Open AccessTetanus neurotoxin-mediated cleavage of cellubrevin impairs epithelial cell migration and integrin-dependent cell adhesion
Author(s) -
Véronique Proux-Gillardeaux,
Julie Gavard,
Théano Irinopoulou,
René-Marc Mège,
Thierry Galli
Publication year - 2005
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0409613102
Subject(s) - microbiology and biotechnology , endocytosis , laminin , fibronectin , cell adhesion , integrin , biology , endosome , exocytosis , cell migration , motility , cell , chemistry , extracellular matrix , intracellular , biochemistry , membrane
A role for endocytosis and exocytosis in cell migration has been proposed but not yet demonstrated. Here, we show that cellubrevin (Cb), an early endosomal v-SNARE, mediates trafficking in the lamellipod of migrating epithelial cells and partially colocalizes with markers of focal contacts. Expression of tetanus neurotoxin, which selectively cleaves Cb, significantly reduced the speed of migrating epithelial cells. Furthermore, expression of tetanus neurotoxin enhanced the adhesion of epithelial cells to collagen, laminin, fibronectin, and E-cadherin; altered spreading on collagen; and impaired the recycling of beta1 integrins. These results suggest that Cb-dependent membrane trafficking participates in cell motility through the regulation of cell adhesion.