| First Author | Mikhailik A | Year | 2007 |
| Journal | Mol Cell | Volume | 27 |
| Issue | 3 | Pages | 486-97 |
| PubMed ID | 17679096 | Mgi Jnum | J:134815 |
| Mgi Id | MGI:3789834 | Doi | 10.1016/j.molcel.2007.06.015 |
| Citation | Mikhailik A, et al. (2007) A phosphatase activity of Sts-1 contributes to the suppression of TCR signaling. Mol Cell 27(3):486-97 |
| abstractText | Precise signaling by the T cell receptor (TCR) is crucial for a proper immune response. To ensure that T cells respond appropriately to antigenic stimuli, TCR signaling pathways are subject to multiple levels of regulation. Sts-1 negatively regulates signaling pathways downstream of the TCR by an unknown mechanism(s). Here, we demonstrate that Sts-1 is a phosphatase that can target the tyrosine kinase Zap-70 among other proteins. The X-ray structure of the Sts-1 C terminus reveals that it has homology to members of the phosphoglycerate mutase/acid phosphatase (PGM/AcP) family of enzymes, with residues known to be important for PGM/AcP catalytic activity conserved in nature and position in Sts-1. Point mutations that impair Sts-1 phosphatase activity in vitro also impair the ability of Sts-1 to regulate TCR signaling in T cells. These observations reveal a PGM/AcP-like enzyme activity involved in the control of antigen receptor signaling. |
