The dynamic spindle matrix

Schweizer, Nina; Weiß, Matthias; Maiato, Hélder

doi:10.1016/j.ceb.2014.01.002

Cited by 30 publications

(26 citation statements)

References 46 publications

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“…The concept of a spindle matrix has long been proposed [12], [13]; however, whether such a structure exists and its molecular composition and how it may interact with the microtubule-based spindle apparatus has remained controversial (reviewed in [14]–[19]). In this study using a variety of biochemical assays we show that the spindle matrix protein, Chromator, can directly interact with microtubules as well as with free tubulin.…”

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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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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“…Different turnover rates were measured at the middle of the spindle versus near poles (63, 64), and selective MT stabilization at poles has been suggested (65). The spindle environment could also stabilize MTs (66, 67), and a mechanical matrix could support the spindle (68). Tight length regulation has been proposed as a principle to shape the spindle (69).…”

Section: What Is the Metaphase Spindle?mentioning

confidence: 99%

Mechanisms of Mitotic Spindle Assembly

Petry

2016

Annu. Rev. Biochem.

195

187

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Life depends on cell proliferation and the accurate segregation of chromosomes, which are mediated by the microtubule (MT)-based mitotic spindle and ~200 essential MT-associated proteins. Yet, a mechanistic understanding of how the mitotic spindle is assembled and achieves chromosome segregation is still missing. This is mostly due to the density of MTs in the spindle, which presumably precludes their direct observation. Recent insight has been gained into the molecular building plan of the metaphase spindle using bulk and single-molecule measurements combined with computational modeling. MT nucleation was uncovered as a key principle of spindle assembly, and mechanistic details about MT nucleation pathways and their coordination are starting to be revealed. Lastly, advances in studying spindle assembly can be applied to address the molecular mechanisms of how the spindle segregates chromosomes.

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“…These include the RanGEF RCC1, the RanGAP, its activating partner RanBP1, and RanBP2 (Figure 2A) [18,19]. Interestingly, some proteins that are nuclear in interphase and SAFs in mitosis, such as lamin B and Rae1, are part of a mitotic spindle matrix, an entity that includes all proteins encompassed in the cytoplasmic region of the spindle [9,20–22]. …”

Section: Spindle Assembly Factors: Extensive Regulationmentioning

confidence: 99%

Nuclear transport factors: global regulation of mitosis

Forbes

Travesa

Nord

et al. 2015

Current Opinion in Cell Biology

107

110

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The unexpected repurposing of nuclear transport proteins from their function in interphase to an equally vital and very different set of functions in mitosis was very surprising. The multi-talented cast when first revealed included the import receptors, importin alpha and beta, the small regulatory GTPase RanGTP, and a subset of nuclear pore proteins. In this review, we report that recent years have revealed new discoveries in each area of this expanding story in vertebrates: (a) The cast of nuclear transport receptors playing a role in mitotic spindle regulation has expanded: both transportin, a nuclear import receptor, and Crm1/Xpo1, an export receptor, are involved in different aspects of spindle assembly. Importin beta and transportin also regulate nuclear envelope and pore assembly. (b) The role of nucleoporins has grown to include recruiting the key microtubule nucleator the γ-TuRC complex and the exportin Crm1 to the mitotic kinetochores of humans. Together they nucleate microtubule formation from the kinetochores towards the centrosomes. (c) New research finds that the original importin beta/RanGTP team have been further co-opted by evolution to help regulate other cellular and organismal activities, ranging from the actual positioning of the spindle within the cell perimeter, to regulation of a newly discovered spindle microtubule branching activity, to regulation of the interaction of microtubule structures with specific actin structures. (d) Lastly, because of the multitudinous roles of karyopherins throughout the cell cycle, a recent large push toward testing their potential as chemotherapeutic targets has begun to yield burgeoning progress in the clinic.

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The dynamic spindle matrix

Cited by 30 publications

References 46 publications

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

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

Mechanisms of Mitotic Spindle Assembly

Nuclear transport factors: global regulation of mitosis

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