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Aurora-C interactions with members of the Chromosome Passenger Complex (CPC), Survivin and Inner Centromere Protein (INCENP) in reference to known Aurora-B interactions to understand the functional significance of Aurora-C overexpression in human cancer cells, is reported.
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Data unveils a novel mechanism of PRMT1-mediated CPC regulation through methylation of INCENP.
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The data suggest that INCENP in the chromosomal passenger complex pathway contributes to estrogen receptor-negative breast cancer susceptibility in the European population.
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Our results provide the structural basis and energetics of the human Aurora-A(G198N) - INCENP complex
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v-Src induces the failure of cytokinesis and the delocalization of Mklp1, Aurora B, and INCENP from the spindle midzone.
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HP1alpha binding by INCENP or Shugoshin 1 (Sgo1) is dispensable for centromeric cohesion protection during mitosis of human cells, but might regulate yet unknown interphase functions of the chromosome passenger complex (CPC) or Sgo1 at the centromeres.
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Results indicate that INCENP-Aurora B localized at centromeres/inner kinetochores is sufficient to mediate SAC activity upon spindle disruption.
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Dephosphorylation of INCENP at anaphase and the concomitant relocation of the chromosomal passenger protein complex prevents kinetochore recruitment of mitotic checkpoint proteins.
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Data show that binding to INCENP is alone critical to the distinct function of Aurora B, and although G198 of Aurora A is required for TPX2 binding, N142G Aurora B retains INCENP binding and Aurora B function.
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Aurora B kinase activity is stimulated by INCENP and C-terminal region of INCENP is sufficient for activation
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association with inner centromere protein (INCENP) activates the novel chromosomal passenger protein, Aurora-C
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Recruitment of MKLP1 to the midzone/midbody by INCENP is a crucial step for the midbody formation and completion of cytokinesis in mammalian cells.
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Aurora-C is a chromosomal passenger protein that disrupts the association of INCENP with Aurora-B and may serve as a key regulator in cell division
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Data show that INCENP has an important role in stabilizing the chromosomal passenger complex, and that Borealin acts to promote binding of Survivin to INCENP.
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INCENP phosphorylation by Cdk1 is necessary for the recruitment of Plk1 to the kinetochore.
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A functional module within the chromosomal passenger complex involving the inner centromere protein INCENP, Survivin, and Borealin.
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protein truncation and in vitro mutagenesis,have identified the nucleolar localization sequences on INCENP
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Borealin and INCENP associate with the helical domain of Survivin to form a tight three-helical bundle.
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High INCENP expression is associated with high grade non-Hodgkin B-cell lymphomas.
