> top > projects > sentences > docs > PubMed:17848550 > annotations

PubMed:17848550 JSONTXT 22 Projects

Annnotations TAB TSV DIC JSON TextAE Lectin_function IAV-Glycan

Id Subject Object Predicate Lexical cue
T1 0-90 Sentence denotes The yeast Hex3.Slx8 heterodimer is a ubiquitin ligase stimulated by substrate sumoylation.
T2 91-227 Sentence denotes Hex3 and Slx8 are Saccharomyces cerevisiae proteins with important functions in DNA damage control and maintenance of genomic stability.
T3 228-279 Sentence denotes Both proteins have RING domains at their C termini.
T4 280-428 Sentence denotes Such domains are common in ubiquitin and ubiquitin-like protein ligases (E3s), but little was known about the molecular functions of either protein.
T5 429-633 Sentence denotes In this study we identified HEX3 as a high-copy suppressor of a temperature-sensitive small ubiquitin-related modifier (SUMO) protease mutant, ulp1ts, suggesting that it may affect cellular SUMO dynamics.
T6 634-702 Sentence denotes Remarkably, even a complete deletion of ULP1 is strongly suppressed.
T7 703-738 Sentence denotes Hex3 forms a heterodimer with Slx8.
T8 739-836 Sentence denotes We found that the Hex3.Slx8 complex has a robust substrate-specific E3 ubiquitin ligase activity.
T9 837-946 Sentence denotes In this E3 complex, Slx8 appears to bear the core ligase function, with Hex3 strongly enhancing its activity.
T10 947-1110 Sentence denotes Notably, SUMO attachment to a substrate stimulates its Hex3.Slx8-dependent ubiquitination, primarily through direct noncovalent interactions between SUMO and Hex3.
T11 1111-1295 Sentence denotes Our data reveal a novel mechanism of substrate targeting in which sumoylation of a protein can help trigger its subsequent ubiquitination by recruiting a SUMO-binding ubiquitin ligase.