Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division

Landino, Jennifer; Norris, Stephen R.; Li, Muyi; Ballister, Edward R.; Lampson, Michael A.; Ohi, Ryoma

doi:10.1091/mbc.e17-06-0399

Cited by 28 publications

(44 citation statements)

References 41 publications

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“…The localization of PLK1 to the central spindle also requires MKLP2, suggesting that PLK1 may associate with the CPC at this structure, like it does at centromeres (44,144,196). In addition, the CPC is targeted to the equatorial cortex through direct INCENP binding to actin (197)(198)(199). Notably, the depletion of CEP192 in human cells inhibits Rac1, a member of the Rho GTPase family that promotes actin polymerization and has been implicated in tumor invasiveness and metastasis (200,201).…”

Section: The Cep192 Complex and The Cpc In The Coevolution Of Centrosmentioning

confidence: 99%

Aurora-PLK1 cascades as key signaling modules in the regulation of mitosis

Joukov¹,

2018

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Mitosis is controlled by reversible protein phosphorylation involving specific kinases and phosphatases. A handful of major mitotic protein kinases, such as the cyclin B-CDK1 complex, the Aurora kinases, and Polo-like kinase 1 (PLK1), cooperatively regulate distinct mitotic processes. Research has identified proteins and mechanisms that integrate these kinases into signaling cascades that guide essential mitotic events. These findings have important implications for our understanding of the mechanisms of mitotic regulation and may advance the development of novel antimitotic drugs. We review collected evidence that in vertebrates, the Aurora kinases serve as catalytic subunits of distinct complexes formed with the four scaffold proteins Bora, CEP192, INCENP, and TPX2, which we deem "core" Aurora cofactors. These complexes and the Aurora-PLK1 cascades organized by Bora, CEP192, and INCENP control crucial aspects of mitosis and all pathways of spindle assembly. We compare the mechanisms of Aurora activation in relation to the different spindle assembly pathways and draw a functional analogy between the CEP192 complex and the chromosomal passenger complex that may reflect the coevolution of centrosomes, kinetochores, and the actomyosin cleavage apparatus. We also analyze the roles and mechanisms of Aurora-PLK1 signaling in the cell and centrosome cycles and in the DNA damage response.

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Section: The Cep192 Complex and The Cpc In The Coevolution Of Centrosmentioning

confidence: 99%

Aurora-PLK1 cascades as key signaling modules in the regulation of mitosis

Joukov¹,

2018

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“…This gradient provides spatial information to position the cleavage furrow [48]. INCENP interacts with actin [49], or MKLP2 in a Myosin II-dependent manner [50], to target the CPC to the equatorial cortex and initiate cleavage furrow ingression. In INCENPb knockdown embryos, cleavage furrows formed and progressed as normal, and NER occurred during telophase, even though Aurora B localization to the central spindle was substantially reduced at early anaphase and became undetectable thereafter (Figure 7).…”

Section: Incenpb Is Critical For the Localization And Activity Of Aurmentioning

confidence: 99%

Switching of INCENP paralogs controls transitions in mitotic chromosomal passenger complex functions

et al. 2019

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A single inner centromere protein (INCENP) found throughout eukaryotes modulates Aurora B kinase activity and chromosomal passenger complex (CPC) localization, which is essential for timely mitotic progression. It has been proposed that INCENP might act as a rheostat to regulate Aurora B activity through mitosis, with successively higher activity threshold levels for chromosome alignment, the spindle checkpoint, anaphase spindle transfer and finally spindle elongation and cytokinesis. It remains mechanistically unclear how this would be achieved. Here, we reveal that the urochordate, Oikopleura dioica, possesses two INCENP paralogs, which display distinct localizations and subfunctionalization in order to complete M-phase. INCENPa was localized on chromosome arms and centromeres by prometaphase, and modulated Aurora B activity to mediate H3S10/S28 phosphorylation, chromosome condensation, spindle assembly and transfer of the CPC to the central spindle. Polo-like kinase (Plk1) recruitment to CDK1 phosphorylated INCENPa was crucial for INCENPa-Aurora B enrichment on centromeres. The second paralog, INCENPb was enriched on centromeres from prometaphase, and relocated to the central spindle at anaphase onset. In the absence of INCENPa, meiotic spindles failed to form, and homologous chromosomes did not segregate. INCENPb was not required for early to mid M-phase events but became essential for the activity and localization of Aurora B on the central spindle and midbody during cytokinesis in order to allow abscission to occur. Together, our results demonstrate that INCENP paralog switching on centromeres modulates Aurora B kinase localization, thus chronologically regulating CPC functions during fast embryonic divisions in the urochordate O. dioica.

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“…Cleavage furrow ingression is controlled by proteins involved in regulating spindle assembly dynamics, which include microtubule associated proteins (α-tubulin), the centraspindlin complex, and the chromosome passenger complex (CPC), comprised of Survivin, Borealin, Inner Centromere Protein (INCENP), and Aurora B kinase (AURKB) 30 . CPC localization at the equatorial cortex is required for sustained cleavage furrow ingression 30,31 . One of the key requirements for completion of cytokinesis is the assembly of the microtubules, specification of the cleavage plane and timely localization of the chromosome passenger complex (CPC) to the cleavage furrow 29,30 .…”

Section: Yb-1 Is Required For Initiation Of Cleavage Furrow Formationmentioning

confidence: 99%

“…Formation of the cleavage furrow requires establishment of the cleavage plane during late metaphase, together with timely localisation of the CPC and organisation of the microtubule fibers at the midzone 30,31 . However, the mechanism that is responsible for establishment of the cleavage plane is unknown 29 .…”

Section: Yb-1 Is Required For Initiation Of Cleavage Furrow Formationmentioning

confidence: 99%

Critical role for cold shock protein YB-1 in cytokinesis

Mehta

Algie

Al-Jabri

et al. 2020

Preprint

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Y-box-binding protein-1, YB-1, is essential for cell division, but it is not clear how it functions. Using live imaging and confocal microscopy we show that YB-1 functions only in the last step of division, specifically being required to initiate cytokinesis. ABSTRACTHigh levels of the cold shock protein Y-box-binding protein-1, YB-1, are tightly correlated with increased cell proliferation and cancer progression. However, the precise mechanism by which YB-1 regulates proliferation is unknown. Here, we found that YB-1 depletion in several cell lines resulted in cytokinesis failure, multinucleation and an increase in G1 transit time. Rescue experiments indicated that YB-1 was required for completion of cytokinesis. Using confocal imaging of cells undergoing cytokinesis both in vitro and in zebrafish embryos, we found that YB-1 was critical for microtubule organization during cytokinesis. Using mass spectrometry we identified multiple novel phosphorylation sites on YB-1. We show that phosphorylation of YB-1 at multiple serine residues was essential for its function during cytokinesis. Using atomistic modelling we show how multiple phosphorylations alter YB-1 conformation, allowing it to interact with protein partners. Our results establish phosphorylated YB-1 as a critical regulator of cytokinesis, defining for the first time precisely how YB-1 regulates cell division.Word Count 157 / 160 words

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Two mechanisms coordinate the recruitment of the chromosomal passenger complex to the plane of cell division

Cited by 28 publications

References 41 publications

Aurora-PLK1 cascades as key signaling modules in the regulation of mitosis

Aurora-PLK1 cascades as key signaling modules in the regulation of mitosis

Switching of INCENP paralogs controls transitions in mitotic chromosomal passenger complex functions

Critical role for cold shock protein YB-1 in cytokinesis

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