The telling tail of L-selectin
- 26 October 2004
- journal article
- review article
- Published by Portland Press Ltd. in Biochemical Society Transactions
- Vol. 32 (6) , 1118-1121
- https://doi.org/10.1042/bst0321118
Abstract
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.Keywords
This publication has 16 references indexed in Scilit:
- Mutagenesis of the Ezrin-Radixin-Moesin Binding Domain of L-selectin Tail Affects Shedding, Microvillar Positioning, and Leukocyte TetheringJournal of Biological Chemistry, 2004
- The Interaction of Protein Kinase C Isozymes α, ι, and θ with the Cytoplasmic Domain of L-selectin Is Modulated by Phosphorylation of the ReceptorPublished by Elsevier ,2004
- Ezrin Is Essential for Epithelial Organization and Villus Morphogenesis in the Developing IntestineDevelopmental Cell, 2004
- Ezrin/radixin/moesin proteins and Rho GTPase signalling in leucocytesImmunology, 2004
- ERM proteins and merlin: integrators at the cell cortexNature Reviews Molecular Cell Biology, 2002
- Cytoplasmic anchorage of L-selectin controls leukocyte capture and rolling by increasing the mechanical stability of the selectin tetherThe Journal of cell biology, 2001
- Normal Development of Mice and Unimpaired Cell Adhesion/Cell Motility/Actin-based Cytoskeleton without Compensatory Up-regulation of Ezrin or Radixin in Moesin Gene KnockoutJournal of Biological Chemistry, 1999
- Adhesion Molecules in Inflammatory DiseasesDrugs, 1998
- The cytoplasmic domain of L-selectin interacts with cytoskeletal proteins via alpha-actinin: receptor positioning in microvilli does not require interaction with alpha-actinin.The Journal of cell biology, 1995
- Neutrophil Mac-1 and MEL-14 Adhesion Proteins Inversely Regulated by Chemotactic FactorsScience, 1989