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

被引：112

作者：

Arquint, Christian ^{[1
]}

Gabryjonczyk, Anna-Maria ^{[1
]}

Imseng, Stefan ^{[1
]}

Boehm, Raphael ^{[1
]}

Sauer, Evelyn ^{[1
]}

Hiller, Sebastian ^{[1
]}

Nigg, Erich A. ^{[1
]}

Maier, Timm ^{[1
]}

机构：

[1] Univ Basel, Biozentrum, Basel, Switzerland

来源：

ELIFE | 2015年 / 4卷

关键词：

CENTROSOME DUPLICATION; SINGLE PROCENTRIOLE; STRUCTURAL BASIS; 9-FOLD SYMMETRY; KINASE-ACTIVITY; MOLECULAR-BASIS; PROTEIN; DOMAIN; RECRUITMENT; BIOGENESIS;

D O I：

10.7554/eLife.07888

中图分类号：

Q [生物科学];

学科分类号：

090105 [作物生产系统与生态工程];

摘要：

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.

引用

页数：22

共 94 条

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