SLP76 and SLP65: complex regulation of signalling in lymphocytes and beyond
- 1 January 2006
- journal article
- review article
- Published by Springer Science and Business Media LLC in Nature Reviews Immunology
- Vol. 6 (1), 67-78
- https://doi.org/10.1038/nri1750
Abstract
SLP76 and SLP65 are adaptor proteins that lack intrinsic enzymatic activity but contain multiple protein-binding domains. These proteins are essential for signalling downstream of integrins and receptors that contain immunoreceptor tyrosine-based activation motifs. The absence of these adaptor proteins profoundly affects various lineages in the haematopoietic compartment and severely compromises vascular development, highlighting their importance as regulators of signalling cascades. In this Review, we discuss the role of SLP76 and SLP65 in several signalling pathways in haematopoietic cells, with an emphasis on recent studies that provide insight into their mechanisms of action.Keywords
This publication has 101 references indexed in Scilit:
- Association of the Src homology 2 domain‐containing leukocyte phosphoprotein of 76 kD (SLP‐76) with the p85 subunit of phosphoinositide 3‐kinaseFEBS Letters, 2004
- Inactivation of c-Cbl Reverses Neonatal Lethality and T Cell Developmental Arrest of SLP-76–deficient MiceThe Journal of Experimental Medicine, 2004
- Binding Specificity of Multiprotein Signaling Complexes Is Determined by Both Cooperative Interactions and Affinity PreferencesBiochemistry, 2004
- SLP-76 Regulates Fcγ Receptor and Integrin Signaling in NeutrophilsImmunity, 2003
- Lipid RaftsCell, 2003
- Integrin α2β1 mediates outside-in regulation of platelet spreading on collagen through activation of Src kinases and PLCγ2The Journal of cell biology, 2003
- T cell receptor ligation induces the formation of dynamically regulated signaling assembliesThe Journal of cell biology, 2002
- Differential Requirement for LAT and SLP-76 in GPVI versus T Cell Receptor SignalingThe Journal of Experimental Medicine, 2002
- Differential Regulation of Activation-induced Tyrosine Phosphorylation and Recruitment of SLP-76 to Vav by Distinct Isoforms of the CD45 Protein-tyrosine PhosphatasePublished by Elsevier BV ,1996
- How receptor tyrosine kinases activate rasTrends in Biochemical Sciences, 1993