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p-GFAP:GFAP dissociates from LAMP2a multimer
Stable Identifier
R-HSA-9626242
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
lysosomal membrane
ReviewStatus
5/5
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Autophagy (Homo sapiens)
Chaperone Mediated Autophagy (Homo sapiens)
p-GFAP:GFAP dissociates from LAMP2a multimer (Homo sapiens)
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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 and transfers the substrate into the lumen. The stability of this complex is regulated by the dynamics of glial fibrillary acidic protein (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 and binds with GTP in the cytosol. This makes p-GFAP available to bind with GFAP in the LAMP2a multimer complex. Consequently, p-GFAP sequesters GFAP from LAMP2a multimer (Bandyopadhyay U et al. 2010). Experiments confirming this event were performed in rats.
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
Participants
Input
p-GFAP:GFAP:LAMP2a multimer [lysosomal membrane]
(Homo sapiens)
Output
LAMP2a multimer complex [lysosomal lumen]
(Homo sapiens)
p-GFAP:GFAP [lysosomal membrane]
(Homo sapiens)
Participates
as an event of
Chaperone Mediated Autophagy (Homo sapiens)
Inferred From
p-Gfap:Gfap dissociates from Lamp2 multimer (Rattus norvegicus)
Authored
Varusai, TM (2019-02-21)
Reviewed
Metzakopian, E (2019-02-22)
Created
Varusai, TM (2018-10-26)
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