Journal
CELLULAR SIGNALLING
Volume 26, Issue 7, Pages 1489-1499Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2014.03.012
Keywords
Proteoglycan; Integrin; Talin; Cell adhesion
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Funding
- Fundacio Bosch i Gimpera, Universitat de Barcelona [FBG300412]
- predoctoral fellowship from Fundacio Bosch i Gimpera [FBG300412]
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Syndecans are cell membrane proteoglycans that can modulate the activity and dynamics of some growth factor receptors and integrins. Here, we show the down-regulation of integrin lymphocyte function-associated antigen-1 (LFA-1) and inhibition of adhesion of Jurkat T cells transfected with syndecan-2. The PDZ-binding domain in the cytoplasmic region of syndecan-2 was necessary to block the LFA-1 high-affinity conformation, and to reduce cellular adhesion. A second cytoplasmic motif comprising tyrosines 179 and 191, and serines 187 and 188 contributed also to reduce LFA-1 function and cellular adhesion. Inhibition of the LFA-1 high-affinity conformation by syndecan-2 was independent of the expression of the talin head domain and RhoA, Rac1 and Cdc42 GTPases. These results demonstrate the importance of PDZ-binding domain of syndecan-2 for controlling LFA-1 affinity and cell adhesion. (C) 2014 Elsevier Inc. All rights reserved.
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