APY29 is considered as a type I kinase inhibitor of inositol requiring kinase enzyme 1 α (IRE1α).[1]
Biochem/physiol Actions
APY29 has the ability to enhance inositol requiring kinase enzyme 1 α (IRE1α) (P830L)′s oligomeric state to rescue RNase activity.[1]
APY29 is a small molecule that inhibits the kinase activity of IRE1α (in vitro autophosphorylation IC50 = 280 nM) by targeting its active site ATP-binding pocket, while simultaneously acting as an allosteric activator of IRE1α RNase activity (EC50 = 460 nM) by keeping the active site in an open conformation. When applied 1 hr prior to stress induction by 4-hr 6 nM thapsigargin treatment, APY29 significantly potentiates stress-induced unfolded protein response (UPR) in rat insulinoma INS-1 cultures (XBP1 mRNA processing induction = 54% without vs. 78% with 1-hr 3 μM APY29 pretreatment).
ATP-competitive IRE1α kinase activity inhibitor and allosteric IRE1α RNase activity activator that enhances stress-induced unfolded protein response (UPR).
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1. The endoribonuclease (RNase) domain of Ire1 initiates a non-conventional mRNA splicing reaction, leading
Depending on endoplasmic reticulum (ER) stress levels, the ER transmembrane multidomain protein IRE1α promotes either adaptation or apoptosis. Unfolded ER proteins cause IRE1α lumenal domain homo-oligomerization, inducing trans autophosphorylation that further drives homo-oligomerization of its cytosolic kinase/endoribonuclease (RNase) domains to
In response to the endoplasmic reticulum (ER) stress induced by herpes simplex virus type 1 (HSV-1) infection, host cells activate the unfolded protein response (UPR) to reduce the protein-folding burden in the ER. The regulation of UPR upon HSV-1 infection
Diets rich in saturated fatty acids (SFAs) produce a form of tissue inflammation driven by "metabolically activated" macrophages. We show that SFAs, when in excess, induce a unique transcriptional signature in both mouse and human macrophages that is enriched by
Nature chemical biology, 8(12), 982-989 (2012-10-23)
Under endoplasmic reticulum stress, unfolded protein accumulation leads to activation of the endoplasmic reticulum transmembrane kinase/endoRNase (RNase) IRE1α. IRE1α oligomerizes, autophosphorylates and initiates splicing of XBP1 mRNA, thus triggering the unfolded protein response (UPR). Here we show that IRE1α's kinase-controlled
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