Reference work entry
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...
- Abtahian F, Guerriero A, Sebzda E, MM L, Zhou R, Mocsai A, Myers EE, Huang B, Jackson DG, Ferrari VA, Tybulewicz V, Lowell CA, Lepore JJ, Koretzky GA, Kahn ML. Regulation of blood and lymphatic vascular separation by signaling proteins SLP-76 and Syk. Science. 2003;299:247–51.PubMedPubMedCentralGoogle Scholar
- Horn J, Wang X, Reichardt P, Stradal TE, Warnecke N, Simeoni L, Gunzer M, Yablonski D, Schraven B, Kliche S. Src homology 2-domain containing leukocyte-specific phosphoprotein of 76 kDa is mandatory for TCR-mediated inside-out signaling, but dispensable for CXCR4-mediated LFA-1 activation, adhesion, and migration of T cells. J Immunol. 2009;183:5756–67.PubMedPubMedCentralGoogle Scholar
- Zeng R, Cannon JL, Abraham RT, Way M, Billadeau DD, Bubeck-Wardenberg J, Burkhardt JK. SLP-76 coordinates Nck-dependent Wiskott-Aldrich syndrome protein recruitment with Vav-1/Cdc42-dependent Wiskott-Aldrich syndrome protein activation at the T cell-APC contact site. J Immunol. 2003;171:1360–8.PubMedPubMedCentralGoogle Scholar
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