ArticleBiochimica et biophysica acta2011
L-selectin transmembrane and cytoplasmic domains are monomeric in membranes.
Article in Biochimica et biophysica acta, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 13 citations in OpenAlex.
- SARS-CoV-2 membrane protein biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Article
- A cell-extrinsic ligand acquired by activated T cells in lymph node can bridge L-selectin and P-selectin.PloS one · 2018Article
- Screening for transmembrane association in divisome proteins using TOXGREEN, a high-throughput variant of the TOXCAT assay.Biochimica et biophysica acta · 2016Article
- Article
- Membrane-enabled dimerization of the intrinsically disordered cytoplasmic domain of ADAM10.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.Journal of molecular biology · 2013Article
- Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.PloS one · 2013Article
- Article
- Interaction of calmodulin with L-selectin at the membrane interface: implication on the regulation of L-selectin shedding.Journal of molecular biology · 2011Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A recombinant protein termed CLS, which corresponds to the C-terminal portion of human L-selectin and contains its entire transmembrane and cytoplasmic domains (residues Ser473-Arg542), has been produced and its oligomeric state in detergents characterized. CLS migrates in the SDS polyacrylamide gel at a pace that is typically expected from a complex twice of its molecular weight. Additional studies revealed, however, that this is due to residues in the cytoplasmic domain, as mutations in this region or its deletion significantly increased the electrophoretic rate of CLS. Analytical ultracentrifugation and fluorescence resonance energy transfer studies indicated that CLS reconstituted in dodecylphosphocholine detergent micelles is monomeric. When the transmembrane domain of L-selectin is inserted into the inner membrane of Escherichia coli as a part of a chimeric protein in the TOXCAT assay, little oligomerization of the chimeric protein is observed. Overall, these results suggest that transmembrane and cytoplasmic domains of L-selectin lack the propensity to self-associate in membranes, in contrast to the previously documented dimerization of the transmembrane domain of closely related P-selectin. This study will provide constraints for future investigations on the interaction of L-selectin and its associating proteins.
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