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AKT1 — HSPA5
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Mao et al., Am J Physiol Cell Physiol 2006
:
We found that the apoptotic effect of NE was associated with increased processing of ER-resident pro-caspase-12, cleavage of caspase-9 and -3, and mitochondrial release of cytochrome c. ER stress was evidenced by upregulation of ER chaperone
GRP78 and transcription factor CHOP and the translocation of XBP-1 from the ER to the nucleus by NE. NE also
reduced phospho-Akt ( Ser473 ), indicating suppression of the phosphatidylinositol 3-kinase ( PI3-kinase ) /Akt survival pathway
Misra et al., J Biol Chem 2006
(Prostatic Neoplasms) :
Silencing of
GRP78 gene expression by RNAi
suppressed activation of Akt ( Thr-308 ),
Akt ( Ser-473 ), and IkappaB kinase alpha kinase
Yamazaki et al., J Immunol 2009
:
These results suggested that loss of
GRP78 by SubAB
leads to transient phosphorylation of
Akt and consequent activation of NF-kappaB through the ATF6 branch of the UPR
Dai et al., Folia Biol (Praha) 2010
:
Importantly,
PI3K/Akt enhanced
GRP78 accumulation through increasing its stability following endoplasmic reticulum stress ... Furthermore,
Akt1 , but not Akt2 or Akt3, was
involved in
GRP78 stability regulation
Gray et al., Int J Cancer 2013
(Endometrial Neoplasms) :
SiRNA studies also revealed that knockdown of GRP78 reduces but does not abrogate AKT activity, demonstrating that
GRP78 is
required for optimal
AKT activity