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PreprintCited by 2Microtubule and mitosis dynamicsNuclear Structure and FunctionGenomics and Chromatin Dynamics

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Phase transition of spindle pole localized protein orchestrates nuclear organization at mitotic exit

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Rajeevan, Ashwathi, Olakkal, Vignesh, Balakrishnan, Madhumitha, Chakrabarty, Dwaipayan, Charon, François, Noordermeer, Daan, Kotak, Sachin·2025·The EMBO Journal
DOI 10.1101/2025.01.22.634232

Preprint — published as 10.1038/s44318-025-00564-4

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Abstract

Animal cells dismantle their nuclear envelope (NE) at the beginning and reconstruct it at the end of mitosis. This process is closely coordinated with spindle pole organization: poles enlarge at mitotic onset and reduce size as mitosis concludes. The significance of this coordination remains unknown. Here, we demonstrate that Aurora A maintains a pole-localized protein NuMA in a dynamic state during anaphase. Without Aurora A, NuMA shifts from a dynamic to a solid phase, abnormally accumulating at the poles, leading to chromosome bending and misshaped nuclei formation around poles. NuMA localization relies on interactions with dynein/dynactin, its coiled-coil domain, and intrinsically disordered region (IDR). Mutagenesis experiments revealed that cation-π interactions within IDR are key for NuMA localization, while glutamine residues trigger its solid-state transition upon Aurora A inhibition. This study emphasizes the role of the physical properties of spindle poles in organizing the nucleus and genome post-mitosis.

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Metadata

Authors
Rajeevan, A., Olakkal, V., Balakrishnan, M., Chakrabarty, D., Charon, F., Noordermeer, D., & Kotak, S.
Affiliations
  • Indian Institute of Science Bangalore (IN)
  • Centre National de la Recherche Scientifique (FR)
Corresponding author
  • Rajeevan, Ashwathi
  • Olakkal, Vignesh
  • Balakrishnan, Madhumitha
  • Chakrabarty, Dwaipayan
ORCID
Venue
The EMBO Journal
Publisher
openRxiv
Published
2025-01-23
Volume
44
Issue
23
Pages
6797-6831
ISSN
0261-4189 (ISSN-L)
DOI
10.1101/2025.01.22.634232
OpenAlex
W4414156011
Cited by
2
References
1
Citations by year
2026: 2
FWCI
0.99
Type
journal article
Language
en
Open access
Licence
Locations
  • The EMBO Journal (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • HAL (submittedVersion, cc-by-nc-nd)
  • HAL (submittedVersion, other-oa)
Funders
  • Department of Biotechnology, Ministry of Science and Technology, India (BT/PR36084/BRB/10/1857/2020)
  • Department of Science and Technology, Ministry of Science and Technology, India (CRG/2022/005151)
  • Agence Nationale de la Recherche (ANR-10-INBS-0009)
  • Indo-French Centre for the Promotion of Advanced Research (7103-4)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Keywords
AURKA, spindle poles, NUMA, nuclear envelope disassembly, nuclear envelope reassembly, mitotic exit, nuclear organization, dynein/dynactin, intrinsically disordered regions, cation-π interactions, solid-state phase transitions, chromosome segregation
MeSH terms
Dynactin Complex, Anaphase, Cell Nucleus, Dyneins, HeLa Cells, Humans, Mitosis, Spindle Apparatus, Cell Cycle Proteins, Nuclear Matrix-Associated Proteins, Antigens, Nuclear, Spindle Poles, Aurora Kinase A

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