Abstract
Some nuclear proteins that are crucial in interphase relocate during the G2/M-phase transition in order to perform their mitotic functions. However, how they perform these functions and the underlying mechanisms remain largely unknown. Here, we report that a fraction of the nuclear periphery proteins lamin-A/C, LAP2α and BAF1 (also known as BANF1) relocate to the spindle and the cell cortex in mitosis. Knockdown of these proteins by using RNA interference (RNAi) induces short and fluffy spindle formation, and disconnection of the spindle from the cell cortex. Disrupting the microtubule assembly leads to accumulation of these proteins in the cell cortex, whereas depolymerizing the actin microfilaments results in the formation of short spindles. We further demonstrate that these proteins are part of a stable complex that links the mitotic spindle to the cell cortex and the spindle matrix by binding to spindle-associated dynein, the actin filaments in the cell cortex and the spindle matrix. Taken together, our findings unveil a unique mechanism where the nuclear periphery proteins lamin-A/C, LAP2α and BAF1 are assembled into a protein complex during mitosis in order to regulate assembly and positioning of the mitotic spindle.