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PubMed:19233847 JSONTXT 25 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-179 Sentence denotes The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins.
T2 180-304 Sentence denotes Cells are equipped with an efficient quality control system to selectively eliminate abnormally folded and damaged proteins.
T3 305-485 Sentence denotes Initially the cell tries to refold the unfolded proteins with the help of molecular chaperones, and failure to refold leads to their degradation by the ubiquitin proteasome system.
T4 486-584 Sentence denotes But how this proteolytic machinery recognizes the abnormally folded proteins is poorly understood.
T5 585-813 Sentence denotes Here, we report that E6-AP, a HECT domain family ubiquitin ligase implicated in Angelman syndrome, interacts with the substrate binding domain of Hsp70/Hsc70 chaperones and promotes the degradation of chaperone bound substrates.
T6 814-997 Sentence denotes The expression of E6-AP was dramatically induced under a variety of stresses, and overexpression of E6-AP was found to protect against endoplasmic reticulum stress-induced cell death.
T7 998-1234 Sentence denotes The inhibition of proteasome function not only increases the expression of E6-AP but also causes its redistribution around microtubule-organizing center, a subcellular structure for the degradation of the cytoplasmic misfolded proteins.
T8 1235-1375 Sentence denotes E6-AP is also recruited to aggresomes containing the cystic fibrosis transmembrane conductance regulator or expanded polyglutamine proteins.
T9 1376-1469 Sentence denotes Finally, we demonstrate that E6-AP ubiquitinates misfolded luciferase that is bound by Hsp70.
T10 1470-1727 Sentence denotes Our results suggest that E6-AP functions as a cellular quality control ubiquitin ligase and, therefore, can be implicated not only in the pathogenesis of Angelman syndrome but also in the biology of neurodegenerative disorders involving protein aggregation.