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, Ca+2 and Sr+2 ions (PDB entry [[3lj0]])' scene='51/516469/Cv/1'>
<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''' or '''serine/threonine protein kinase/endoribonuclease Ire1'''.  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.  


== Structural highlights ==
== Structural highlights ==

Revision as of 13:38, 25 August 2020

<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'>

FunctionFunction

Ire1 or serine/threonine protein kinase/endoribonuclease Ire1. 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 highlightsStructural highlights

Yeast Ire1 structure contains 3 phosphorylated residues: . Ire1 shows a different and for quercetin. Quercetin is a powerful activator of Ire1. [2].

3D structures of Ire13D structures of Ire1

2hz6 – hIre1 N terminal (mutant) – human
4z7g, 5hgi – hIre1 cytoplasmic domain
3p23, 4yzd - hIre1 cytoplasmic domain + ADP
4u6r, 4yz9, 4z7h – hIre1 cytoplasmic domain + inhibitor
4yzc – hIre1 cytoplasmic domain + satuorosporine
4pl3, 4pl4, 4pl5 – mIre1 cytoplasmic domain (mutant) + inhibitor – mouse
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


ReferencesReferences

  1. 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
  2. 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:http://dx.doi.org/10.1016/j.tcb.2013.06.005

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky