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First published online May 14, 2007
doi: 10.1242/10.1242/jcs.000653

Journal of Cell Science 120, 1818-1828 (2007)
Published by The Company of Biologists 2007
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Research Article

EGF induces macropinocytosis and SNX1-modulated recycling of E-cadherin

David M. Bryant1,*, Markus C. Kerr1, Luke A. Hammond1, Shannon R. Joseph1, Keith E. Mostov2, Rohan D. Teasdale1 and Jennifer L. Stow1,{ddagger}

1 Institute for Molecular Bioscience, The University of Queensland, Brisbane, QLD 4072, Australia
2 Department of Anatomy, University of California, San Francisco, CA 94143, USA

{ddagger} Author for correspondence (e-mail: j.stow{at}imb.uq.edu.au)

Accepted 5 April 2007

In epithelia, junction proteins are endocytosed for modulation of cell-cell adhesion and cell polarity. In response to growth factors, the cell-cell adhesion protein E-cadherin is internalized from the cell surface with degradation or recycling as potential fates. However, the cellular machinery involved in cadherin internalization and recycling remains controversial. Here we investigated EGF-induced E-cadherin internalization. EGF stimulation of MCF-7 cells resulted in Rac1-modulated macropinocytosis of the E-cadherin-catenin complex into endosomal compartments that colocalized with EEA1 and the sorting nexin, SNX1. Depletion of cellular SNX1 levels by siRNA resulted in increased intracellular accumulation and turnover of E-cadherin internalized from the cell surface in response to EGF. Moreover, SNX1 was also required for efficient recycling of internalized E-cadherin and re-establishment of epithelial adhesion. Together, these findings demonstrate a role for SNX1 in retrieval of E-cadherin from a degradative endosomal pathway and in membrane trafficking pathways that regulate E-cadherin recycling.

Key words: Sorting Nexin, EGF, Cadherin, Macropinocytosis, Recycling, Cell-cell adhesion




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