ITPR1

(redirected from IP3R1)

ITPR1

A gene on chromosome 3p26.1 that encodes an intracellular receptor for a so-called second messenger (inositol 1,4,5-trisphosphate (IP3)) which, once stimulated by IP3, mediates calcium release from the endoplasmic reticulum. The three IP3 receptor subtypes—IP3R1, IP3R2 and IP3R3—are present in the wild as homo- and heterotetramers, are associated with calmodulin and FK506-binding protein, and are modulated through phosphorylation by PKA, PKC, PKG and CaMKII.

Molecular pathology
IPTR1 mutations cause spinocerebellar ataxia type 15.
References in periodicals archive ?
Cav1.2 and Cav1.3 were distributed on cellular membrane and cytoplasm as IP[sub]3R1, IP[sub]3R2, IP[sub]3R3, and RyR2 in both groups, but positive staining of Cav1.2, IP3R1, IP3R2, and RyR2 were not uniform in achalasia.
For example, antago-miR mediated inactivation of miR-25, which is selectively upregulated in cardiomyocytes from TAC-overloaded hearts and targets mRNAs such as sarcoplasmic reticulum calcium ATPase 2a (SERCA2a) and inositol-3'-phosphate receptor-1 (IP3R1), improves calcium reuptake and myocardial contractility during HF [175].
After transfer, membranes were immunoblotted with the following primary antibodies: PMCA1, PMCA 4, and PMCA total (Affinity Bioreagents, Rockford, IL), SERCA 2 (Thermo Scientific, Pierce antibodies, Rockford, IL, USA), NCX1 (Swant, Bellinzona, Switzerland), STIM1 (Cell Signaling, Beverly, USA), Orai1 (Proteintech, USA), and IP3R1 (Millipore, USA).
(2011) Genetic ablation and chemical inhibition of IP3R1 reduce mutant huntingtin aggregation.
Liu, "TNF[alpha]-induced IP3R1 expression through TNFR1/PC-PLC/ PKC[alpha] and TNFR2 signalling pathways in human mesangial cell," Nephrology Dialysis Transplantation, vol.
Phosphorylation of IP3R1 and the regulation of [Ca.sup.2+]i response at fertilization: a role for the MAP kinase pathway.
Mikoshiba and colleagues demonstrated that a neuronal protein called inositol 1,4,5-trisphosphate receptor 1 (IP3R1) which regulates cellular calcium signaling was destroyed by ER stress and subsequently induced neuronal cell death and brain damage.