| First Author | Mukherjee O | Year | 2012 |
| Journal | Biochim Biophys Acta | Volume | 1823 |
| Issue | 2 | Pages | 206-14 |
| PubMed ID | 22182704 | Mgi Jnum | J:180662 |
| Mgi Id | MGI:5306822 | Doi | 10.1016/j.bbamcr.2011.11.019 |
| Citation | Mukherjee O, et al. (2012) The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-alpha interaction. Biochim Biophys Acta 1823(2):206-14 |
| abstractText | The SH2-containing inositol 5'-phosphatase, SHIP1, negatively regulates signal transduction from the B cell antigen receptor (BCR). The mode of coupling between SHIP1 and the BCR has not been elucidated so far. In comparison to wild-type cells, B cells expressing a mutant IgD- or IgM-BCR containing a C-terminally truncated Ig-alpha respond to pervanadate stimulation with markedly reduced tyrosine phosphorylation of SHIP1 and augmented activation of protein kinase B. This indicates that SHIP1 is capable of interacting with the C-terminus of Ig-alpha. Employing a system of fluorescence resonance energy transfer in S2 cells, we can clearly demonstrate interaction between the SH2-domain of SHIP1 and Ig-alpha. Furthermore, a fluorescently labeled SH2-domain of SHIP1 translocates to the plasma membrane in an Ig-alpha-dependent manner. Interestingly, whereas the SHIP1 SH2-domain can be pulled-down with phospho-peptides corresponding to the immunoreceptor tyrosine-based activation motif (ITAM) of Ig-alpha from detergent lysates, no interaction between full-length SHIP1 and the phosphorylated Ig-alpha ITAM can be observed. Further studies show that the SH2-domain of SHIP1 can bind to the C-terminus of the SHIP1 molecule, most probably by inter- as well as intra-molecular means, and that this interaction regulates the association between different forms of SHIP1 and Ig-alpha. |
