Crystal structures reveal transient PERK luminal domain tetramerization in endoplasmic reticulum stress signaling

Stress caused by accumulation of misfolded proteins within the endoplasmic reticulum (ER) elicits a cellular unfolded protein response (UPR) aimed at maintaining protein‐folding capacity. PERK, a key upstream component, recognizes ER stress via its luminal sensor/transducer domain, but the molecular...

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Veröffentlicht in:	The EMBO journal 2015-06, Vol.34 (11), p.1589-1600
Hauptverfasser:	Carrara, Marta, Prischi, Filippo, Nowak, Piotr R, Ali, Maruf MU
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Biophysics cell signaling Cells, Cultured Crystal structure Crystallography, X-Ray eIF-2 Kinase - chemistry eIF-2 Kinase - genetics eIF-2 Kinase - metabolism EMBO32 EMBO40 Endoplasmic reticulum Endoplasmic Reticulum Stress - physiology ER stress Eukaryotic Initiation Factor-2 - genetics Eukaryotic Initiation Factor-2 - metabolism Humans Mice Mice, Knockout Molecular biology Mutation PERK Phosphorylation - physiology Protein folding Protein Multimerization - physiology Protein Structure, Quaternary Protein Structure, Tertiary Signal Transduction - physiology unfolded protein response Unfolded Protein Response - physiology
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