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A centrosome interactome provides insight into organelle assembly and reveals a non-duplication role for Plk4
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A centrosome interactome provides insight into organelle assembly and reveals a non-duplication role for Plk4
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Journal Article
A centrosome interactome provides insight into organelle assembly and reveals a non-duplication role for Plk4
2016
Overview
The centrosome is the major microtubule-organizing centre of many cells, best known for its role in mitotic spindle organization. How the proteins of the centrosome are accurately assembled to carry out its many functions remains poorly understood. The non-membrane-bound nature of the centrosome dictates that protein–protein interactions drive its assembly and functions. To investigate this massive macromolecular organelle, we generated a ‘domain-level’ centrosome interactome using direct protein–protein interaction data from a focused yeast two-hybrid screen. We then used biochemistry, cell biology and the model organism
Drosophila
to provide insight into the protein organization and kinase regulatory machinery required for centrosome assembly. Finally, we identified a novel role for Plk4, the master regulator of centriole duplication. We show that Plk4 phosphorylates Cep135 to properly position the essential centriole component Asterless. This interaction landscape affords a critical framework for research of normal and aberrant centrosomes.
The centrosome is a large intracellular structure that serves as the microtubule-organising center, but how it is accurately assembled is not known. Here the authors generate a ‘domain-level’ centrosome interactome and show that Plk4 positions the essential centriole component Asterless by phosphorylating Cep135.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/106
/ 14/1
/ 14/35
/ 64/24
/ 82/58
/ Animals
/ Biology
/ Cell Cycle Proteins - chemistry
/ Cell Cycle Proteins - metabolism
/ Drosophila melanogaster - metabolism
/ Drosophila Proteins - metabolism
/ Genomes
/ Humanities and Social Sciences
/ Insects
/ Kinases
/ Protein Serine-Threonine Kinases - metabolism
/ Proteins
/ Science
/ Yeasts
