2N19

STIL binding to the Polo-box domain 3 of PLK4 regulates centriole duplication

2N19 の概要

• エントリーDOI: 10.2210/pdb2n19/pdb
• 関連するPDBエントリー: 2N15
• NMR情報: BMRB: 25552
• 分子名称: Serine/threonine-protein kinase PLK4 (1 entity in total)
• 機能のキーワード: transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O00444
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9629.83

構造登録者

Boehm, R.,Arquint, C.,Gabryjonczyk, A.,Imseng, S.,Sauer, E.,Hiller, S.,Nigg, E.,Maier, T. (登録日: 2015-03-24, 公開日: 2015-08-12, 最終更新日: 2024-05-15)

主引用文献

Arquint, C.,Gabryjonczyk, A.M.,Imseng, S.,Bohm, R.,Sauer, E.,Hiller, S.,Nigg, E.A.,Maier, T.
STIL binding to Polo-box 3 of PLK4 regulates centriole duplication.
Elife, 4:-, 2015

PubMed Abstract: Polo-like kinases (PLK) are eukaryotic regulators of cell cycle progression, mitosis and cytokinesis; PLK4 is a master regulator of centriole duplication. Here, we demonstrate that the SCL/TAL1 interrupting locus (STIL) protein interacts via its coiled-coil region (STIL-CC) with PLK4 in vivo. STIL-CC is the first identified interaction partner of Polo-box 3 (PB3) of PLK4 and also uses a secondary interaction site in the PLK4 L1 region. Structure determination of free PLK4-PB3 and its STIL-CC complex via NMR and crystallography reveals a novel mode of Polo-box-peptide interaction mimicking coiled-coil formation. In vivo analysis of structure-guided STIL mutants reveals distinct binding modes to PLK4-PB3 and L1, as well as interplay of STIL oligomerization with PLK4 binding. We suggest that the STIL-CC/PLK4 interaction mediates PLK4 activation as well as stabilization of centriolar PLK4 and plays a key role in centriole duplication.

PubMed: 26188084
DOI: 10.7554/eLife.07888

実験手法

SOLUTION NMR