By C. A. Stewart, E. Vivier, M. Colonna (auth.), R.W. Compans, M.D. Cooper, T. Honjo, H. Koprowski, F. Melchers, M.B.A. Oldstone, S. Olsnes, M. Potter, P.K. Vogt, H. Wagner, Eric Vivier DVM, PhD., Marco Colonna M.D. (eds.)

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This is a simplified model based on current evidence from a number of studies that are described in the text respectively, whereas 2B4S has only one [85]. Upon engagement, the receptor is recruited to lipid rafts at the target cell interface in an actin-dependent manner, and tyrosine residues in the ITSM sequences are phosphorylated [173]. Phosphorylation of the ITSM sequences creates specific binding sites for SH2 domain-containing proteins, most notably signaling lymphocyte activation molecule (SLAM)-associated protein (SAP, also known as SH2D1A) [98, 143, 154].

In line with these studies, activation of Rac GTPases in NK cells with a pharmacological agent was recently shown to dramatically reorganize actin dynamics, increase target cell adhesion, and enhance cytotoxicity [109]. In addition to their roles in the cytolytic response, activated MAPKs can be transported to the nucleus to regulate transcription [36, 177]. A growing body of evidence demonstrates selective transcriptional regulation events resulting from the activation of specific MAPKs [138, 177].

4 A model of the patterns of recruitment of SHP-1 and SHP-2 to phosphorylated amino (N)- and carboxy (C)-terminal ITIMs of KIR and their inhibitory consequences. This model is based on biochemical and functional studies described in the text that examined mutant KIR in which the cytoplasmic ITIM tyrosines were selectively changed to phenylalanine, which cannot be phosphorylated 38 A. W. MacFarlane IV · K. S. Campbell SHP-1 and SHP-2 share 60% sequence identity and very high homology in secondary and tertiary structures.

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