4E61

Crystal structure of the EB1-like motif of Bim1p

4E61 の概要

• エントリーDOI: 10.2210/pdb4e61/pdb
• 分子名称: Protein BIM1 (1 entity in total)
• 機能のキーワード: eb1-like motif, coiled-coil, spindle orientation, mitosis, kar9p, phosphorylation, mitotic spindle, microtubules, cell cycle
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm, cytoskeleton: P40013
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23616.32

構造登録者

Huels, D.,Storchova, Z.,Niessing, D. (登録日: 2012-03-15, 公開日: 2012-04-11, 最終更新日: 2024-04-03)

主引用文献

Huls, D.,Storchova, Z.,Niessing, D.
Post-translational Modifications Regulate Assembly of Early Spindle Orientation Complex in Yeast.
J.Biol.Chem., 287:16238-16245, 2012

PubMed Abstract: Mitosis begins with the tethering of chromosomes to the mitotic spindle and their orientation perpendicular to the axis of cell division. In budding yeast, mitotic spindle orientation and the subsequent chromosome segregation are two independent processes. Early spindle orientation is driven by the actin-bound myosin Myo2p, which interacts with the adapter Kar9p. The latter also binds to microtubule-associated Bim1p, thereby connecting both types of cytoskeleton. This study focuses on the interaction between Kar9p and Bim1p and its regulation. We solved the crystal structure of the previously reported Kar9p-binding motif of Bim1p and identified a second, novel Kar9p interaction domain. We further show that two independent post-translational modification events regulate their interaction. Whereas Kar9p sumoylation is required for efficient complex formation with Bim1p, Aurora B/Ipl1p-dependent phosphorylation of Bim1p down-regulates their interaction. The observed effects of these modifications allow us to propose a novel regulatory framework for the assembly and disassembly of the early spindle orientation complex.

PubMed: 22461628
DOI: 10.1074/jbc.M112.347872

実験手法

X-RAY DIFFRACTION (2.45 Å)