Publications by authors named "James E Mullally"
Article Synopsis
- * Its activity is triggered by chemical stress and DNA binding, and Wss1 is essential for surviving UV radiation and certain DNA damage-inducing drugs.
- * Wss1 operates within a complex with Cdc48 and Doa1 to extend SUMO chains on target proteins, and its workings may link DNA damage response to autophagy.
Ubiquitin binding proteins regulate the stability, function, and/or localization of ubiquitinated proteins. Here we report the crystal structures of the zinc-finger ubiquitin binding domain (ZnF UBP) from the deubiquitinating enzyme isopeptidase T (IsoT, or USP5) alone and in complex with ubiquitin. Unlike other ubiquitin binding domains, this domain contains a deep binding pocket where the C-terminal diglycine motif of ubiquitin is inserted, thus explaining the specificity of IsoT for an unmodified C terminus on the proximal subunit of polyubiquitin.
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- * This study reveals that Doa1 directly interacts with Cdc48 through a newly identified ubiquitin binding domain called PFU, and both Doa1’s PUL and PFU domains help form a complex that brings ubiquitinated proteins to Cdc48.
- * The findings suggest that Doa1 and Cdc48 mutations affect each other (epistatic), indicating their interaction is crucial for cellular function; furthermore, evidence shows a conserved role of PLAA in humans, highlighting similarities between
Article Synopsis
- LKB1 is a serine/threonine kinase tumor suppressor that plays a crucial role in regulating cellular processes like growth and metabolism.
- Reactive lipids, particularly cyclopentenone prostaglandins, modify LKB1, specifically targeting the Cys210 residue, which influences its activity and the downstream AMP kinase pathway.
- The study highlights how certain reactive lipids linked to inflammation can inhibit LKB1, potentially leading to increased risks for diseases like cancer by disrupting its normal function against growth signals.
Article Synopsis
- The Symposium on Ubiquitin and Signaling focused on the role of ubiquitin in cellular signaling processes, highlighting its importance in protein degradation and regulation.
- Experts presented recent research findings that illustrate how ubiquitin modification affects various physiological functions and disease mechanisms.
- The event fostered discussions on potential therapeutic applications of targeting ubiquitin pathways in diseases such as cancer and neurodegeneration.
Article Synopsis
- * In animal studies, curcumin has shown protective effects against cancer caused by chemical exposure, highlighting its potential in cancer prevention strategies.
- * It alters the structure of the p53 protein, which is crucial for tumor suppression, affecting its ability to function properly in regulating cell growth and responding to DNA damage.
Article Synopsis
- * The effectiveness of these prostaglandins is linked to their chemical structures, where features like olefin-ketone conjugation and nucleophilic reactivity play critical roles in their cytotoxic effects.
- * Recent studies on punaglandins isolated from the soft coral Telesto riisei reveal that they inhibit isopeptidase activity and exhibit greater antiproliferative effects than other previously studied prostaglandins, suggesting they could be a