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First published online 23 November 2004
doi: 10.1242/jcs.01561

Journal of Cell Science 117, 6413-6424 (2004)
Published by The Company of Biologists 2004
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Research Article

Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma membrane following EGF stimulation

Ana Merino-Trigo1,*, Markus C. Kerr2, Fiona Houghton1, Anna Lindberg2, Christina Mitchell3, Rohan D. Teasdale2 and Paul A. Gleeson1,{ddagger}

1 The Russell Grimwade School of Biochemistry and Molecular Biology, The University of Melbourne, Melbourne, Victoria, 3010, Australia
2 Institute for Molecular Bioscience and Special Research Centre for Functional and Applied Genomics, University of Queensland, Brisbane, Queensland, 4072, Australia
3 Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, 3800, Australia

{ddagger} Author for correspondence (e-mail: pgleeson{at}unimelb.edu.au)

Accepted 23 September 2004

Sorting nexins are a large family of proteins that contain the phosphoinositide-binding Phox homology (PX) domain. A number of sorting nexins are known to bind to PtdIns(3)P, which mediates their localization to membranes of the endocytic pathway. We show here that sorting nexin 5 (SNX5) can be recruited to two distinct membrane compartments. In non-stimulated cells, the PX domain was independently targeted to endosomal structures and colocalized with full-length SNX5. The membrane binding of the PX domain was inhibited by the PI 3-kinase inhibitor, wortmannin. Although SNX5 colocalized with a fluid-phase marker and was found predominantly within a PtdIns(3)P-rich endosomal domain, very little colocalization was observed between SNX5 and the PtdIns(3)P-binding protein, EEA1. Using liposome-based binding assays, we have shown that the PX domain of SNX5 interacts not only with PtdIns(3)P but also with PtdIns(3,4)P2. In response to EGF stimulation, either the SNX5-PX domain or full-length SNX5 was rapidly recruited to the plasma membrane. The localization of SNX1, which does not bind PtdIns(3,4)P2, was unaffected by EGF signalling. Therefore, SNX5 is localized to a subdomain of the early endosome distinct from EEA1 and, following EGF stimulation and elevation of PtdIns(3,4)P2, is also transiently recruited to the plasma membrane. These results indicate that SNX5 may have functions not only associated with endosomal sorting but also with the phosphoinositide-signalling pathway.

Key words: Sorting nexins, Phox homology domain, Early endosomes, EGF signalling, Phosphoinositides


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