Eef1a1 dissociates from p-Gfap

Stable Identifier
R-RNO-9626032
Type
Reaction [dissociation]
Species
Rattus norvegicus
Compartment
General
SVG |   | PPTX  | SBGN
Eef1a1 dissociates from p-Gfap

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 (Lamp2). Subsequently, Lamp2 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. When GTP becomes available, Eef1a1 dissociates from Gfap (Bandyopadhyay U et al. 2010).

Literature References
PubMed ID Title Journal Year
20797626 Identification of regulators of chaperone-mediated autophagy

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

Mol. Cell 2010
Participants
Orthologous Events
Authored
Reviewed
Created
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