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Blood, 15 October 2006, Vol. 108, No. 8, pp. 2624-2631. Prepublished online as a Blood First Edition Paper on April 25, 2006; DOI 10.1182/blood-2005-12-007484. This Article Full Text (PDF) All Versions of this Article: blood-2005-12-007484v1 108/8/2624    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Gampel, A. Articles by Mellor, H. Search for Related Content PubMed PubMed Citation Articles by Gampel, A. Articles by Mellor, H. Related Collections Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 21, 2005 Accepted March 24, 2006 VEGF regulates the mobilisation of VEGFR-2/KDR from an intracellular endothelial storage compartment Alexandra Gampel, Lara Moss, Matt C Jones, Val Brunton, Jim C Norman, and Harry Mellor* Mammalian Cell Biology Laboratory, Department of Biochemistry, University of Bristol Beatson Institute Beatson Institute for Cancer Research, Cancer Research UK, Beatson Laboratories * Corresponding author; email: h.mellor{at}bristol.ac.uk. Endothelial cells respond to vascular endothelial growth factor (VEGF) to produce new blood vessels. This process of angiogenesis makes a critical contribution during embryogenesis and also in the response to ischemia in adult tissues. We have studied the intracellular trafficking of the major VEGF receptor; KDR (VEGFR-2). Unlike other related growth factor receptors, we find that a significant proportion of KDR is held in an endosomal storage pool within endothelial cells. We find that KDR can be delivered to the plasma membrane from this intracellular pool, and that VEGF stimulates this recycling to the cell surface. KDR recycling appears to be distinct from the previously characterised Rab4 and Rab11-dependent pathways, but instead, KDR+ recycling vesicles contain Src tyrosine kinase and VEGF-stimulated recycling requires Src activation. Taken together, these data show that intracellular trafficking of KDR is markedly different from other receptor tyrosine kinases, and suggest that the regulation of KDR trafficking by VEGF provides a novel mechanism for controlling the sensitivity of endothelial cells to pro-angiogenic signals. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: VEGF calls its receptors from the recycling compartment Yihai Cao Blood 2006 108: 2506-2507. [Full Text] [PDF] This article has been cited by other articles: A. Baba, K. Akagi, M. Takayanagi, J. G. Flanagan, T. Kobayashi, and M. Hattori Fyn Tyrosine Kinase Regulates the Surface Expression of Glycosylphosphatidylinositol-linked Ephrin via the Modulation of Sphingomyelin Metabolism J. Biol. Chem., April 3, 2009; 284(14): 9206 - 9214. [Abstract] [Full Text] [PDF] R. Silva, G. D'Amico, K. M. Hodivala-Dilke, and L. E. Reynolds Integrins: The Keys to Unlocking Angiogenesis Arterioscler Thromb Vasc Biol, October 1, 2008; 28(10): 1703 - 1713. [Abstract] [Full Text] [PDF] R. Rollason, V. Korolchuk, C. Hamilton, P. Schu, and G. Banting Clathrin-mediated endocytosis of a lipid-raft-associated protein is mediated through a dual tyrosine motif J. Cell Sci., November 1, 2007; 120(21): 3850 - 3858. [Abstract] [Full Text] [PDF] M. Garcia Blanes, M. Oubaha, Y. Rautureau, and J.-P. Gratton Phosphorylation of Tyrosine 801 of Vascular Endothelial Growth Factor Receptor-2 Is Necessary for Akt-dependent Endothelial Nitric-oxide Synthase Activation and Nitric Oxide Release from Endothelial Cells J. Biol. Chem., April 6, 2007; 282(14): 10660 - 10669. [Abstract] [Full Text] [PDF]

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