4BL0

Crystal structure of yeast Bub3-Bub1 bound to phospho-Spc105

4BL0 の概要

• エントリーDOI: 10.2210/pdb4bl0/pdb
• 分子名称: CELL CYCLE ARREST PROTEIN BUB3, CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1, SPINDLE POLE BODY COMPONENT SPC105, ... (5 entities in total)
• 機能のキーワード: cell cycle, bubr1, mad3, rae1, gle2, glebs, mad1, mad2, spindle assembly checkpoint, knl1, casc5, spc7, blinkin, kinetochore, mitosis, cell division, aneuploidy
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Nucleus (Probable): P26449; Nucleus: P41695; Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body: P53148
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 99280.60

構造登録者

Primorac, I.,Weir, J.R.,Musacchio, A. (登録日: 2013-04-30, 公開日: 2013-09-18, 最終更新日: 2024-10-09)

主引用文献

Primorac, I.,Weir, J.R.,Chiroli, E.,Gross, F.,Hoffmann, I.,Van Gerwen, S.,Ciliberto, A.,Musacchio, A.
Bub3 Reads Phosphorylated Melt Repeats to Promote Spindle Assembly Checkpoint Signaling
Elife, 2:01030-, 2013

PubMed Abstract: Regulation of macromolecular interactions by phosphorylation is crucial in signaling networks. In the spindle assembly checkpoint (SAC), which enables errorless chromosome segregation, phosphorylation promotes recruitment of SAC proteins to tensionless kinetochores. The SAC kinase Mps1 phosphorylates multiple Met-Glu-Leu-Thr (MELT) motifs on the kinetochore subunit Spc105/Knl1. The phosphorylated MELT motifs (MELT(P)) then promote recruitment of downstream signaling components. How MELT(P) motifs are recognized is unclear. In this study, we report that Bub3, a 7-bladed β-propeller, is the MELT(P) reader. It contains an exceptionally well-conserved interface that docks the MELT(P) sequence on the side of the β-propeller in a previously unknown binding mode. Mutations targeting the Bub3 interface prevent kinetochore recruitment of the SAC kinase Bub1. Crucially, they also cause a checkpoint defect, showing that recognition of phosphorylated targets by Bub3 is required for checkpoint signaling. Our data provide the first detailed mechanistic insight into how phosphorylation promotes recruitment of checkpoint proteins to kinetochores. DOI:http://dx.doi.org/10.7554/eLife.01030.001.

PubMed: 24066227
DOI: 10.7554/ELIFE.01030

実験手法

X-RAY DIFFRACTION (1.95 Å)