SHP1 binds p-CD22

Stable Identifier
Reaction [binding]
Homo sapiens
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The phosphorylated ITIMs of CD22 facilitates recruitment of the tyrosine phosphatase SHP1 (Src homology region 2 domain-containing phosphatase-1 also referred as PTPN6/Tyrosine-protein phosphatase non-receptor type 6), which down modulates BCR signalling (Doody et al. 1995). Activation of SHP1 regulates the strength of the BCR-induced Ca+2 signal. Regulation of Ca+2 signalling occurs both by dephosphorylation of intracellular SHP1 substrates which are important for triggering of Ca+2 signals (Adachi et al. 2001, Stebbins et al. 2003), as well as by a SHP1 dependent activation of the Ca+2 plasma membrane pump PMCA4 which controls termination of the signal (Muller et al. 2013, Ghosh et al. 2006).

Literature References
PubMed ID Title Journal Year
7618087 A role in B cell activation for CD22 and the protein tyrosine phosphatase SHP

Thomas, ML, Doody, GM, Matthews, RJ, Justement, LB, Lin, J, Delibrias, CC, Fearon, DT

Science 1995
9890995 Definition of the sites of interaction between the protein tyrosine phosphatase SHP-1 and CD22

Blasioli, J, Thomas, ML, Paust, S

J. Biol. Chem. 1999
23836650 CD22 ligand-binding and signaling domains reciprocally regulate B-cell Ca2+ signaling

Angermüller, S, Brandl, C, Maity, PC, Müller, J, Obermeier, I, Nitschke, L, Reth, M, Mrotzek, S, Wöhner, M

Proc. Natl. Acad. Sci. U.S.A. 2013
Orthologous Events
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