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Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina

ABSTRACT: To identify genes affected by the mutations in CAP-H2 and CRWN1/4.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE179466 | GEO | 2022/06/15

REPOSITORIES: GEO

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Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina [36 samples]

Project description:To identify genes affected by the mutations in CAP-H2 and CRWN1/4 under the DNA damaging condition

2022-06-15 | GSE179793 | GEO

Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina

Project description:Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina

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Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina [36 samples]

Project description:Two-step regulation of centromere distribution by condensin II with LINC complex and nuclear lamina [36 samples]

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CRWN nuclear lamina components maintain the H3K27me3 landscape and promote successful reproduction in Arabidopsis

Project description:The nuclear lamina, a crucial sub-nuclear protein matrix, maintains nuclear structure and genomic function. Our study centers on the Arabidopsis lamina component CROWDED NUCLEIs (CRWNs), unveiling their extensive role in the development of the reproductive system with a specific focus on the endosperm, which is pivotal in seed development. We showed that quadruple crwn null gametophytes exhibit limited viability, and crwn1 crwn2 (crwn1/2) mutations lead to defective seeds often having enlarged chalazal cysts and variable timing of endosperm cellularization. crwn1/2 endosperm also exhibit perturbations of level of tri-methylation of lysin 27 on histone H3 (H3K27me3) and transcriptomics. In addition, we found that PHERES1 (PHE1) targets and defense-related genes are mis-regulated in crwn1/2 endosperm, showing that both development and stress responses are affected by CRWNs simultaneously. The data also suggest that CRWNs affect various aspects of physiology of both vegetative and reproductive tissues but there are tissue-specific roles.

2024-05-02 | GSE243032 | GEO

RNA-seq in NT, CAP-D3, and CAP-H2 expressing cells treated with DMSO or menadione

Project description:The goal of this experiment was to identify transcripts that are differentially expressed in CAP-D3 and CAP-H2 depleted cells with and without exposure to menadione

2019-10-30 | GSE139540 | GEO

A two-step mechanism for epigenetic specification of centromere identity and function.

Project description:The basic determinant of chromosome inheritance, the centromere, is specified in many eukaryotes by an epigenetic mark. Using gene targeting in human cells and fission yeast, chromatin containing the centromere-specific histone H3 variant CENP-A is demonstrated to be the epigenetic mark that acts through a two-step mechanism to identify, maintain and propagate centromere function indefinitely. Initially, centromere position is replicated and maintained by chromatin assembled with the centromere-targeting domain (CATD) of CENP-A substituted into H3. Subsequently, nucleation of kinetochore assembly onto CATD-containing chromatin is shown to require either the amino- or carboxy-terminal tail of CENP-A for recruitment of inner kinetochore proteins, including stabilizing CENP-B binding to human centromeres or direct recruitment of CENP-C, respectively.

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Monopolin recruits condensin to organize centromere DNA and repetitive DNA sequences.

Project description:The establishment and maintenance of higher-order structure at centromeres is essential for accurate chromosome segregation. The monopolin complex is thought to cross-link multiple kinetochore complexes to prevent merotelic attachments that result in chromosome missegregation. This model is based on structural analysis and the requirement that monopolin execute mitotic and meiotic chromosome segregation in Schizosaccharomyces pombe, which has more than one kinetochore-microtubule attachment/centromere, and co-orient sister chromatids in meiosis I in Saccharomyces cerevisiae. Recent data from S. pombe suggest an alternative possibility: that the recruitment of condensin is the primary function of monopolin. Here we test these models using the yeast Candida albicans. C. albicans cells lacking monopolin exhibit defects in chromosome segregation, increased distance between centromeres, and decreased stability of several types of repeat DNA. Of note, changing kinetochore-microtubule copy number from one to more than one kinetochore-microtubule/centromere does not alter the requirement for monopolin. Furthermore, monopolin recruits condensin to C. albicans centromeres, and overexpression of condensin suppresses chromosome segregation defects in strains lacking monopolin. We propose that the key function of monopolin is to recruit condensin in order to promote the assembly of higher-order structure at centromere and repetitive DNA.

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Phospho-regulation of the Shugoshin - Condensin interaction at the centromere in budding yeast.

Project description:Correct bioriented attachment of sister chromatids to the mitotic spindle is essential for chromosome segregation. In budding yeast, the conserved protein shugoshin (Sgo1) contributes to biorientation by recruiting the protein phosphatase PP2A-Rts1 and the condensin complex to centromeres. Using peptide prints, we identified a Serine-Rich Motif (SRM) of Sgo1 that mediates the interaction with condensin and is essential for centromeric condensin recruitment and the establishment of biorientation. We show that the interaction is regulated via phosphorylation within the SRM and we determined the phospho-sites using mass spectrometry. Analysis of the phosphomimic and phosphoresistant mutants revealed that SRM phosphorylation disrupts the shugoshin-condensin interaction. We present evidence that Mps1, a central kinase in the spindle assembly checkpoint, directly phosphorylates Sgo1 within the SRM to regulate the interaction with condensin and thereby condensin localization to centromeres. Our findings identify novel mechanisms that control shugoshin activity at the centromere in budding yeast.

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The LINC complex transmits integrin-dependent tension to the nuclear lamina and represses epidermal differentiation.

Project description:While the mechanisms by which chemical signals control cell fate have been well studied, the impact of mechanical inputs on cell fate decisions is not well understood. Here, using the well-defined system of keratinocyte differentiation in the skin, we examine whether and how direct force transmission to the nucleus regulates epidermal cell fate. Using a molecular biosensor, we find that tension on the nucleus through linker of nucleoskeleton and cytoskeleton (LINC) complexes requires integrin engagement in undifferentiated epidermal stem cells and is released during differentiation concomitant with decreased tension on A-type lamins. LINC complex ablation in mice reveals that LINC complexes are required to repress epidermal differentiation in vivo and in vitro and influence accessibility of epidermal differentiation genes, suggesting that force transduction from engaged integrins to the nucleus plays a role in maintaining keratinocyte progenitors. This work reveals a direct mechanotransduction pathway capable of relaying adhesion-specific signals to regulate cell fate.

| S-EPMC8051949 | biostudies-literature

Mitotic phosphorylation of SUN1 loosens its connection with the nuclear lamina while the LINC complex remains intact.

Project description:At the onset mitosis in higher eukaryotes, the nuclear envelope (NE) undergoes dramatic deconstruction to allow separation of duplicated chromosomes. Studies have shown that during this process of nuclear envelope breakdown (NEBD), the extensive protein networks of the nuclear lamina are disassembled through phosphorylation of lamins and several inner nuclear membrane (INM) proteins. The LINC complex, composed of SUN and nesprin proteins, is involved in multiple interactions at the NE and plays vital roles in nuclear and cellular mechanics by connecting the nucleus to the cytoskeleton. Here, we show that SUN1, located in the INM, undergoes mitosis-specific phosphorylation on at least 3 sites within its nucleoplasmic N-terminus. We further identify Cdk1 as the kinase responsible for serine 48 and 333 phosphorylation, while serine 138 is phosphorylated by Plk1. In mitotic cells, SUN1 loses its interaction with N-terminal domain binding partners lamin A/C, emerin, and short nesprin-2 isoforms. Furthermore, a triple phosphomimetic SUN1 mutant displays increased solubility and reduced retention at the NE. In contrast, the central LINC complex interaction between the SUN1 C-terminus and the KASH domain of nesprin-2 is maintained during mitosis. Together, these data support a model whereby mitotic phosphorylation of SUN1 disrupts interactions with nucleoplasmic binding partners, promoting disassembly of the nuclear lamina and, potentially, its chromatin interactions. At the same time, our data add to an emerging picture that the core LINC complex plays an active role in NEBD.

| S-EPMC4164488 | biostudies-literature

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