Ire1: Difference between revisions
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<StructureSection load='3lj0' size='400' side='right' caption='Structure of yeast Ire1 cytoplasmic domain dimer complex with quercetin, ADP | <StructureSection load='3lj0' size='400' side='right' caption='Structure of yeast Ire1 cytoplasmic domain dimer complex with quercetin, ADP, Ca+2 and Sr+2 ions (PDB entry [[3lj0]])' scene='51/516469/Cv/1'> | ||
== Function == | == Function == | ||
'''Ire1''' is a serine/threonine protein kinase/endoribonuclease. It is important in altering gene expression as a response to endoplasmic reticulum-based stress signals<ref>PMID:11034898</ref>. The endoribonuclase domain of Ire1 is a transcriptional activator which triggers growth arrest and apoptosis. The kinase domain of Ire1 is required for activation of the endoribonuclase domain. Ire1 senses unfolded proteins causing its auto-activation. | '''Ire1''' is a serine/threonine protein kinase/endoribonuclease. It is important in altering gene expression as a response to endoplasmic reticulum-based stress signals<ref>PMID:11034898</ref>. The endoribonuclase domain of Ire1 is a transcriptional activator which triggers growth arrest and apoptosis. The kinase domain of Ire1 is required for activation of the endoribonuclase domain. Ire1 senses unfolded proteins causing its auto-activation. | ||
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== Structural highlights == | == Structural highlights == | ||
Yeast Ire1 structure contains 3 phosphorylated residues: 2 Ser and a Thr. | Yeast Ire1 structure contains 3 phosphorylated residues: 2 Ser and a Thr. Ire1 shows a different binding site for ADP and for quercetin. Quercetin is a powerful activator of Ire1. Ire1 binds 2 molecules of quercetin at its dimer interface<ref>PMID:23880584</ref>. | ||
==3D structures of Ire1== | ==3D structures of Ire1== | ||
Revision as of 07:15, 10 April 2016
<StructureSection load='3lj0' size='400' side='right' caption='Structure of yeast Ire1 cytoplasmic domain dimer complex with quercetin, ADP, Ca+2 and Sr+2 ions (PDB entry 3lj0)' scene='51/516469/Cv/1'>
Function
Ire1 is a serine/threonine protein kinase/endoribonuclease. It is important in altering gene expression as a response to endoplasmic reticulum-based stress signals[1]. The endoribonuclase domain of Ire1 is a transcriptional activator which triggers growth arrest and apoptosis. The kinase domain of Ire1 is required for activation of the endoribonuclase domain. Ire1 senses unfolded proteins causing its auto-activation.
Structural highlights
Yeast Ire1 structure contains 3 phosphorylated residues: 2 Ser and a Thr. Ire1 shows a different binding site for ADP and for quercetin. Quercetin is a powerful activator of Ire1. Ire1 binds 2 molecules of quercetin at its dimer interface[2].
3D structures of Ire1
2hz6 – hIre1 N terminal (mutant) – human
2rio, 3fbv, 3sdm – yIre1 cytoplasmic domain – yeast
3sdj - yIre1 cytoplasmic domain (mutant)
2bei – yIre1 lumenal domain + peptide
3lj0 - yIre1 cytoplasmic domain + quercetin + ADP
3lj1, 3lj2 - yIre1 cytoplasmic domain + inhibitor
3p23 - hIre1 cytoplasmic domain + ADP
References
- ↑ Urano F, Bertolotti A, Ron D. IRE1 and efferent signaling from the endoplasmic reticulum. J Cell Sci. 2000 Nov;113 Pt 21:3697-702. PMID:11034898
- ↑ Chen Y, Brandizzi F. IRE1: ER stress sensor and cell fate executor. Trends Cell Biol. 2013 Nov;23(11):547-55. doi: 10.1016/j.tcb.2013.06.005. Epub, 2013 Jul 21. PMID:23880584 doi:https://dx.doi.org/10.1016/j.tcb.2013.06.005
