p-Gfap binds Eef1a1

Stable Identifier
R-RNO-9626037
Type
Reaction [binding]
Species
Rattus norvegicus
Compartment
lysosomal membrane
ReviewStatus
5/5
General
SVG | 
PNG
Low
Medium
High
 | PPTX  | SBGN
p-Gfap binds Eef1a1
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 (Bandyopadhyay U et al. 2010, Arias E et al. 2015).
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
26118642 Lysosomal mTORC2/PHLPP1/Akt Regulate Chaperone-Mediated Autophagy

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

Mol. Cell 2015
Participants
Input
Output
Orthologous Events
p-GFAP binds EEF1A1 (Homo sapiens)
Authored
Varusai, TM  (2019-11-08)
Reviewed
Metzakopian, E  (2019-02-22)
Created
Varusai, TM  (2018-10-25)
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