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A more recent version of this article appeared on February 1, 2003
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Submitted on July 9, 2002
Revised on October 8, 2002
Accepted on October 28, 2002
1 Laboratoire de Biologie Moléculaire et Cellulaire UMR 5665 CNRS/ENS, INRA 913, Ecole Normale Supérieure de Lyon 46, allée d'Italie, 69007 Lyon, France
2 Laboratoire de Physique UMR 5672 CNRS - ENS Lyon, Ecole Normale Supérieure de Lyon 46, allée d'Italie, 69007 Lyon, France
* Corresponding author. E-mail address: fabard{at}biomail.ucsd.edu.
Podosomes, small actin based adhesion structures, differ from focal adhesions in two aspects: their core structure and their ability to organize into large patterns in osteoclasts. To address the mechanisms underlying these features, we imaged live pre-osteoclasts expressing GFP-actin during their differentiation. We observe that podosomes always form inside or close to podosome groups, which are surrounded by an actin cloud. Fluorescence recovery after photobleaching shows that actin turns over in individual podosomes on the contrary to cortactin, suggesting a continuous actin polymerization in the podosome core. The observation of podosome assemblies during osteoclast differentiation reveals that they evolve from simple clusters to rings that expand by the continuous formation of new podosomes at their outer ridge and inhibition of podosome formation inside the rings. This self-organization of podosomes into dynamic rings is the mechanism that drives podosomes at the periphery of the cell in large circular patterns. We show furthermore that an additional step of differentiation, requiring microtubules integrity, stabilizes the podosomes circles at the cell periphery to form the characteristic podosome belt pattern of mature osteoclasts. These results provide therefore a mechanism for the patterning of podosomes in osteoclasts and reveal a turnover of actin inside the podosome.
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