Cep152 acts as a scaffold for recruitment of Plk4 and CPAP to the centrosome

Both gain and loss of function studies have identified the Polo-like kinase Plk4/Sak as a crucial regulator of centriole biogenesis, but the mechanisms governing centrosome duplication are incompletely understood. In this study, we show that the pericentriolar material protein, Cep152, interacts wit...

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Published inThe Journal of cell biology Vol. 191; no. 4; pp. 731 - 739
Main Authors Cizmecioglu, Onur, Arnold, Marc, Bahtz, Ramona, Settele, Florian, Ehret, Lena, Haselmann-Weiss, Uta, Antony, Claude, Hoffmann, Ingrid
Format Journal Article
LanguageEnglish
Published United States The Rockefeller University Press 15.11.2010
Rockefeller University Press
Subjects
Animal cells
Animals
Antibodies
Biosynthesis
Cell cycle
Cell Cycle - physiology
Cell Cycle Proteins - genetics
Cell Cycle Proteins - metabolism
Cell division
Cell Line
Cell lines
Cellular biology
Centrioles
Centrosome - metabolism
Centrosomes
Fluorescence Recovery After Photobleaching
Gene expression
HeLa cells
Humans
Kinases
Microtubule-Associated Proteins - genetics
Microtubule-Associated Proteins - metabolism
Protein Binding
Protein-Serine-Threonine Kinases - genetics
Protein-Serine-Threonine Kinases - metabolism
Proteins
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
RNA, Small Interfering
Small interfering RNA
Somatic cells
Spindle Apparatus - metabolism
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Summary:Both gain and loss of function studies have identified the Polo-like kinase Plk4/Sak as a crucial regulator of centriole biogenesis, but the mechanisms governing centrosome duplication are incompletely understood. In this study, we show that the pericentriolar material protein, Cep152, interacts with the distinctive cryptic Polo-box of Plk4 via its N-terminal domain and is required for Plk4-induced centriole overduplication. Reduction of endogenous Cep152 levels results in a failure in centriole duplication, loss of centrioles, and formation of monopolar mitotic spindles. Interfering with Cep152 function prevents recruitment of Plk4 to the centrosome and promotes loss of CPAP, a protein required for the control of centriole length in Plk4-regulated centriole biogenesis. Our results suggest that Cep152 recruits Plk4 and CPAP to the centrosome to ensure a faithful centrosome duplication process.
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O. Cizmecioglu and M. Arnold contributed equally to this paper.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.201007107