| First Author | Wang H | Year | 2003 |
| Journal | Nat Immunol | Volume | 4 |
| Issue | 4 | Pages | 366-74 |
| PubMed ID | 12652296 | Mgi Jnum | J:265617 |
| Mgi Id | MGI:6201899 | Doi | 10.1038/ni913 |
| Citation | Wang H, et al. (2003) SKAP-55 regulates integrin adhesion and formation of T cell-APC conjugates. Nat Immunol 4(4):366-74 |
| abstractText | Src kinase-associated phosphoprotein of 55 kDa (SKAP-55; encoded by SCAP1) is a T cell adaptor protein of unknown function that contains a pleckstrin homology and an SH3 domain. Here we show that SKAP-55 regulates integrin-mediated adhesion and conjugate formation between T cells and antigen-presenting cells (APCs). SKAP-55 enhances adhesion to fibronectin and intercellular adhesion molecule-1 (ICAM-1), colocalizes with actin at the T cell-APC synapse and promotes the clustering of lymphocyte-associated antigen-1 (LFA-1). Enhanced conjugation is comparable to that induced by adhesion and degranulation-promoting adaptor protein (ADAP), a binding partner of SKAP-55, and is abrogated by deletion of the SKAP-55 SH3 domain. Conjugate formation is accompanied by the translocation of SKAP-55 to membrane rafts, an event that is regulated by both LFA-1 and T cell receptor ligation. Our findings identify a mechanism by which SKAP-55 modulates T cell responses to antigen. |
