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Target Concepts:
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Query: UMLS:C0162871 (
abdominal aortic aneurysm
)
8,664
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Cell viability during chronological aging and after apoptotic stimuli in some yeast mutants with altered mitochondrial morphology was followed; a function for the corresponding genes in the apoptotic process was assessed. MDM30 and DNM1, the genes encoding an
F-box protein
and the dynamin-related GTPase, respectively, are involved in triggering aging and apoptosis. In contrast, YME1, encoding a subunit of the mitochondrial inner membrane i-
AAA
proteinase complex, has a protective role in these processes. FIS1, the mitochondrial fission gene, might play a protective role after an apoptotic insult while it seems to promote cell death in aging cells.
...
PMID:Apoptosis and aging in mitochondrial morphology mutants of S. cerevisiae. 1829 44
Organisms can adapt to a broad spectrum of sudden and dramatic changes in their environment. These abrupt changes are often perceived as stress and trigger responses that facilitate survival and eventual adaptation. The ubiquitin-proteasome system (UPS) is involved in most cellular processes. Unsurprisingly, components of the UPS also play crucial roles during various stress response programs. The budding yeast SCF
Met30
complex is an essential cullin-RING ubiquitin ligase that connects metabolic and heavy metal stress to cell cycle regulation. Cadmium exposure results in the active dissociation of the
F-box protein
Met30 from the core ligase, leading to SCF
Met30
inactivation. Consequently, SCF
Met30
substrate ubiquitylation is blocked and triggers a downstream cascade to activate a specific transcriptional stress response program. Signal-induced dissociation is initiated by autoubiquitylation of Met30 and serves as a recruitment signal for the
AAA
-ATPase Cdc48/p97, which actively disassembles the complex. Here we show that the UBX cofactor Shp1/p47 is an additional key element for SCF
Met30
disassembly during heavy metal stress. Although the cofactor can directly interact with the ATPase, Cdc48 and Shp1 are recruited independently to SCF
Met30
during cadmium stress. An intact UBX domain is crucial for effective SCF
Met30
disassembly, and a concentration threshold of Shp1 recruited to SCF
Met30
needs to be exceeded to initiate Met30 dissociation. The latter is likely related to Shp1-mediated control of Cdc48 ATPase activity. This study identifies Shp1 as the crucial Cdc48 cofactor for signal-induced selective disassembly of a multisubunit protein complex to modulate activity.
...
PMID:Cdc48 cofactor Shp1 regulates signal-induced SCF
Met30
disassembly. 3281 89