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Why is Lamin B Receptor Downregulated in Senescence?
Author(s): Emilie Lukášová, Aleš Kovařík and Stanislav KozubekEmilie Lukášová, Aleš Kovařík and Stanislav Kozubek
An important mechanism ensuring spatial organization of chromatin structure and genome function in eukaryotic nuclei consists in anchoring of specific heterochromatin regions to nuclear envelope by proteins of inner nuclear membrane (INM) that are able to recognize these regions and simultaneously bind either Lamin A/C or lamin B1. One of these proteins is lamin B receptor (LBR) that binds lamin B1 and tethers heterochromatin to INM in embryonic and undifferentiated cells. It is replaced by lamin A/C with specific lamin A/C binding proteins (especially LEM-domain proteins) at the beginning of cell differentiation. Our functional experiments in cancer cell lines show that heterochromatin in cancer cells is tethered to INM by LBR that is downregulated together with lamin B1 at the onset of cell transition to senescence. A coordinated regulation of these proteins is evidenced also by dow.. View More»