L-selectin is constitutively expressed on the surface of most leucocytes and is important for tethering and subsequent rolling of leucocytes on endothelial cells, facilitating their migration into secondary lymphoid organs (e.g. naive T cells) and sites of inflammation (e.g. neutrophils). Previous studies have shown that the 17-amino-acid L-selectin cytoplasmic tail is important for its function in cell adhesion and, hence, identifying binding partners will provide insight into how L-selectin is regulated in leucocytes. This review describes currently known binding partners of the L-selectin tail and how their associations affect L-selectin function.
© 2004 The Biochemical Society