Do nuclear envelope and intranuclear proteins reorganize during mitosis to form an elastic, hydrogel-like spindle matrix?

Johansen, Kristen M.; Forer, Arthur; Yao, Changfu; Girton, Jack

doi:10.1007/s10577-011-9187-6

Cited by 51 publications

(60 citation statements)

References 158 publications

(209 reference statements)

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“…3F). In mitosis, abnormal torsional movement is caused by a perturbed spindle matrix; the improper assembly of a bipolar spindle and an imbalance of spindle forces resulted in curling and twisting of spindle microtubules similar to what we observed in RBBP4-depleted oocytes (;37%) [22,23]. Moreover, when we conducted an assay to visualize microtubules that formed stable attachments to kinetochores, we observed more microtubules that curled and interlaced with each other in RBBP4 KD oocytes as compared to controls, where the microtubules most often emanated as straight rods from the poles (Fig.…”

Section: Rbbp4 Depletion Causes Defects In Spindle Formationsupporting

confidence: 82%

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

Balboula¹,

Stein²,

Schultz³

et al. 2015

Biology of Reproduction

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During meiosis I (MI) in oocytes, the maturation-associated decrease of histone acetylation is critical for normal meiotic progression and accurate chromosome segregation. RBBP4 is a component of several different histone deacetylase containing chromatin-remodeling complexes, but RBBP4's role in regulating MI is not known. Depleting RBBP4 in mouse oocytes resulted in multipolar spindles at metaphase (Met) I with subsequent perturbed meiotic progression and increased incidence of abnormal spindles, chromosome misalignment, and aneuploidy at Met II. We attribute these defects to improper deacetylation of histones because histones H3K4, H4K8, H4K12, and H4K16 were hyperacetylated in RBBP4-depleted oocytes. Importantly, we show that RBBP4-mediated histone deacetylation is essential for regulating bipolar spindle assembly, at least partially, through promoting Aurora kinase (AURK) C function. To our knowledge, these results are the first to identify RBBP4 as a regulator of histone deacetylation during oocyte maturation, and they provide evidence that deacetylation is required for bipolar spindle assembly through AURKC.

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Section: Rbbp4 Depletion Causes Defects In Spindle Formationsupporting

confidence: 82%

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

Balboula¹,

Stein²,

Schultz³

et al. 2015

Biology of Reproduction

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“…However, how this process is coordinated with disassembly and reassembly of nuclear structures during mitotic progression is poorly understood [20]. It is also not clear how cell cycle regulators and other diffusible molecules are localized and confined to the spindle region in the absence of diffusion barriers following nuclear envelope breakdown [16], [18], [21]. To begin to address these issues Yao et al [5] depolymerized tubulin by injecting colchicine into syncytial embryos prior to prophase.…”

Section: Discussionmentioning

confidence: 99%

The Spindle Matrix Protein, Chromator, Is a Novel Tubulin Binding Protein That Can Interact with Both Microtubules and Free Tubulin

Yao

Wang

et al. 2014

PLoS ONE

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The chromodomain protein, Chromator, is localized to chromosomes during interphase; however, during cell division together with other nuclear proteins Chromator redistributes to form a macro molecular spindle matrix complex that embeds the microtubule spindle apparatus. It has been demonstrated that the CTD of Chromator is sufficient for localization to the spindle matrix and that expression of this domain alone could partially rescue Chro mutant microtubule spindle defects. Furthermore, the presence of frayed and unstable microtubule spindles during mitosis after Chromator RNAi depletion in S2 cells indicated that Chromator may interact with microtubules. In this study using a variety of biochemical assays we have tested this hypothesis and show that Chromator not only has binding activity to microtubules with a Kd of 0.23 µM but also to free tubulin. Furthermore, we have mapped the interaction with microtubules to a relatively small stretch of 139 amino acids in the carboxy-terminal region of Chromator. This sequence is likely to contain a novel microtubule binding interface since database searches did not find any sequence matches with known microtubule binding motifs.

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“…4). U ext denotes the sequestration potential imposed by the spindle on the streaming proteins; it phenomenologically integrates all sequestrating factors that tend to retain SAC components within the spindle apparatus, e.g., association with spindle matrix (48)(49)(50), peri-spindle membranous networks (49,51). k B is the Boltzmann constant, and T is temperature.…”

Section: Appendixmentioning

confidence: 99%

Spindle Size Scaling Contributes to Robust Silencing of Mitotic Spindle Assembly Checkpoint

Chen

Liu

2016

Biophysical Journal

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Chromosome segregation during mitosis hinges on proper assembly of the microtubule spindle that establishes bipolar attachment to each chromosome. Experiments demonstrate allometry of mitotic spindles and a universal scaling relationship between spindle size and cell size across metazoans, which indicates a conserved principle of spindle assembly at play during evolution. However, the nature of this principle is currently unknown. Researchers have focused on deriving the mechanistic underpinning of the size scaling from the mechanical aspects of the spindle assembly process. In this work we take a different standpoint and ask: What is the size scaling for? We address this question from the functional perspectives of spindle assembly checkpoint (SAC). SAC is the critical surveillance mechanism that prevents premature chromosome segregation in the presence of unattached or misattached chromosomes. The SAC signal gets silenced after and only after the last chromosome-spindle attachment in mitosis. We previously established a model that explains the robustness of SAC silencing based on spindle-mediated spatiotemporal regulation of SAC proteins. Here, we refine the previous model, and find that robust and timely SAC silencing entails proper size scaling of mitotic spindle. This finding provides, to our knowledge, a novel, function-oriented angle toward understanding the observed spindle allometry, and the universal scaling relationship between spindle size and cell size in metazoans. In a broad sense, the functional requirement of robust SAC silencing could have helped shape the spindle assembly mechanism in evolution.

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Do nuclear envelope and intranuclear proteins reorganize during mitosis to form an elastic, hydrogel-like spindle matrix?

Cited by 51 publications

References 158 publications

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

RBBP4 Regulates Histone Deacetylation and Bipolar Spindle Assembly During Oocyte Maturation in the Mouse1

The Spindle Matrix Protein, Chromator, Is a Novel Tubulin Binding Protein That Can Interact with Both Microtubules and Free Tubulin

Spindle Size Scaling Contributes to Robust Silencing of Mitotic Spindle Assembly Checkpoint

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