Centrioles resist forces applied on centrosomes during G2/M transition

• Published in: Biology of the cell Vol. 97; no. 6; pp. 425 - 434
• Main Authors: Abal, Miguel, Keryer, Guy, Bornens, Michel
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.06.2005
• Subjects: Antibodies, Monoclonal - chemistry; Cell Cycle; Cell Division; Centrioles - metabolism; Centrioles - ultrastructure; centrosome; Centrosome - metabolism; Centrosome - ultrastructure; dynein; Dyneins - metabolism; Eg5; G1 Phase; G2 Phase; Green Fluorescent Proteins - metabolism; HeLa Cells; Humans; Kinesin - metabolism; mAb GT335; Microscopy, Fluorescence; Microscopy, Video; Models, Biological; Molecular Motor Proteins; Peptides - chemistry; polyglutamylated tubulin; S Phase; Time Factors; Tubulin - chemistry
• ISSN: 0248-4900; 1768-322X
• DOI: 10.1042/BC20040112

Background information. Centrosome movements at the onset of mitosis result from a balance between the pulling and pushing forces mediated by microtubules. The structural stability of the centrosome core structure, the centriole pair, is correlated with a heavy polyglutamylation of centriole tubulin. Results. Using HeLa cells stably expressing centrin—green fluorescent protein as a centriole marker, we monitored the effect of microinjecting an anti‐(polyglutamylated tubulin) monoclonal antibody, GT335, in G1/S or G2 cells. In contrast with the slow effect of the monoclonal antibody GT335 during interphase, a dramatic and rapid centrosome fragmentation occurred in cells microinjected in G2 that was both Eg5‐ and dynein‐dependent. Inhibition of either one of these two motors significantly decreased the scattering of centrosome fragments, and inhibition of centrosome segregation by impairing microtubule dynamics abolished centrosome fragmentation. Conclusions. Our results demonstrate that the compact structure of the mitotic centrosome is capable of absorbing most of the pulling and pushing forces during G2/M transition and suggest that centrosomes could act as mechanosensors integrating tensions during cell division.