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1. aII-Spectrin Identified as Essential Spring Component of NucleoskeletonMohammad F. Islam, Carnegie-Mellon University, DMR 0619424 We observed the presence of a nuclear envelope (NE)-localized and NE-enhanced aII-spectrin and actin in mammalian cells. Previously, co-immunoprecipitation studied have suggested that both aII-spectrin and actin should be enhanced at the NE due to binding partners, but it was not shown directly. Using high resolution confocal imaging, we were able to show endogenous protein colocalization of aII-spectrin (a and b) and actin (c) with NE-localized lamin B in HeLa cells at the NE using antibody labeling. This data suggests the potential relevance of new structural proteins, beyond lamin filaments, in the nucleus. Scale bar = 5 mm.

2. aII-Spectrin Identified as Essential Spring Component of NucleoskeletonMohammad F. Islam, Carnegie-Mellon University, DMR 0619424 Cells crawl through tissues and other interstitial spaces, and after deformation they must regain their original shape. We have determined that this nuclear “memory” comes from a set of spring-like proteins known as spectrins, which localize via actin proteins at the nuclear envelope with other structural proteins. The change in expression and localization of these spectrins has significant functional impact in certain muscular dystropies and other lamin-related diseases. force