Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Pancreatic eukaryotic initiation factor-2alpha kinase (PEK) homologues in humans, Drosophila melanogaster and Caenorhabditis elegans that mediate translational control in response to endoplasmic reticulum stress.
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Identified and characterized C. elegans PEK; demonstrated eIF2alpha kinase activity in yeast expression system; showed PEK inhibits translation through eIF2alpha hyperphosphorylation and eIF2B inhibition.
"To address the role of C. elegans PEK in translational control, we expressed this kinase in yeast and found that it inhibits growth by hyperphosphorylation of eIF-2alpha and inhibition of eIF-2B."
Complementary signaling pathways regulate the unfolded protein response and are required for C. elegans development.
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Established that pek-1 mediates translation attenuation arm of UPR; showed pek-1 acts in complementary pathways with ire-1/xbp-1 for development and survival; demonstrated synthetic lethality of double UPR mutants.
"In addition, ire-1/xbp-1 acts with pek-1, a protein kinase that mediates translation attenuation, in complementary pathways that are essential for worm development and survival."
Physiological IRE-1-XBP-1 and PEK-1 signaling in Caenorhabditis elegans larval development and immunity.
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Demonstrated increased PEK-1-dependent eIF2alpha phosphorylation in xbp-1 mutants; defined temperature-dependent requirements for XBP-1 and PEK-1; showed both pathways maintain ER homeostasis under physiological conditions including immune activation.
"XBP-1 deficiency increases PEK-1 dependent phosphorylation of eIF2α."
Protective coupling of mitochondrial function and protein synthesis via the eIF2α kinase GCN-2.
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Demonstrated GCN-2 and PEK-1 have overlapping roles in eIF2alpha phosphorylation; showed gcn-2;pek-1 double mutants in context of mitochondrial stress studies.
"GCN-2, an eIF2α kinase that modulates cytosolic protein synthesis, functions in a complementary pathway to that of HAF-1 and ATFS-1."
A novel interaction between aging and ER overload in a protein conformational dementia.
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Used C. elegans FENIB model to show UPR pathways including PEK-1 modulate aggregation of misfolded proteins; downregulation of UPR pathways favors mutant protein accumulation.
"Specifically, downregulation of the unfolded protein response (UPR) pathways in the worm favors mutant SRP-2 accumulation"
Deep research report on pek-1