Related Experiment Video
Updated: Apr 6, 2026

Directly Measuring Forces Within Reconstituted Active Microtubule Bundles
Published on: May 10, 2022
An epigenetic regulator emerges as microtubule minus-end binding and stabilizing factor in mitosis
Sylvain Meunier1, Maria Shvedunova2, Nhuong Van Nguyen2
11] Cell and Developmental Biology Programme, Centre for Genomic Regulation (CRG), Dr Aiguader 88, 08003 Barcelona, Spain [2] Universitat Pompeu Fabra (UPF), Dr Aiguader 88, 08003 Barcelona, Spain.
Abstract:
The evolutionary conserved NSL complex is a prominent epigenetic regulator controlling expression of thousands of genes. Here we uncover a novel function of the NSL complex members in mitosis. As the cell enters mitosis, KANSL1 and KANSL3 undergo a marked relocalisation from the chromatin to the mitotic spindle. By stabilizing microtubule minus ends in a RanGTP-dependent manner, they are essential for spindle assembly and chromosome segregation. Moreover, we identify KANSL3 as a microtubule minus-end-binding protein, revealing a new class of mitosis-specific microtubule minus-end regulators. By adopting distinct functions in interphase and mitosis, KANSL proteins provide a link to coordinate the tasks of faithful expression and inheritance of the genome during different phases of the cell cycle.
More Related Videos
08:33Combining Mitotic Cell Synchronization and High Resolution Confocal Microscopy to Study the Role of Multifunctional Cell Cycle Proteins During Mitosis
Published on: December 5, 2017
12:26Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
Related Concept Videos
Microtubule Instability
Microtubule Instability
Anaphase A and B
Plus-end depolymerization releases tubulin heterodimers from the terminal region of the microtubule. As tubulin subunits are lost, the Ndc80 complexes detach...
Destabilization of Microtubules
Forces Acting on Chromosomes
Microtubules and motor proteins exert two types of forces on...
Microtubule Associated Proteins (MAPs)