منابع مشابه
Die later with ESCRT!
The consequences of necroptosis depend on immunomodulatory molecules, the expression of which requires time before the burst of a cell. Gong et al. now provide evidence for ESCRT-III-mediated plasma membrane repair to extend the time to death during necroptosis. Regulated cell death is not restricted to apoptosis, but includes several forms of regulated necrosis. The best characterized signalin...
متن کاملMutate now, die later. Evolutionary dynamics with delayed selection.
We analyze here the evolutionary consequences of selection with delay in a population genetics context. In the classical works on evolutionary dynamics, an individual produces off-springs in direct proportion to its fitness, a process in which mutations may occur. In the present scenario of delayed selection, individuals that acquire deleterious mutations can still reproduce unharmed for severa...
متن کاملThe Great Diadema antillarum Die-Off: 30 Years Later.
In 1983-1984, the sea urchin Diadema antillarum suffered mass mortality throughout the Caribbean, Florida, and Bermuda. The demise of this herbivore contributed to a phase shift of Caribbean reefs from coral-dominated to alga-dominated communities. A compilation of published data of D. antillarum population densities shows that there has been moderate recovery since 1983, with the highest rates...
متن کاملComparative analysis of ESCRT-I, ESCRT-II and ESCRT-III function in Drosophila by efficient isolation of ESCRT mutants.
ESCRT proteins were initially isolated in yeast as a single functional set of conserved components controlling endosomal cargo sorting and multivesicular body (MVB) biogenesis. Recent work has suggested that metazoan ESCRT proteins might have more functionally diverse roles, but the limited availability of ESCRT mutants in species other than yeast has hampered a thorough analysis. Here, we used...
متن کاملNovel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly.
The AAA+ ATPase VPS4 plays an essential role in multivesicular body biogenesis and is thought to act by disassembling ESCRT-III complexes. VPS4 oligomerization and ATPase activity are promoted by binding to LIP5. LIP5 also binds to the ESCRT-III like protein CHMP5/hVps60, but how this affects its function remains unclear. Here we confirm that LIP5 binds tightly to CHMP5, but also find that it b...
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ژورنال
عنوان ژورنال: Oncotarget
سال: 2017
ISSN: 1949-2553
DOI: 10.18632/oncotarget.17903