@Article{Mukherjee:Weingarten:Padberg:The_SHIP_inter:2012,
  author =	 {Mukherjee, Oindrilla and Weingarten, Lars and Padberg, 
                  Inken and Pracht, Catrin and Sinha, Rileen and Hochdorfer, 
                  Thomas and Kuppig, Stephan and Backofen, Rolf and Reth, 
                  Michael and Huber, Michael},
  title =	 {The {SH2}-domain of {SHIP1} interacts with the {SHIP1} 
                  {C}-terminus: {Impact} on {SHIP1}/{Ig}-alpha interaction},
  journal =	 {Biochim Biophys Acta},
  year =	 {2012},
  volume =	 {1823},
  number =	 {2},
  pages =	 {206-14},
  user =	 {arichter},
  pmid =	 {22182704},
  doi = 	 {10.1016/j.bbamcr.2011.11.019},
  issn = 	 {0006-3002},
  issn =         {0167-4889},
  abstract =	 {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.}
}