A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes

doi:10.1083/jcb.150.2.377

Published online 24 July 2000. doi:10.1083/jcb.150.2.377

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© The Rockefeller University Press, 0021-9525/2000//377 $5.00
The Journal of Cell Biology, Volume 150, Number 2, , 2000 377-390

Original Article

A Functional Link between Dynamin and the Actin Cytoskeleton at Podosomes

Gian-Carlo Ochoa^a^,b, Vladimir I. Slepnev^a^,b, Lynn Neff^b^,c, Niels Ringstad^a^,b, Kohji Takei^a^,b, Laurie Daniell^a^,b, Warren Kim^a^,b, Hong Cao^d, Mark McNiven^d, Roland Baron^b^,c, and Pietro De Camilli^a^,b

^a Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510
^b Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06510
^c Department of Orthopaedic Surgery, Yale University School of Medicine, New Haven, Connecticut 06510
^d Mayo Clinic, Rochester, Minnesota 55905
Department of Cell Biology, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06510.(203) 737-4436(203) 737-4465

pietro.decamilli{at}yale.edu

Cell transformation by Rous sarcoma virus results in a dramaticchange of adhesion structures with the substratum. Adhesionplaques are replaced by dot-like attachment sites called podosomes.Podosomes are also found constitutively in motile nontransformedcells such as leukocytes, macrophages, and osteoclasts. Theyare represented by columnar arrays of actin which are perpendicularto the substratum and contain tubular invaginations of the plasmamembrane. Given the similarity of these tubules to those generatedby dynamin around a variety of membrane templates, we investigatedwhether dynamin is present at podosomes. Immunoreactivitiesfor dynamin 2 and for the dynamin 2–binding protein endophilin2 (SH3P8) were detected at podosomes of transformed cells andosteoclasts. Furthermore, GFP wild-type dynamin 2aa was targetedto podosomes. As shown by fluorescence recovery after photobleaching,GFP-dynamin 2aa and GFP-actin had a very rapid and similar turnoverat podosomes. Expression of the GFP-dynamin 2aa^G273D abolishedpodosomes while GFP-dynamin^K44A was targeted to podosomes butdelayed actin turnover. These data demonstrate a functionallink between a member of the dynamin family and actin at attachmentsites between cells and the substratum.

Key Words: clathrin • endocytosis • actin patches • Src • osteoclast

Abbreviation used in this paper: FRAP, fluorescence recoveryafter photobleaching.

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