Complex Commingling: Nucleoporins and the Spindle  Assembly Checkpoint

Mossaid, Ikram; Fahrenkrog, Birthe

doi:10.3390/cells4040706

Cited by 20 publications

(16 citation statements)

References 145 publications

(227 reference statements)

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“…These data support previous studies in humans and other organisms that have shown that MAD1L1 associates with TPR, NUP153, and NUP107 and is important for generating the MAD1L1-MAD2L1 complex in early mitosis to establish the SAC (62)(63)(64)(65)(66)(67)(68). Similarly, MAD2L1 was found to associate with TPR (previously verified in (63), NUP50, Nup153, NUP210 and ELYS (supplemental Fig.…”

Section: Analysis Of Core Sac Protein-kinetochore Protein Proximity Asupporting

confidence: 90%

Dissection of the Spindle Assembly Checkpoint by Proximity Proteomics

Garcia

Velasquez

Gao

et al. 2020

Preprint

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The spindle assembly checkpoint (SAC) is critical for sensing defective microtubule-kinetochore attachments and tension across the kinetochore and functions to arrest cells in prometaphase to allow time to repair any errors prior to proceeding into anaphase. The SAC has a central role in ensuring the fidelity of chromosome segregation and its dysregulation has been linked to the development of human diseases like cancer. The establishment and maintenance of the SAC relies on multiple protein complexes that are intricately regulated in a spatial and temporal manner through posttranslational modifications like phosphorylation. Over the past few decades the SAC has been highly investigated and much has been learned about its protein constituents and the pathways and factors that regulate its activity. However, the spatio-temporal proximity associations of the core SAC components have not been explored in a systematic manner. Here, we have taken a BioID2 proximity-labeling proteomic approach to define the proximity protein environment for each of the five core SAC proteins BUB1, BUB3, BUBR1, MAD1L1, and MAD2L1 under conditions where the SAC is active in prometaphase. These five protein association maps were integrated to generate the SAC proximity protein network that contains multiple layers of information related to core SAC protein complexes, protein-protein interactions, and proximity associations. Our analysis validated many of the known SAC complexes and protein-protein interactions. Additionally, it uncovered new protein associations that lend insight into the functioning of the SAC and highlighted future areas that should be investigated to generate a comprehensive understanding of the SAC.3

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Section: Analysis Of Core Sac Protein-kinetochore Protein Proximity Asupporting

confidence: 90%

Dissection of the Spindle Assembly Checkpoint by Proximity Proteomics

Garcia

Velasquez

Gao

et al. 2020

Preprint

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“…One possibility to explain these findings is to consider that MAD2 plays a role controlling the translocation of DNA damage repair proteins to the nucleus [27] . In agreement with these results, MAD2 has been shown to be localized at the nuclear pore during interphase and to interact with TRp1 and Nup153 proteins [28] . For instance, in a work performed using HeLa cells, it was demonstrated that MAD2 interacts with XPD and ERCC1, two key proteins that participate in nucleotide excision repair pathway (NER).…”

Section: Mad2 More Than a Mitotic Regulator?supporting

confidence: 79%

MAD2 in the Spotlight as a Cancer Therapy Regulator

Sanchez-Perez¹

2016

IJCO

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MAD2 is a key protein required for mitotic checkpoint function and for the maintenance of accuracy on the mitotic process of every cell cycle. Deregulation of MAD2 is associated with both progression and poor prognosis in cancer disease. However, new evidence highlights the implication of MAD2 in other biological functions besides its classical Mitotic checkpoint implication, such as apoptosis, senescence and also DNA damage repair, which can ultimately define the response to a specific treatment. Development of novel therapeutic approaches and optimization of the existing therapies are now required for the design of successful treatments of cancer. MAD2 is emerging as a new key target for the design of more effective and personalized treatments in cancer disease.

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“…The duration of mitosis depends both on mitotic timers and on satisfaction of the spindle assembly checkpoint [68][69][70][71] . When a minimal time has elapsed and the last pair of chromosomes has been aligned at the metaphase plate (reviewed in REF.…”

Section: Mitotic Exitmentioning

confidence: 99%

Coupling changes in cell shape to chromosome segregation

Ramkumar

Baum

2016

Nat Rev Mol Cell Biol

124

132

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Animal cells undergo dramatic changes in shape, mechanics and polarity as they progress through the different stages of cell division. These changes begin at mitotic entry, with cell-substrate adhesion remodelling, assembly of a cortical actomyosin network and osmotic swelling, which together enable cells to adopt a near spherical form even when growing in a crowded tissue environment. These shape changes, which probably aid spindle assembly and positioning, are then reversed at mitotic exit to restore the interphase cell morphology. Here, we discuss the dynamics, regulation and function of these processes, and how cell shape changes and sister chromatid segregation are coupled to ensure that the daughter cells generated through division receive their fair inheritance.

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Complex Commingling: Nucleoporins and the Spindle Assembly Checkpoint

Cited by 20 publications

References 145 publications

Dissection of the Spindle Assembly Checkpoint by Proximity Proteomics

Dissection of the Spindle Assembly Checkpoint by Proximity Proteomics

MAD2 in the Spotlight as a Cancer Therapy Regulator

Coupling changes in cell shape to chromosome segregation

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