Historical Background
SLP-76 was first identified as a substrate of the protein tyrosine kinases that are activated by T-cell antigen receptors (TCRs) (Jackman et al. 1995). SLP-76, which functions as a signal transducer downstream of TCRs, is an adaptor protein that has three modular domains: an amino (N)-terminal acidic domain with three tyrosine (Y) phosphorylation motifs, a central proline-rich region, and a carboxy (C)-terminal SH2 domain (Fig. 1). Two other proteins, B-cell linker protein (BLNK/BASH/BCA/SLP-65) and cytokine-dependent hematopoietic cell linker (CLNK/MIST), constitute a family of SLP-76 adaptors, each expressed exclusively in hematopoietic cells. The three family members have only a moderate degree of sequence homology, but share a characteristic domain structure (Fig. 1). These SLP-76 family members are critical for nucleation of large signaling...
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Lee, J.R. (2018). SLP-76. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_474
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DOI: https://doi.org/10.1007/978-3-319-67199-4_474
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