Caveolin-1 polarization in transmigrating endothelial cells requires binding to intermediate filaments

Santilman, V., Baran, J., Anand-Apte, B., Evans, R. M. and Parat, M. (2007) Caveolin-1 polarization in transmigrating endothelial cells requires binding to intermediate filaments. Angiogenesis, 10 4: 297-305. doi:10.1007/s10456-007-9083-z


Author Santilman, V.
Baran, J.
Anand-Apte, B.
Evans, R. M.
Parat, M.
Title Caveolin-1 polarization in transmigrating endothelial cells requires binding to intermediate filaments
Journal name Angiogenesis   Check publisher's open access policy
ISSN 0969-6970
Publication date 2007
Sub-type Article (original research)
DOI 10.1007/s10456-007-9083-z
Volume 10
Issue 4
Start page 297
End page 305
Total pages 9
Editor Griffioen, A.
Bischoff, J.
Place of publication Netherlands
Publisher Springer Netherlands
Collection year 2008
Subject C1
320602 Cell Physiology
730108 Cancer and related disorders
Abstract Caveolin-1 influences cell migration through multiple signaling pathways. In a previous report, we have shown that caveolin-1 is polarized in three-dimensional migrating endothelial cells (EC), and that caveolin-1 accumulation at the front of transmigrating cells requires the phosphorylatable Tyr14 residue of caveolin-1. Immuno-electron microscopy further indicated that caveolin-1 was distributed along cytoskeletal structures in the anterior of transmigrating EC [Parat MO, Anand-Apte B, Fox PL (Mol Biol Cell 14:3156–3168, 2003)]. In the present study, we investigate whether caveolin-1 interacts with intermediate filaments (IF) and whether this interaction is required for caveolin-1 polarization in transmigrating cells. The distribution of vimentin is polarized in cells traversing a filter pore and overlaps with the distribution of caveolin-1, which accumulates in the cell front. In vivo sprouting EC also exhibit an anterior polarization of these two proteins. Furthermore, caveolin-1 co-purifies with intermediate filaments, suggesting an interaction between caveolin-1 and IF. Vimentin-deficient SW13 cells exhibit a dramatically altered polarization of caveolin-1-GFP, which no longer accumulates in the protruding cell extension. In addition, the Tyr14 residue of caveolin-1 is required for co-purification of the protein with IF. Taken together, our results show that caveolin-1 Tyr14 is necessary for binding to intermediate filaments, which in turn is required for anterior polarization of caveolin-1 in transmigrating cells.
Keyword Endothelial cells
Sprouting
Angiogenesis
Migration
Cell motility
Vimentin
Q-Index Code C1
Q-Index Status Confirmed Code

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
2008 Higher Education Research Data Collection
School of Pharmacy Publications
 
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Created: Tue, 22 Apr 2008, 10:14:20 EST by Elizabeth Pyke on behalf of School of Pharmacy