| First Author | Sekine Y | Year | 2005 |
| Journal | J Biol Chem | Volume | 280 |
| Issue | 9 | Pages | 8188-96 |
| PubMed ID | 15611091 | Mgi Jnum | J:97253 |
| Mgi Id | MGI:3575049 | Doi | 10.1074/jbc.M411692200 |
| Citation | Sekine Y, et al. (2005) Physical and functional interactions between STAP-2/BKS and STAT5. J Biol Chem 280(9):8188-96 |
| abstractText | Signal-transducing adaptor protein family of proteins (STAPs), which currently contains two members, are proposed to be adaptor molecules because of their pleckstrin homology (PH) and Src-homology 2 (SH2)-like domains. STAP-1 has been shown to interact with STAT5 and the tyrosine kinase Tec. With regard to STAP-2/BKS functions, immunoprecipitation experiments and intracellular stainings revealed STAP-2/BKS binds STAT5 in several types of cells. Mutational studies revealed that the PH- and SH2-like domains of STAP-2/BKS interacted with the C-terminal region of STAT5. STAP-2/BKS and STAT5 were found to constitutively co-localize in the cytoplasm of resting cells, but STAP-2/BKS was found to dissociate upon STAT5 phosphorylation, suggesting a role in regulating signaling of STAT5. The physiological role of these interactions is not fully understood, but in studies of overexpression of STAP-2/BKS, cytokine-induced tyrosine phosphorylation and transcriptional activation of STAT5 was diminished. In addition, thymocytes from STAP-2/BKS-deficient mice showed the enhanced interleukin-2-dependent cell growth. Taken together, STAP-2/BKS is an additional modulator of STAT5-mediated signaling. |
