GFAP binds LAMP2a multimer

Stable Identifier
Homo sapiens
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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
20797626 Identification of regulators of chaperone-mediated autophagy

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

Mol. Cell 2010
21282471 Chaperone-mediated autophagy at a glance

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

J. Cell. Sci. 2011
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