The Chromosomal Passenger Complex Is Required for Chromatin-Induced Microtubule Stabilization and Spindle Assembly

Sampath, Srinath C.; Ohi, Ryoma; Leismann, Oliver; Salic, Adrian; Pozniakovski, Andrei; Funabiki, Hironori

doi:10.1016/j.cell.2004.06.026

Cited by 400 publications

(489 citation statements)

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“…The CPPs Survivin, Aurora B, INCENP and Borealin sequentially colocalize to the chromosome centromeres, the spindle midzone, the cleavage furrow and finally to the midbody as mitosis progresses (Adams et al, 2001a, b;Gassman et al, 2004;Sampath et al, 2004). The CPPs are already expressed at the G2/M transition and, at least in the case of Survivin, expression at earlier cell cycle stages has been reported in different types of both normal and tumor cells (Krysan et al, 2004;Song et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…Like INCENP, Survivin has been reported to constitute both a substrate and an activator for Aurora B (Chen et al, 2003;Wheatley et al, 2004). Borealin, which was independently isolated as DasraB, is the most recently identified and the least characterized subunit of the chromosomal passenger complex (Gassman et al, 2004;Sampath et al, 2004). Borealin is phosphorylated by Aurora B in vitro but, unlike Survivin and INCENP, does not appear to increase the activity of the kinase (Gassman et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

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Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

et al. 2006

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As mitosis progresses, the chromosomal passenger proteins (CPPs) Survivin, Aurora B, INCENP and Borealin dynamically colocalize to mitotic structures. Chromosomal passenger proteins are already expressed during G2, whereas the nuclear envelope is only disassembled at the end of prophase. However, the mechanisms that modulate their nucleocytoplasmic localization before nuclear envelope breakdown (NEB) are poorly characterized. Using epitope-tagged proteins, we show that Aurora B, like Survivin, undergoes CRM1-mediated nucleocytoplasmic shuttling, although both proteins lack identifiable 'classical' nuclear transport signals. On the other hand, INCENP resides more stably in the nucleus and contains multiple nuclear localization signals. Finally, Borealin was detected in the nucleolus and the cytoplasm, but its cytoplasmic localization is not directly regulated by CRM1. Coexpression experiments indicate that the nuclear localization of Aurora B, but not of Survivin, is modulated by INCENP and that Survivin prevents the nucleolar accumulation of Borealin. Our data reveal that, in contrast to their closely related localization during mitosis, the nucleocytoplasmic localization of the CPPs before NEB is largely unrelated. Furthermore, the specific effect of INCENP and Survivin on the localization of Aurora B and Borealin, respectively, suggests that different complexes of CPPs may exist not only during mitosis, as recently reported, but also before NEB.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

et al. 2006

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“…These are molecules of the chromosomal passenger complex (CDCA8 and Aurora kinase B; ref. 34 37,38), and several members of the kinesin superfamily of mitotic motor proteins involved in spindle function and cytokinesis (KIFC1, KIF23, KIF11, and KNSL7; refs. 39 -45).…”

Section: Discussionmentioning

confidence: 99%

Expression of Late Cell Cycle Genes and an Increased Proliferative Capacity Characterize Very Early Relapse of Childhood Acute Lymphoblastic Leukemia

Kirschner-Schwabe

Lottaz

Tödling

et al. 2006

Clinical Cancer Research

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Purpose: In childhood acute lymphoblastic leukemia (ALL), f25% of patients suffer from relapse. In recurrent disease, despite intensified therapy, overall cure rates of 40% remain unsatisfactory and survival rates are particularly poor in certain subgroups. The probability of long-term survival after relapse is predicted from well-established prognostic factors (i.e., time and site of relapse, immunophenotype, and minimal residual disease). However, the underlying biological determinants of these prognostic factors remain poorly understood. Experimental Design: Aiming at identifying molecular pathways associated with these clinically well-defined prognostic factors, we did gene expression profiling on 60 prospectively collected samples of first relapse patients enrolled on the relapse trial ALL-REZ BFM 2002 of the Berlin-Frankfurt-Mu« nster study group. Results: We show here that patients with very early relapse of ALL are characterized by a distinctive gene expression pattern.We identified a set of 83 genes differentially expressed in very early relapsed ALL compared with late relapsed disease. The vast majority of genes were up-regulated and many were late cell cycle genes with a function in mitosis. In addition, samples from patients with very early relapse showed a significant increase in the percentage of S and G 2 -M phase cells and this correlated well with the expression level of cell cycle genes. Conclusions: Very early relapse of ALL is characterized by an increased proliferative capacity of leukemic blasts and up-regulated mitotic genes.The latter suggests that novel drugs, targeting late cell cycle proteins, might be beneficial for these patients that typically face a dismal prognosis.Acute lymphoblastic leukemia (ALL) is the most common malignant disease in children (1). Although event-free survival rates range between 70% and 75%, relapse of ALL remains the fourth most frequent diagnosis in childhood cancer affecting 25% of ALL patients (2). At relapse, overall cure rates of f40% remain unsatisfactory and survival rates are particularly poor in certain subgroups (3). Treatment of relapse usually implies intensified polychemotherapy containing high-dose elements. Although in most children, second remissions can be induced high-risk patients require further treatment intensification by stem cell transplantation. Stem cell transplantation provides a better relapse-free survival rate than chemotherapy alone but is also associated with higher treatment-related morbidity and mortality rates (2). Thus, alternative treatment strategies are needed to improve the treatment and outcome of patients with relapsed ALL.In the treatment of ALL relapse, intensity of chemotherapy and stem cell transplantation are indicated by well-established prognostic factors (summarized in ref.2), with the most evident being the time to relapse. Early recurrence of disease with respect to frontline therapy affects f60% of patients and is associated with a high rate of nonresponse to treatment, shorter duration of second ...

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“…We therefore asked whether the effects seen on this pathway upon depletion of Sgo could be specifically linked to any of these two kinases. Aurora B is present in Xenopus extracts in the so-called chromosomal passenger complex (CPC), together with INCENP, survivin, and Dasra/ Borealin (Sampath et al 2004). The CPC is required for proper localization of Sgo and Bub1 in early mitosis (Vigneron et al 2004;Resnick et al 2006;Boyarchuk et al 2007).…”

Section: Cohesin Distribution Is Affected By Sgo Depletionmentioning

confidence: 99%

Shugoshin regulates cohesion by driving relocalization of PP2A in Xenopus extracts

Rivera

Losada

2008

Chromosoma

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The Chromosomal Passenger Complex Is Required for Chromatin-Induced Microtubule Stabilization and Spindle Assembly

Cited by 400 publications

References 46 publications

Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

Subcellular localization and nucleocytoplasmic transport of the chromosomal passenger proteins before nuclear envelope breakdown

Expression of Late Cell Cycle Genes and an Increased Proliferative Capacity Characterize Very Early Relapse of Childhood Acute Lymphoblastic Leukemia

Shugoshin regulates cohesion by driving relocalization of PP2A in Xenopus extracts

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