Structure of a Blinkin-BUBR1 Complex Reveals an Interaction Crucial for Kinetochore-Mitotic Checkpoint Regulation via an Unanticipated Binding Site

@inproceedings{BolanosGarcia2011StructureOA,
  title={Structure of a Blinkin-BUBR1 Complex Reveals an Interaction Crucial for Kinetochore-Mitotic Checkpoint Regulation via an Unanticipated Binding Site},
  author={Victor M. Bolanos-Garcia and Tiziana Lischetti and Dijana Matak-Vinkov{\'i}c and Ernesto Cota and Pete J. Simpson and Dimitri Y. Chirgadze and David R. Spring and Carol V Robinson and Jakob Nilsson and Tom L. Blundell},
  booktitle={Structure},
  year={2011}
}
The maintenance of genomic stability relies on the spindle assembly checkpoint (SAC), which ensures accurate chromosome segregation by delaying the onset of anaphase until all chromosomes are properly bioriented and attached to the mitotic spindle. BUB1 and BUBR1 kinases are central for this process and by interacting with Blinkin, link the SAC with the kinetochore, the macromolecular assembly that connects microtubules with centromeric DNA. Here, we identify the Blinkin motif critical for… CONTINUE READING
BETA

Similar Papers

Citations

Publications citing this paper.
SHOWING 1-10 OF 32 CITATIONS

Functional organization of the CCAN protein complex

VIEW 4 EXCERPTS
CITES BACKGROUND
HIGHLY INFLUENCED

Direct binding between BubR1 and B56-PP2A phosphatase complexes regulate mitotic progression.

  • Journal of cell science
  • 2013
VIEW 4 EXCERPTS
CITES METHODS
HIGHLY INFLUENCED

The Bub1-TPR Domain Interacts Directly with Mad3 to Generate Robust Spindle Checkpoint Arrest

Ioanna Leontiou, Nitobe London, +7 authors Kevin G. Hardwick
  • Current Biology
  • 2019
VIEW 1 EXCERPT
CITES BACKGROUND