Dynamin 2 binds γ-tubulin and participates in centrosome cohesion

Heather M. Thompson, Hong Cao, Jing Chen, Ursula Euteneuer, Mark A. McNiven

Research output: Contribution to journalArticlepeer-review

135 Scopus citations


Dynamin 2 (Dyn2) is a large GTPase involved in vesicle formation and actin reorganization1-3. In this study, we report a novel role for Dyn2 as a component of the centrosome that is involved in centrosome cohesion. By light microscopy, Dyn2 localized aside centrin and colocalized with γ-tubulin at the centrosome; by immunoelectron microscopy, however, Dyn2 was detected in the pericentriolar material as well as on centrioles. Exogenously expressed green fluorescent protein (GFP)-tagged Dyn2 also localized to the centrosome, whereas glutathione S-transferase (GST)-tagged Dyn2 pulled down a protein complex(es) containing actin, α-tubulin and γ-tubulin from liver homogenate. Furthermore, gel overlay and immunoprecipitation indicated a direct interaction between γ-tubulin and a 219-amino-acid middle domain of Dyn2. Reduction of Dyn2 protein levels with small-interfering RNA (siRNA) resulted in centrosome splitting, whereas microtubule nucleation from centrosomes was not affected, suggesting a role for Dyn2 in centrosome cohesion. Finally, fluorescence recovery after photobleaching (FRAP) analysis of a GFP-tagged Dyn2 middle domain indicated that Dyn2 is a dynamic exchangeable component of the centrosome. These findings suggest a novel function for Dyn2 as a participant in centrosome cohesion.

Original languageEnglish (US)
Pages (from-to)335-342
Number of pages8
JournalNature Cell Biology
Issue number4
StatePublished - Apr 2004

ASJC Scopus subject areas

  • Cell Biology


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