We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Dimerization controls the lipid raft partitioning of uPAR/CD87 and regulates its biological functions.
- Authors
Orla Cunningham; Annapaola Andolfo; Maria Lisa Santovito; Lucia Iuzzolino; Francesco Blasi; Nicolai Sidenius
- Abstract
The urokinase-type plasminogen activator receptor (uPAR/CD87) is a glycosylphosphatidylinositol-anchored membrane protein with multiple functions in extracellular proteolysis, cell adhesion, cell migration and proliferation. We now report that cell surface uPAR dimerizes and that dimeric uPAR partitions preferentially to detergent-resistant lipid rafts. Dimerization of uPAR did not require raft partitioning as the lowering of membrane cholesterol failed to reduce dimerization and as a transmembrane uPAR chimera, which does not partition to lipid rafts, also dimerized efficiently. While uPA bound to uPAR independently of its membrane localization and dimerization status, uPA-induced uPAR cleavage was strongly accelerated in lipid rafts. In contrast to uPA, the binding of Vn occurred preferentially to raft- associated dimeric uPAR and was completely blocked by cholesterol depletion.
- Subjects
PLASMINOGEN; UROKINASE; PROTEOLYSIS; CELL adhesion
- Publication
EMBO Journal, 2003, Vol 22, Issue 22, p5994
- ISSN
0261-4189
- Publication type
Article
- DOI
10.1093/emboj/cdg588