The SH2-domain of SHIP1 interacts with the SHIP1 C-terminus: Impact on SHIP1/Ig-α interaction
| Autor: | Michael Huber, Stephan Kuppig, Inken Padberg, Catrin Pracht, Thomas Hochdörfer, Rolf Backofen, Rileen Sinha, Lars Weingarten, Oindrilla Mukherjee, Michael Reth |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Interaction
Recombinant Fusion Proteins Syk Protein tyrosine phosphatase Immunoglobulin alpha-Chains SH2 domain Receptor tyrosine kinase src Homology Domains Mice chemistry.chemical_compound Tumor Cells Cultured Animals Tyrosine Molecular Biology B-Lymphocytes biology Cell Membrane Inositol Polyphosphate 5-Phosphatases Tyrosine phosphorylation Cell Biology Phosphoric Monoester Hydrolases Cell biology Biochemistry chemistry Phosphatidylinositol-3 4 5-Trisphosphate 5-Phosphatases biology.protein Phosphorylation Signal transduction BCR/SHIP1/Syk/tyrosine phosphorylation Dimerization |
| Zdroj: | Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823(2):206-214 |
| ISSN: | 0167-4889 |
| DOI: | 10.1016/j.bbamcr.2011.11.019 |
| Popis: | 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-α 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-α. Employing a system of fluorescence resonance energy transfer in S2 cells, we can clearly demonstrate interaction between the SH2-domain of SHIP1 and Ig-α. Furthermore, a fluorescently labeled SH2-domain of SHIP1 translocates to the plasma membrane in an Ig-α-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-α from detergent lysates, no interaction between full-length SHIP1 and the phosphorylated Ig-α 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-α. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect