p-GFAP binds EEF1A1

Stable Identifier
R-HSA-9626046
Type
Reaction [binding]
Species
Homo sapiens
Compartment
lysosomal membrane
ReviewStatus
5/5
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p-GFAP binds EEF1A1
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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
20797626 Identification of regulators of chaperone-mediated autophagy

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

Mol. Cell 2010
26118642 Lysosomal mTORC2/PHLPP1/Akt Regulate Chaperone-Mediated Autophagy

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

Mol. Cell 2015
Participants
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Output
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Inferred From
p-Gfap binds Eef1a1 (Rattus norvegicus)
Authored
Varusai, TM  (2019-02-21)
Reviewed
Metzakopian, E  (2019-02-22)
Created
Varusai, TM  (2018-10-25)
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