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Corrigan, A.

Publications and source records attributed to Corrigan, A..

2 recordsLinked to original sources

Nuclear fascin regulates cancer cell survival

Fascin is an important regulator of F-actin bundling leading to enhanced filopodia assembly. Fascin is also overexpressed in most solid tumours where it supports invasion through control of F-actin structures at the periphery and nuclear envelope. Recently fascin has been identified in the nucleus of a broad range of cell types but the contributions of nuclear fascin to cancer cell behaviour remain unknown. Here we demonstrate that fascin bundles F-actin within the nucleus to support chromatin organisation and efficient DNA damage response. Fascin associates directly with phosphorylated Histone H3 leading to regulated levels of nuclear fascin to support these phenotypes. Forcing nuclear fascin accumulation through the expression of nuclear-targeted fascin-specific nanobodies or inhibition of Histone H3 kinases results in enhanced and sustained nuclear F-actin bundling leading to reduced invasion, viability and nuclear fascin-specific/driven apoptosis. These findings represent an additional important route through which fascin can support tumorigenesis and provide insight into potential pathways for targeted fascin-dependent cancer cell killing.

cancer biology↗

Two-Step Interphase Microtubule Disassembly Aids Spindle Morphogenesis

Entry into mitosis triggers profound changes in cell shape and cytoskeletal organisation. Here, by studying microtubule remodelling in human flat mitotic cells, we identify a two-step process of interphase microtubule disassembly. First, a microtubule stabilizing protein, Ensconsin, is inactivated in prophase as a consequence of its phosphorylation downstream of Cdk1/CyclinB. This leads to a reduction in interphase microtubule stability that may help to fuel the growth of centrosomally-nucleated microtubules. The peripheral interphase microtubules that remain are then rapidly lost as the concentration of tubulin heterodimers falls following dissolution of the nuclear compartment boundary. Finally, we show that a failure to destabilize microtubules in prophase leads to the formation of microtubule clumps, which interfere with spindle assembly. Overall, this analysis highlights the importance of the stepwise remodelling of the microtubule cytoskeleton, and the significance of permeabilization of the nuclear envelope in coordinating the changes in cellular organisation and biochemistry that accompany mitotic entry.

cell biology↗