-21)
Reviewed
Metzakopian, E  (2019-02-22)
Created
Varusai, TM  (2018-10-19)