Recent Advances in Mechanisms of Mitotic and Meiotic Chromosome Segregation and Error Correction

A special issue of Cells (ISSN 2073-4409). This special issue belongs to the section "Cell Proliferation and Division".

Deadline for manuscript submissions: closed (31 October 2023) | Viewed by 2548

Special Issue Editors


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Guest Editor
Deptartment of Biochemistry and Molecular Medicine, School of Medicine and Health Sciences, George Washington University, Washington, DC, USA
Interests: aging; cancer; cell cycle; cell death; cell senescence; cell signaling; oncogenes; tumor suppressors

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Guest Editor
Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA, USA
Interests: mitosis; chromosomes; centromeres; kinetochores; spindle assembly

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Guest Editor
Department of Biology, University of Pennsylvania, Philadelphia, PA, USA
Interests: cell

Special Issue Information

Dear Colleagues,

Chromosome segregation ensures the equal inheritance of genetic material among progeny across generations. Accurate segregation is essential to maintaining genomic integrity and preventing catastrophic outcomes. Over the years, we have broadened our understanding of the myriad pathways that control this central process required to maintain life in perpetuity, but some aspects remain unaddressed.

In this Special Issue, first, we hope to reflect on recent advances in understanding the functional basis for error correction in mitosis. Error correction mechanisms, including those controlling anaphase chromosome movement, have been studied for years, but we especially want to focus on recent studies that revisit models for how chromosomes are segregated accurately to each pole. Second, we would like to cover recent studies on the highly error-prone oocyte chromosome segregation process, including acentrosomal spindle assembly, maternal aging, early embryonic aneuploidy, meiotic checkpoints, and female meiotic drive or biased segregation.  

We envision that this Special Issue will provide a holistic view of the existing models and upcoming new models for error-free segregation mechanisms in both mitosis and meiosis, ultimately reflecting on the progress of this field and considering future directions. We welcome mini-reviews, review articles, and original research articles focused on this topic across a diverse array of model systems.

We look forward to your contributions to this Special Issue of Cells.

Dr. Goberdhan P. Dimri
Dr. Nootan Pandey
Dr. Arunika Das
Guest Editors

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Keywords

  • mitosis
  • meiosis
  • segregation
  • error correction
  • centromeres
  • kinetochores

Published Papers (2 papers)

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Research

18 pages, 8392 KiB  
Article
Independent and Complementary Functions of Caf1b and Hir1 for Chromatin Assembly in Tetrahymena thermophila
by Huijuan Hao, Chenhui Ren, Yinjie Lian, Min Zhao, Tao Bo, Jing Xu and Wei Wang
Cells 2023, 12(24), 2828; https://doi.org/10.3390/cells12242828 - 13 Dec 2023
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Abstract
Histones and DNA associate to form the nucleosomes of eukaryotic chromatin. Chromatin assembly factor 1 (CAF-1) complex and histone regulatory protein A (HIRA) complex mediate replication-couple (RC) and replication-independent (RI) nucleosome assembly, respectively. CHAF1B and HIRA share a similar domain but play different [...] Read more.
Histones and DNA associate to form the nucleosomes of eukaryotic chromatin. Chromatin assembly factor 1 (CAF-1) complex and histone regulatory protein A (HIRA) complex mediate replication-couple (RC) and replication-independent (RI) nucleosome assembly, respectively. CHAF1B and HIRA share a similar domain but play different roles in nucleosome assembly by binding to the different interactors. At present, there is limited understanding for the similarities and differences in their respective functions. Tetrahymena thermophila contains transcriptionally active polyploid macronuclei (MAC) and transcriptionally silent diploid micronuclei (MIC). Here, the distribution patterns of Caf1b and Hir1 exhibited both similarities and distinctions. Both proteins localized to the MAC and MIC during growth, and to the MIC during conjugation. However, Hir1 exhibited additional signaling on parental MAC and new MAC during sexual reproduction and displayed a punctate signal on developing anlagen. Caf1b and Hir1 only co-localized in the MIC with Pcna1 during conjugation. Knockdown of CAF1B impeded cellular growth and arrested sexual reproductive development. Loss of HIR1 led to MIC chromosome defects and aborted sexual development. Co-interference of CAF1B and HIR1 led to a more severe phenotype. Moreover, CAF1B knockdown led to the up-regulation of HIR1 expression, while knockdown of HIR1 also led to an increase in CAF1B expression. Furthermore, Caf1b and Hir1 interacted with different interactors. These results showed that CAF-1 and Hir1 have independent and complementary functions for chromatin assembly in T. thermophila. Full article
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21 pages, 9323 KiB  
Article
Distinct Mitotic Functions of Nucleolar and Spindle-Associated Protein 1 (NuSAP1) Are Controlled by Two Consensus SUMOylation Sites
by Michela Damizia, Ludovica Altieri, Vincenzo Costanzo and Patrizia Lavia
Cells 2023, 12(21), 2545; https://doi.org/10.3390/cells12212545 - 30 Oct 2023
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Abstract
Nucleolar and Spindle-Associated Protein 1 (NuSAP1) is an important mitotic regulator, implicated in control of mitotic microtubule stability and chromosome segregation. NuSAP1 regulates these processes by interacting with several protein partners. Its abundance, activity and interactions are therefore tightly regulated during mitosis. Protein [...] Read more.
Nucleolar and Spindle-Associated Protein 1 (NuSAP1) is an important mitotic regulator, implicated in control of mitotic microtubule stability and chromosome segregation. NuSAP1 regulates these processes by interacting with several protein partners. Its abundance, activity and interactions are therefore tightly regulated during mitosis. Protein conjugation with SUMO (Small Ubiquitin-like MOdifier peptide) is a reversible post-translational modification that modulates rapid changes in the structure, interaction(s) and localization of proteins. NuSAP1 was previously found to interact with RANBP2, a nucleoporin with SUMO ligase and SUMO-stabilizing activity, but how this interaction affects NuSAP1 activity has remained elusive. Here, we show that NuSAP1 interacts with RANBP2 and forms proximity ligation products with SUMO2/3 peptides in a RANBP2-dependent manner at key mitotic sites. A bioinformatic search identified two putative SUMO consensus sites in NuSAP1, within the DNA-binding and the microtubule-binding domains, respectively. Site-specific mutagenesis, and mitotic phenotyping in cell lines expressing each NuSAP1 mutant version, revealed selective roles of each individual site in control of NuSAP1 localization and in generation of specific mitotic defects and distinct fates in daughter cells. These results identify therefore two new regulatory sites for NuSAP1 functions and implicate RANBP2 in control of NuSAP1 activity. Full article
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