| First Author | Draber P | Year | 2011 |
| Journal | Mol Cell Biol | Volume | 31 |
| Issue | 22 | Pages | 4550-62 |
| PubMed ID | 21930792 | Mgi Jnum | J:178776 |
| Mgi Id | MGI:5300118 | Doi | 10.1128/MCB.05817-11 |
| Citation | Draber P, et al. (2011) SCIMP, a transmembrane adaptor protein involved in major histocompatibility complex class II signaling. Mol Cell Biol 31(22):4550-62 |
| abstractText | Formation of the immunological synapse between an antigen-presenting cell (APC) and a T cell leads to signal generation in both cells involved. In T cells, the lipid raft-associated transmembrane adaptor protein LAT plays a central role. Its phosphorylation is a crucial step in signal propagation, including the calcium response and mitogen-activated protein kinase activation, and largely depends on its association with the SLP76 adaptor protein. Here we report the discovery of a new palmitoylated transmembrane adaptor protein, termed SCIMP. SCIMP is expressed in B cells and other professional APCs and is localized in the immunological synapse due to its association with tetraspanin-enriched microdomains. In B cells, it is constitutively associated with Lyn kinase and becomes tyrosine phosphorylated after major histocompatibility complex type II (MHC-II) stimulation. When phosphorylated, SCIMP binds to the SLP65 adaptor protein and also to the inhibitory kinase Csk. While the association with SLP65 initiates the downstream signaling cascades, Csk binding functions as a negative regulatory loop. The results suggest that SCIMP is involved in signal transduction after MHC-II stimulation and therefore serves as a regulator of antigen presentation and other APC functions. |
