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

Merino-Trigo, A., Kerr, M. C., Houghton, F., Lindberg, A., Mitchell, C., Teasdale, R. D. and Gleeson, P. A. (2004) Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma imembrane following EGF stimulation. Journal of Cell Science, 117 26: 6413-6424. doi:10.1242/jcs.01561

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Author Merino-Trigo, A.
Kerr, M. C.
Houghton, F.
Lindberg, A.
Mitchell, C.
Teasdale, R. D.
Gleeson, P. A.
Title Sorting nexin 5 is localized to a subdomain of the early endosomes and is recruited to the plasma imembrane following EGF stimulation
Journal name Journal of Cell Science   Check publisher's open access policy
ISSN 0021-9533
Publication date 2004-01-01
Sub-type Article (original research)
DOI 10.1242/jcs.01561
Open Access Status File (Publisher version)
Volume 117
Issue 26
Start page 6413
End page 6424
Total pages 12
Place of publication Cambridge
Publisher Company of Biologists Ltd
Language eng
Subject C1
270200 Genetics
780105 Biological sciences
Abstract 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)P-2. 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)P-2, 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)P-2, 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.
Keyword Cell Biology
Sorting Nexins
Phox Homology Domain
Early Endosomes
Egf Signalling
Phosphoinositides
Pleckstrin-homology-domain
Px-domain
Phosphatidylinositol 3,4-bisphosphate
Fyve Finger
Lipid Products
Cell-surface
In-vivo
Protein
Receptor
Family
Q-Index Code C1

 
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Created: Wed, 15 Aug 2007, 14:45:00 EST