Wip1 controls the translocation of the chromosomal passenger complex to the central spindle for faithful mitotic exit

2020 ◽  
Author(s):  
Xianghua Zhang ◽  
Ji Eun Park ◽  
Eun Ho Kim ◽  
Jihee Hong ◽  
Ki-Tae Hwang ◽  
...  
Keyword(s):  
Mitotic Exit ◽  
Chromosomal Passenger Complex ◽  
Central Spindle ◽  
Chromosomal Passenger

scholarly journals Uncoupling the Central Spindle-associated Function of the Chromosomal Passenger Complex from Its Role at Centromeres

2006 ◽  
Vol 17 (4) ◽  
pp. 1897-1909 ◽  
Author(s):  
Susanne M.A. Lens ◽  
Jose A. Rodriguez ◽  
Gerben Vader ◽  
Simone W. Span ◽  
Giuseppe Giaccone ◽  
...  
Keyword(s):  
Spindle Checkpoint ◽  
Aurora B ◽  
Deletion Mutants ◽  
Chromosomal Passenger Complex ◽  
Central Spindle ◽  
Survivin Protein ◽  
C Terminus ◽  
Chromosomal Passenger ◽  
Associated Function ◽  
Bir Domain

Survivin is a component of the chromosomal passenger complex (CPC) that plays a role in maintenance of an active spindle checkpoint and in cytokinesis. To study whether these different functions can be attributed to distinct domains within the Survivin protein, we complemented Survivin-depleted cells with a variety of point- and deletion-mutants of Survivin. We show that an intact baculovirus IAP repeat (BIR) domain is required for proper spindle checkpoint functioning, but dispensable for cytokinesis. In line with this, mutants lacking an intact BIR domain localized normally to the central spindle, but their localization to inner centromeres was severely perturbed. Consequently, these mutants failed to recruit Aurora B, Borealin/Dasra B, and BubR1 to centromeres and kinetochores, but they had retained the ability to recruit Aurora B and Borealin/Dasra B to the midzone and midbody. Thus, the C terminus of Survivin is sufficient for central spindle localization and execution of cytokinesis, but the additional presence of a functional BIR domain is essential for centromere targeting and spindle checkpoint function. Importantly, our data show that the function of the CPC at the centromere can be separated from its function at the central spindle and that execution of cytokinesis does not require prior concentration of the CPC at centromeres.

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

2017 ◽  
Vol 28 (25) ◽  
pp. 3634-3646 ◽  
Author(s):  
Jennifer Landino ◽  
Stephen R. Norris ◽  
Muyi Li ◽  
Edward R. Ballister ◽  
Michael A. Lampson ◽  
...  
Keyword(s):  
Live Cell Imaging ◽  
Cell Imaging ◽  
Cleavage Plane ◽  
Mitotic Exit ◽  
Actin Binding ◽  
Alternative Mechanism ◽  
Dependent Manner ◽  
Chromosomal Passenger Complex ◽  
Division Plane ◽  
Chromosomal Passenger

During cytokinesis, the chromosomal passenger complex (CPC) promotes midzone organization, specifies the cleavage plane, and regulates furrow contractility. The localizations of the CPC are coupled to its cytokinetic functions. At the metaphase-to-anaphase transition, the CPC dissociates from centromeres and localizes to midzone microtubules and the equatorial cortex. CPC relocalization to the cell middle is thought to depend on MKlp2-driven, plus end–directed transport. In support of this idea, MKlp2 depletion impairs cytokinesis; however, cytokinesis failure stems from furrow regression rather than failed initiation of furrowing. This suggests that an alternative mechanism(s) may concentrate the CPC at the division plane. We show here that direct actin binding, via the inner centromere protein (INCENP), enhances CPC enrichment at the equatorial cortex, thus acting in tandem with MKlp2. INCENP overexpression rescues furrowing in MKlp2-depleted cells in an INCENP-actin binding–dependent manner. Using live-cell imaging, we also find that MKlp2-dependent targeting of the CPC is biphasic. MKlp2 targets the CPC to the anti-parallel microtubule overlap of the midzone, after which the MKlp2-CPC complex moves in a nondirected manner. Collectively, our work suggests that both actin binding and MKlp2-dependent midzone targeting cooperate to precisely position the CPC during mitotic exit, and that these pathways converge to ensure successful cleavage furrow ingression.

scholarly journals Borealin

2004 ◽  
Vol 166 (2) ◽  
pp. 179-191 ◽  
Author(s):  
Reto Gassmann ◽  
Ana Carvalho ◽  
Alexander J. Henzing ◽  
Sandrine Ruchaud ◽  
Damien F. Hudson ◽  
...  
Keyword(s):  
Rna Interference ◽  
Histone H3 ◽  
Aurora B ◽  
Mitotic Progression ◽  
Aurora B Kinase ◽  
Chromosomal Passenger Complex ◽  
Central Spindle ◽  
Chromosomal Passenger ◽  
Bipolar Spindles

The chromosomal passenger complex of Aurora B kinase, INCENP, and Survivin has essential regulatory roles at centromeres and the central spindle in mitosis. Here, we describe Borealin, a novel member of the complex. Approximately half of Aurora B in mitotic cells is complexed with INCENP, Borealin, and Survivin; and Borealin binds Survivin and INCENP in vitro. A second complex contains Aurora B and INCENP, but no Borealin or Survivin. Depletion of Borealin by RNA interference delays mitotic progression and results in kinetochore–spindle misattachments and an increase in bipolar spindles associated with ectopic asters. The extra poles, which apparently form after chromosomes achieve a bipolar orientation, severely disrupt the partitioning of chromosomes in anaphase. Borealin depletion has little effect on histone H3 serine10 phosphorylation. These results implicate the chromosomal passenger holocomplex in the maintenance of spindle integrity and suggest that histone H3 serine10 phosphorylation is performed by an Aurora B–INCENP subcomplex.

scholarly journals APC/CCdh1 is required for the termination of chromosomal passenger complex activity upon mitotic exit

2020 ◽  
Vol 133 (18) ◽  
pp. jcs251314
Author(s):  
Takaaki Tsunematsu ◽  
Rieko Arakaki ◽  
Hidehiko Kawai ◽  
Jan Ruppert ◽  
Koichi Tsuneyama ◽  
...  
Keyword(s):  
Dna Replication ◽  
Kinase Activity ◽  
Mitotic Exit ◽  
Serum Starvation ◽  
Aurora B ◽  
Anaphase Promoting Complex ◽  
Complex Activity ◽  
Chromosomal Passenger Complex ◽  
N Terminus ◽  
Chromosomal Passenger

ABSTRACTDuring mitosis, the chromosomal passenger complex (CPC) ensures the faithful transmission of the genome. The CPC is composed of the enzymatic component Aurora B (AURKB) and the three regulatory and targeting components borealin, INCENP, and survivin (also known as BIRC5). Although the CPC is known to be involved in diverse mitotic events, it is still unclear how CPC function terminates after mitosis. Here we show that borealin is ubiquitylated by the anaphase promoting complex/cyclosome (APC/C) and its cofactor Cdh1 (also known as FZR1) and is subsequently degraded in G1 phase. Cdh1 binds to regions within the N terminus of borealin that act as a non-canonical degron. Aurora B has also been shown previously to be degraded by the APC/CCdh1 from late mitosis to G1. Indeed, Cdh1 depletion sustains an Aurora B activity with stable levels of borealin and Aurora B throughout the cell cycle, and causes reduced efficiency of DNA replication after release from serum starvation. Notably, inhibition of Aurora B kinase activity improves the efficiency of DNA replication in Cdh1-depleted cells. We thus propose that APC/CCdh1 terminates CPC activity upon mitotic exit and thereby contributes to proper control of DNA replication.

scholarly journals Mutual Dependence of Mob1 and the Chromosomal Passenger Complex for Localization during Mitosis

2010 ◽  
Vol 21 (3) ◽  
pp. 380-392 ◽  
Author(s):  
Lori Jo Wilmeth ◽  
Sanjay Shrestha ◽  
Gilbert Montaño ◽  
Jennifer Rashe ◽  
Charles Bradley Shuster
Keyword(s):  
Mitotic Exit ◽  
Signaling Cascades ◽  
Mitotic Progression ◽  
Chromosomal Passenger Complex ◽  
Related Family ◽  
Cytoplasmic Material ◽  
Spindle Poles ◽  
Chromosomal Passenger ◽  
Early Anaphase ◽  
Spindle Midzone

The spatial and temporal coordination of chromosome segregation with cytokinesis is essential to ensure that each daughter cell receives the correct complement of chromosomal and cytoplasmic material. In yeast, mitotic exit and cytokinesis are coordinated by signaling cascades whose terminal components include a nuclear Dbf2-related family kinase and a noncatalytic subunit, Mps one binding (Mob) 1. There are five human Mob1 isoforms, all of which display redundant localization patterns at the spindle poles and kinetochores in early mitosis, and the spindle midzone during cytokinesis. Mob1 shares similar localization patterns to Polo-like kinase (Plk1) and the chromosomal passenger complex (CPC), and although depletion of Plk1 resulted in a loss of Mob1 from the spindle poles, Mob1 recruitment to kinetochores was unaffected. Conversely, disruption of CPC signaling resulted in a loss of Mob1 from kinetochores without disrupting recruitment to the spindle poles. In Mob1-depleted cells, the relocalization of the CPC and mitotic kinesin-like protein (MKLP) 2 to the spindle midzone was delayed during early anaphase, and as a consequence, the midzone recruitment of MKLP1 also was affected. Together, these results suggest that Mob1 and the other mammalian orthologues of the mitotic exit network regulate mitotic progression by facilitating the timely mobilization of the CPC to the spindle midzone.

scholarly journals Chromosome-directed oocyte spindle assembly depends HP1 and the Chromosomal Passenger Complex

2020 ◽  
Author(s):  
Lin-Ing Wang ◽  
Tyler DeFosse ◽  
Rachel A. Battaglia ◽  
Victoria F. Wagner ◽  
Kim S. McKim
Keyword(s):  
Homologous Chromosome ◽  
Spindle Assembly ◽  
Aurora B ◽  
Aurora B Kinase ◽  
Chromosomal Passenger Complex ◽  
Central Spindle ◽  
Bipolar Spindle ◽  
Chromosomal Passenger ◽  
Spindle Microtubules

AbstractThe chromosomes in the oocytes of many animals appear to promote bipolar spindle assembly. In Drosophila oocytes, spindle assembly requires the chromosomal passenger complex (CPC), which consists of INCENP, Borealin, Survivin and Aurora B. To determine what recruits the CPC to the chromosomes and its role in spindle assembly, we developed a strategy to manipulate the function and localization of INCENP, which is critical for recruiting the Aurora B kinase. We found that an interaction between Borealin and HP1 is crucial for the initial recruitment of the CPC to the chromosomes and is sufficient to build kinetochores and recruit spindle microtubules. We also found that HP1 moves from the chromosomes to the spindle microtubules along with the CPC, and based on this, propose a mechanism for how the CPC moves from the chromosomes to the microtubules. Within the central spindle, rather than at the centromeres, the CPC and HP1 are required for homologous chromosome bi-orientation.

scholarly journals Molecular basis of MKLP2-dependent Aurora B transport from chromatin to the anaphase central spindle

2020 ◽  
Vol 219 (7) ◽  
Author(s):  
Michela Serena ◽  
Ricardo Nunes Bastos ◽  
Paul R. Elliott ◽  
Francis A. Barr
Keyword(s):  
Atpase Activity ◽  
Molecular Basis ◽  
Histone H3 ◽  
Aurora B ◽  
Complete Structure ◽  
Chromosomal Passenger Complex ◽  
Central Spindle ◽  
Dependent Atpase ◽  
Chromosomal Passenger ◽  
Dependent Transport

The Aurora B chromosomal passenger complex (CPC) is a conserved regulator of mitosis. Its functions require localization first to the chromosome arms and then centromeres in mitosis and subsequently the central spindle in anaphase. Here, we analyze the requirements for core CPC subunits, survivin and INCENP, and the mitotic kinesin-like protein 2 (MKLP2) in targeting to these distinct localizations. Centromere recruitment of the CPC requires interaction of survivin with histone H3 phosphorylated at threonine 3, and we provide a complete structure of this assembly. Furthermore, we show that the INCENP RRKKRR-motif is required for both centromeric localization of the CPC in metaphase and MKLP2-dependent transport in anaphase. MKLP2 and DNA bind competitively to this motif, and INCENP T59 phosphorylation acts as a switch preventing MKLP2 binding in metaphase. In anaphase, CPC binding promotes the microtubule-dependent ATPase activity of MKLP2. These results explain how centromere targeting of the CPC in mitosis is coupled to its movement to the central spindle in anaphase.

scholarly journals Effects of Full-Length Borealin on the Composition and Protein−Protein Interaction Activity of a Binary Chromosomal Passenger Complex†

Biochemistry ◽  
2009 ◽  
Vol 48 (6) ◽  
pp. 1156-1161 ◽  
Author(s):  
Lihong Zhou ◽  
Jiejin Li ◽  
Roger George ◽  
Sandrine Ruchaud ◽  
Hong-Gang Zhou ◽  
...  
Keyword(s):  
Protein Interaction ◽  
Full Length ◽  
Chromosomal Passenger Complex ◽  
Protein Protein Interaction ◽  
Chromosomal Passenger
Sign in / Sign up

Export Citation Format

Share Document