The interaction of IQGAP1 with the exocyst complex is required for tumor cell invasion downstream of Cdc42 and RhoA

Journal of Cell Biology - Tập 181 Số 6 - Trang 985-998 - 2008
Mika Sakurai‐Yageta1,2, Chiara Recchi1,2, Gaëlle Le Dez1,2, Jean‐Baptiste Sibarita1,2, Laurent Daviet3, Jacques Camonis1,4, Crislyn D’Souza‐Schorey5,6, Philippe Chavrier1,2
11Institut Curie, Centre de Recherche, Paris F-75248, France
22Centre National de la Recherche Scientifique, Unite Mixte Recherche 144, Paris F-75248, France
33Hybrigenics SA, Paris F-75014, France
44Institut National de la Santé et de la Recherche Médicale, Unite 528, Paris F-75248, France
55Department of Biological Sciences
66Walther Cancer Research Center, University of Notre Dame, Notre Dame, IN 46556

Tóm tắt

Invadopodia are actin-based membrane protrusions formed at contact sites between invasive tumor cells and the extracellular matrix with matrix proteolytic activity. Actin regulatory proteins participate in invadopodia formation, whereas matrix degradation requires metalloproteinases (MMPs) targeted to invadopodia. In this study, we show that the vesicle-tethering exocyst complex is required for matrix proteolysis and invasion of breast carcinoma cells. We demonstrate that the exocyst subunits Sec3 and Sec8 interact with the polarity protein IQGAP1 and that this interaction is triggered by active Cdc42 and RhoA, which are essential for matrix degradation. Interaction between IQGAP1 and the exocyst is necessary for invadopodia activity because enhancement of matrix degradation induced by the expression of IQGAP1 is lost upon deletion of the exocyst-binding site. We further show that the exocyst and IQGAP1 are required for the accumulation of cell surface membrane type 1 MMP at invadopodia. Based on these results, we propose that invadopodia function in tumor cells relies on the coordination of cytoskeletal assembly and exocytosis downstream of Rho guanosine triphosphatases.

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Thông tin
Thông tin xuất bản

Journal of Cell Biology

Tập 181 Số 6

985-998

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