SAP and EAT2 binds SLAMF6

Stable Identifier
R-HSA-5685603
Type
Reaction [binding]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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SAP and EAT2 binds SLAMF6
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The cytoplasmic tails of the SLAM-family receptors contain immunoreceptor tyrosine-based switch motifs (ITSMs). These ITSMs act as docking sites for the SH2 domain of SLAM-associated protein (SAP) and the related Ewing's sarcoma-associated transcript (EAT) 2 (Latour & Veillette 2004, Kageyama et al. 2012). Both SAP and EAT2 are expressed in natural killer (NK) cells, and their combined expression is essential for NK cells to kill abnormal hematopoietic cells. SAP mediates this effect by combining SLAM family receptors to the protein kinase FYN and exchange factor VAV, thereby promoting conjugate formation between NK cells and target cells. While EAT2 mediates its effects in NK cells by linking SLAM family receptors to phospholipase C-gamma, calcium fluxes amd ERK kinase (Perez-Quintero et al. 2014).
Literature References
PubMed ID Title Journal Year
15541655 The SAP family of adaptors in immune regulation

Latour, S, Veillette, A

Semin. Immunol. 2004
11489943 NTB-A [correction of GNTB-A], a novel SH2D1A-associated surface molecule contributing to the inability of natural killer cells to kill Epstein-Barr virus-infected B cells in X-linked lymphoproliferative disease

Bottino, C, Sivori, S, Moretta, A, Moretta, L, Biassoni, R, Falco, M, Augugliaro, R, Landi, E, Marcenaro, E, Notarangelo, LD, Parolini, S

J. Exp. Med. 2001
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Authored
Garapati, P V  (2015-03-27)
Reviewed
Barrow, AD  (2015-05-13)
Created
Garapati, P V  (2015-03-27)
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