4YYP

Crystal structure of human PLK4-PB3 in complex with STIL-CC

Summary for 4YYP

• Entry DOI: 10.2210/pdb4yyp/pdb
• Related: 2n15
• NMR Information: BMRB: 26547
• Descriptor: Serine/threonine-protein kinase PLK4, SCL-interrupting locus protein, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: polo-box, complex, transferase
• Biological source: Homo sapiens (Human); More
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole: O00444; Cytoplasm, cytosol : Q15468
• Total number of polymer chains: 2
• Total formula weight: 13454.65

Authors

Imseng, S.,Arquint, C.,Gabryjonczyk, A.,Boehm, R.,Sauer, E.,Hiller, S.,Nigg, E.A.,Maier, T. (deposition date: 2015-03-24, release date: 2015-07-29, Last modification date: 2024-01-10)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.6 Å)