p-GFAP binds EEF1A1

Stable Identifier
R-HSA-9626046
Type
Reaction [binding]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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 (LAMP2a). Subsequently, LAMP2a forms a multimeric complex stabilized with the aid of HSP90 and glial fibrillary acidic protein (GFAP). This multimer allows the transfer of substrate into the lumen. The stability of this complex is regulated by the dynamics of GFAP and elongation factor 1α (EEF1A1). During autophagy, a phosphorylated version of GFAP remains bound to EEF1A1 (Bandyopadhyay U et al. 2010, Arias E et al. 2015). Experiments confirming this binding were performed in rats.

Literature References
PubMed ID Title Journal Year
26118642 Lysosomal mTORC2/PHLPP1/Akt Regulate Chaperone-Mediated Autophagy

Arias, E, Koga, H, Diaz, A, Mocholi, E, Patel, B, Cuervo, AM

Mol. Cell 2015
20797626 Identification of regulators of chaperone-mediated autophagy

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

Mol. Cell 2010
Participants
Participant Of
Orthologous Events
Authored
Reviewed
Created