2N19

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

Summary for 2N19

• Entry DOI: 10.2210/pdb2n19/pdb
• Related: 2N15
• NMR Information: BMRB: 25552
• Descriptor: Serine/threonine-protein kinase PLK4 (1 entity in total)
• Functional Keywords: transferase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole : O00444
• Total number of polymer chains: 1
• Total formula weight: 9629.83

Authors

Boehm, R.,Arquint, C.,Gabryjonczyk, A.,Imseng, S.,Sauer, E.,Hiller, S.,Nigg, E.,Maier, T. (deposition date: 2015-03-24, release date: 2015-08-12, Last modification date: 2024-05-15)

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

SOLUTION NMR