Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Bypass of Activation Loop Phosphorylation by Aspartate 836 in Activation of the Endoribonuclease Activity of Ire1.

Molecular and cellular biology - 15 Aug 2017

Armstrong Michael C, Šestak Sergej, Ali Ahmed A, Sagini Hanan A M, Brown Max, Baty Karen, Treumann Achim, Schröder Martin

Abstract excerpt

The bifunctional protein kinase-endoribonuclease Ire1 initiates splicing of the mRNA for the transcription factor Hac1 when unfolded proteins accumulate in the endoplasmic reticulum. Activation of Saccharomyces cerevisiae Ire1 coincides with autophosphorylation of its activation loop at S840, S841, T844, and S850. Mass spectrometric analysis of Ire1 expressed in Escherichia coli identified S837 as another...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Aspartic Acid
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Endoplasmic Reticulum Stress

Share to Epistasis, Genetic

Share to Genes, Reporter

Share to Mutant Proteins

Share to Protein Phosphatase 2

Share to RNA Splicing

Source

Open in PubMed Open full text

Identifiers

PMID: 28559428
DOI: 10.1128/MCB.00655-16
PMCID: PMC5533888

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Bypass of Activation Loop Phosphorylation by Aspartate 836 in Activation of the Endoribonuclease Activity of Ire1.PMID 28559428Read ↗

IRE1- and HAC1-independent transcriptional regulation in the unfolded protein response of yeast.Semantic proximity Read ↗

The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein ResponseSemantic proximity Read ↗

Self-association and BiP dissociation are not sufficient for activation of the ER stress sensor Ire1.Semantic proximity Read ↗

Mechanism of non-spliceosomal mRNA splicing in the unfolded protein response pathway.Semantic proximity Read ↗

IRE1 and efferent signaling from the endoplasmic reticulumSemantic proximity Read ↗

Phosphorylation at Ser724 of the ER stress sensor IRE1α governs its activation state and limits ER stress-induced hepatosteatosis.Semantic proximity Read ↗

Adaptation to ER Stress by Slt2, Counterpart of Human MAP Kinase ERK1/2, via Enhancing Splicing and Translation of <i>HAC1</i> mRNA in <i>Saccharomyces cerevisiae</i>Semantic proximity Read ↗

Optogenetic Clustering of Human IRE1 Reveals Differential Regulation of Transcription and mRNA Splice Isoform Abundance by the UPRSemantic proximity Read ↗

IRE1α Kinase Activation Modes Control Alternate Endoribonuclease Outputs to Determine Divergent Cell FatesSemantic proximity Read ↗

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells.Semantic proximity Read ↗

Asc1p/RACK1 Connects Ribosomes to Eukaryotic Phosphosignaling.Semantic proximity Read ↗

A conserved structural determinant located at the interdomain region of mammalian inositol-requiring enzyme 1alpha.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.