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

Arquint C, Gabryjonczyk AM, Imseng S, Böhm R, Sauer E, Hiller S, Nigg EA, Maier T - Elife (2015)

Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Biozentrum, University of Basel, Basel, Switzerland.

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.

No MeSH data available.


Related in: MedlinePlus

Backbone dynamics of PLK4-PB3.Measurements of the 15N{1H}-NOE, which is sensitive to local dynamics on the ps–ns time scale. Backbone dynamics of PLK4-PB3 (dark blue, top) and PLK4-PB3 as part of the PLK4-PB3/STIL–CC complex (light blue, center) and their difference (black, bottom). Asterisks indicate residues that are unassigned in at least one of two forms.DOI:http://dx.doi.org/10.7554/eLife.07888.012
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fig5s2: Backbone dynamics of PLK4-PB3.Measurements of the 15N{1H}-NOE, which is sensitive to local dynamics on the ps–ns time scale. Backbone dynamics of PLK4-PB3 (dark blue, top) and PLK4-PB3 as part of the PLK4-PB3/STIL–CC complex (light blue, center) and their difference (black, bottom). Asterisks indicate residues that are unassigned in at least one of two forms.DOI:http://dx.doi.org/10.7554/eLife.07888.012


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

Arquint C, Gabryjonczyk AM, Imseng S, Böhm R, Sauer E, Hiller S, Nigg EA, Maier T - Elife (2015)

Backbone dynamics of PLK4-PB3.Measurements of the 15N{1H}-NOE, which is sensitive to local dynamics on the ps–ns time scale. Backbone dynamics of PLK4-PB3 (dark blue, top) and PLK4-PB3 as part of the PLK4-PB3/STIL–CC complex (light blue, center) and their difference (black, bottom). Asterisks indicate residues that are unassigned in at least one of two forms.DOI:http://dx.doi.org/10.7554/eLife.07888.012
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4530586&req=5

fig5s2: Backbone dynamics of PLK4-PB3.Measurements of the 15N{1H}-NOE, which is sensitive to local dynamics on the ps–ns time scale. Backbone dynamics of PLK4-PB3 (dark blue, top) and PLK4-PB3 as part of the PLK4-PB3/STIL–CC complex (light blue, center) and their difference (black, bottom). Asterisks indicate residues that are unassigned in at least one of two forms.DOI:http://dx.doi.org/10.7554/eLife.07888.012
Bottom Line: 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.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.

View Article: PubMed Central - PubMed

Affiliation: Biozentrum, University of Basel, Basel, Switzerland.

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.

No MeSH data available.


Related in: MedlinePlus