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Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis
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Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis
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Journal Article
Molecular basis for unidirectional scaffold switching of human Plk4 in centriole biogenesis
2014
Overview
Plk4 regulates centriole duplication. Two centrosomal scaffold proteins, Cep192 and Cep152, are shown to interact with Plk4 in a temporally and spatially regulated manner, and structural analyses reveal that these interactions are mutually exclusive.
Polo-like kinase 4 (Plk4) is a key regulator of centriole duplication, an event critical for the maintenance of genomic integrity. We show that Plk4 relocalizes from the inner Cep192 ring to the outer Cep152 ring as newly recruited Cep152 assembles around the Cep192-encircled daughter centriole. Crystal-structure analyses revealed that Cep192- and Cep152-derived peptides bind the cryptic polo box (CPB) of Plk4 in opposite orientations and in a mutually exclusive manner. The Cep152 peptide bound to the CPB markedly better than did the Cep192 peptide and effectively 'snatched' the CPB away from a preformed CPB–Cep192 peptide complex. A cancer-associated Cep152 mutation impairing the Plk4 interaction induced defects in procentriole assembly and chromosome segregation. Thus, Plk4 is intricately regulated in time and space through ordered interactions with two distinct scaffolds, Cep192 and Cep152, and a failure in this process may lead to human cancer.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Cell Cycle Proteins - chemistry
/ Cell Cycle Proteins - genetics
/ Cell Cycle Proteins - metabolism
/ Chromosomal Proteins, Non-Histone - chemistry
/ Chromosomal Proteins, Non-Histone - metabolism
/ Genomics
/ Humans
/ Kinases
/ Mutation
/ Peptides
/ Protein Interaction Domains and Motifs
/ Protein Serine-Threonine Kinases - chemistry
/ Protein Serine-Threonine Kinases - metabolism
