4G7N

The Structure of the Plk4 Cryptic Polo Box Reveals Two Tandem Polo Boxes Required for Centriole Duplication

Summary for 4G7N

• Entry DOI: 10.2210/pdb4g7n/pdb
• Descriptor: Serine/threonine-protein kinase PLK4, SULFATE ION (3 entities in total)
• Functional Keywords: polo box, kinase targeting and regulation, asterless, centriole, transferase
• Biological source: Drosophila melanogaster (Fruit fly)
• Cellular location: Cytoplasm, cytoskeleton, centrosome, centriole: O97143
• Total number of polymer chains: 2
• Total formula weight: 51997.36

Authors

Slep, K.C.,Slevin, L.K. (deposition date: 2012-07-20, release date: 2012-10-10, Last modification date: 2024-10-09)

Primary citation

Slevin, L.K.,Nye, J.,Pinkerton, D.C.,Buster, D.W.,Rogers, G.C.,Slep, K.C.
The structure of the plk4 cryptic polo box reveals two tandem polo boxes required for centriole duplication.
Structure, 20:1905-1917, 2012

PubMed Abstract: Centrioles are key microtubule polarity determinants. Centriole duplication is tightly controlled to prevent cells from developing multipolar spindles, a situation that promotes chromosomal instability. A conserved component in the duplication pathway is Plk4, a polo kinase family member that localizes to centrioles in M/G1. To limit centriole duplication, Plk4 levels are controlled through trans-autophosphorylation that primes ubiquitination. In contrast to Plks 1-3, Plk4 possesses a unique central region called the "cryptic polo box." Here, we present the crystal structure of this region at 2.3 Å resolution. Surprisingly, the structure reveals two tandem homodimerized polo boxes, PB1-PB2, that form a unique winged architecture. The full PB1-PB2 cassette is required for binding the centriolar protein Asterless as well as robust centriole targeting. Thus, with its C-terminal polo box (PB3), Plk4 has a triple polo box architecture that facilitates oligomerization, targeting, and promotes trans-autophosphorylation, limiting centriole duplication to once per cell cycle.

PubMed: 23000383
DOI: 10.1016/j.str.2012.08.025

Experimental method

X-RAY DIFFRACTION (2.3 Å)