NuMA interaction with chromatin is vital for proper chromosome decondensation at the mitotic exit.

Abstract:

:NuMA is an abundant long coiled-coil protein that plays a prominent role in spindle organization during mitosis. In interphase, NuMA is localized to the nucleus and hypothesized to control gene expression and chromatin organization. However, because of the prominent mitotic phenotype upon NuMA loss, its precise function in the interphase nucleus remains elusive. Here, we report that NuMA is associated with chromatin in interphase and prophase but released upon nuclear envelope breakdown (NEBD) by the action of Cdk1. We uncover that NuMA directly interacts with DNA via evolutionarily conserved sequences in its C-terminus. Notably, the expression of the DNA-binding-deficient mutant of NuMA affects chromatin decondensation at the mitotic exit, and nuclear shape in interphase. We show that the nuclear shape defects observed upon mutant NuMA expression are due to its potential to polymerize into higher-order fibrillar structures. Overall, this work establishes the spindle-independent function of NuMA in choreographing proper chromatin decompaction and nuclear shape by directly associating with the DNA.

journal_name

Mol Biol Cell

authors

Rajeevan A,Keshri R,Kapoor S,Kotak S

doi

10.1091/mbc.E20-06-0415

subject

Has Abstract

pub_date

2020-10-15 00:00:00

pages

2437-2451

issue

22

eissn

1059-1524

issn

1939-4586

journal_volume

31

pub_type

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