5OID

Complex Trichoplax STIL-NTD:human CEP85 coiled coil domain 4

5OID の概要

• エントリーDOI: 10.2210/pdb5oid/pdb
• 分子名称: Putative uncharacterized protein, Centrosomal protein of 85 kDa (2 entities in total)
• 機能のキーワード: centrosomes, centriole, stil, cep85, protein binding
• 由来する生物種: Trichoplax adhaerens; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome : Q6P2H3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 51008.80

構造登録者

van Breugel, M. (登録日: 2017-07-18, 公開日: 2018-04-18, 最終更新日: 2024-11-20)

主引用文献

Liu, Y.,Gupta, G.D.,Barnabas, D.D.,Agircan, F.G.,Mehmood, S.,Wu, D.,Coyaud, E.,Johnson, C.M.,McLaughlin, S.H.,Andreeva, A.,Freund, S.M.V.,Robinson, C.V.,Cheung, S.W.T.,Raught, B.,Pelletier, L.,van Breugel, M.
Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly.
Nat Commun, 9:1731-1731, 2018

PubMed Abstract: Centrosomes are required for faithful chromosome segregation during mitosis. They are composed of a centriole pair that recruits and organizes the microtubule-nucleating pericentriolar material. Centriole duplication is tightly controlled in vivo and aberrations in this process are associated with several human diseases, including cancer and microcephaly. Although factors essential for centriole assembly, such as STIL and PLK4, have been identified, the underlying molecular mechanisms that drive this process are incompletely understood. Combining protein proximity mapping with high-resolution structural methods, we identify CEP85 as a centriole duplication factor that directly interacts with STIL through a highly conserved interaction interface involving a previously uncharacterised domain of STIL. Structure-guided mutational analyses in vivo demonstrate that this interaction is essential for efficient centriolar targeting of STIL, PLK4 activation and faithful daughter centriole assembly. Taken together, our results illuminate a molecular mechanism underpinning the spatiotemporal regulation of the early stages of centriole duplication.

PubMed: 29712910
DOI: 10.1038/s41467-018-04122-x

実験手法

X-RAY DIFFRACTION (4.6 Å)