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Caspase-mediated cleavage of the chromosome-binding domain of lamina-associated polypeptide 2α

Journal of Cell Science, 2000
ABSTRACT Lamina-associated polypeptide 2α (LAP2α) is a non-membrane-bound isoform of the LAP2 family involved in nuclear structure organization. Using various cell systems, including Jurkat, HL-60, and HeLa cells, and different death-inducing agents, such as anti-Fas antibody, topoisomerase inhibitors, and staurosporine, we found that ...
J, Gotzmann, S, Vlcek, R, Foisner
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Nonspecific steric hindrance of protein particles by lamina-associated domains

Genomic organization within the nucleus is crucial for gene regulation and cell health, as disruptions in this organization are linked to genetic disorders and cancers. Recent studies suggest that molecular-scale organization of chromatin near the nuclear periphery (lamina-associated domains, LADs) affects gene regulation, providing transciptional ...
Naz Bardakcı, Aykut Erbaş, Ozan S. Sarıyer +2 more
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Substructure and maturation of lamina-associated domains in neurons of the developing and adult human brain

Summary Approximately 30-40% of the human genome is anchored to the nuclear lamina (NL) through variably sized (10 kb-10 Mb) lamina-associated domains (LADs), which can be classified into two subtypes (T1 and T2) based on their level of lamina-association.
Chujing Zhang +8 more
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Interplay of epigenetic regulation and chromatin-lamina interaction modulates the morphology of lamina-associated domains