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Vol. 14, Issue 3, 1074-1084, March 2003
*Department of Cell Biology and Oncology, Istituto di
Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, S. Maria Imbaro (Chieti), 66030 Italy; The degradation of extracellular matrix (ECM) by matrix
metalloproteases is crucial in physiological and pathological
cell invasion alike. Degradation occurs at specific sites where
invasive cells make contact with the ECM via specialized plasma
membrane protrusions termed invadopodia. Herein, we show that the
dynamin 2 (Dyn2), a GTPase implicated in the control of actin-driven
cytoskeletal remodeling events and membrane transport, is necessary for
focalized matrix degradation at invadopodia. Dynamin was inhibited by
using two approaches: 1) expression of dominant negative
GTPase-impaired or proline-rich domain-deleted Dyn2 mutants; and 2)
inhibition of the dynamin regulator calcineurin by cyclosporin A. In
both cases, the number and extension of ECM degradation foci were
drastically reduced. To understand the site and mechanism of dynamin
action, the cellular structures devoted to ECM degradation were
analyzed by correlative confocal light-electron microscopy. Invadopodia were found to be organized into a previously undescribed
ECM-degradation structure consisting of a large invagination of the
ventral plasma membrane surface in close spatial relationship with the
Golgi complex. Dyn2 seemed to be concentrated at invadopodia.
Endocrine
Unit, Department of Internal Medicine, Ospedale Civile "Renzetti",
Lanciano (Chieti), 66034 Italy; and Department
of Biochemistry and Molecular Biology, Center for Basic Research in
Digestive Diseases, Mayo Clinic, Rochester, Minnesota 55905
Online version of this article contains video material for some
figures. Online version is available at www.molbiolcell.org.
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