Dynamic relocalization of the chromosomal passenger complex proteins inner centromere protein (INCENP) and aurora-B kinase during male mouse meiosis

Abstract

INCENP and aurora-B kinase are two chromosomal passenger proteins that are thought to play key roles in coordinating chromosome segregation with cytokinesis in somatic cells. Here we have analyzed their subcellular distribution, and that of phosphorylated histone H3, and the timing of their relative appearance in mouse spermatocytes during both meiotic divisions. Our results show that in mitotic spermatogonial cells, INCENP and aurora-B show the same pattern of distribution as they do in cultured somatic cells. INCENP labels the synaptonemal complex central element from zygotene up to late pachytene when it begins to relocalize to heterochromatic chromocentres. Aurora-B first appears at chromocentres in late diplotene before the initial phosphorylation of histone H3. INCENP and aurora-B concentrate at centromeres during diakinesis and appear during metaphase I as T-shaped signals at their inner domains, just below associated sister kinetochores. During late anaphase I both proteins relocalize to the spindle midzone. Both proteins colocalize at a connecting strand traversing the centromere region and joining sister kinetochores, in metaphase II centromeres. This strand disappears at the metaphase II/anaphase II transition and relocalizes to the spindle midzone. We discuss the complex dynamic relocalization of the chromosomal passenger complex during prophase I. Additionally, we suggest that this complex may regulate sister-chromatid centromere cohesion during both meiotic divisions.

Involvement of the cohesin Rad21 and SCP3 in monopolar attachment of sister kinetochores during mouse meiosis I

“…4G). The same results were observed after colocalizing SCP3 with the aurora-B kinase, that in turn colocalized with INCENP (Parra et al, 2003). Altogether, these results show that SCP3 and SCP2 are located at the inner centromere domain beneath the closely associated sister kinetochores, and colocalizing with the chromosomal passenger complex proteins INCENP and aurora-B.…”

“…We have recently found in mouse spermatocytes that INCENP and aurora-B colocalize at the inner domain of metaphase I centromeres and at a connecting strand joining sister kinetochores in metaphase II centromeres. Accordingly, we have proposed that these passenger proteins may regulate sister-chromatid centromere cohesion during both meiotic divisions (Parra et al, 2003).…”

Evaluation of the Aurora Kinase Inhibitor, ZM447439, in Canine Malignant Lymphoid Cells <i>in Vitro</i>

“…Previous studies have shown that aurora-A and aurora-B are overexpressed by a variety of tumors, including bladder, breast, colorectal, esophageal, glioma, pancreatic and prostate tumors in humans [8][9][10][11][12][13]. Aurora-B is located at chromosome 17 p 13.1, and localizes at centromeres during prometaphase; then relocates to the central spindle and the midbody during anaphase and telophase [14,15]. Aurora-B is also a part of the chromosome passenger complex, which contains important factors such as the inner centromere proteins borealin and survivin, necessary for proper kinetochore-microtubule attachment [16].…”

Gene mapping of sperm quality parameters in recombinant inbred strains of mice

“…Other genes found in this region, Hist3h2ba, Hist3h2bb and Hist3h2a (histone 3, H2ba, H2bb, H2a), are responsible for histone 3 activity and function. The protein product of Aurkb, aurora kinase B, which is active before histone phosphorylation (Parra et al, 2003), influences chromosome segregation in male meiosis (Tang et al, 2006) and is responsible for an increased level of abnormal sperm head morphology (Chemes and Rawe, 2003). Another candidate gene in region 11q24-11q31 is Sparc, coding for a secreted acidic cysteine-rich glycoprotein which may influence the formation of abnormal spermatozoa due to its role in the regulation of embryonic testis development (Wilson et al, 2006).…”