ArticleJournal of molecular biology2013
FERM domain of moesin desorbs the basic-rich cytoplasmic domain of l-selectin from the anionic membrane surface.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 12 citations in OpenAlex.
- Observational
- Molecular mechanism for bidirectional regulation of CD44 for lipid raft affiliation by palmitoylations and PIP2.PLoS computational biology · 2020Article
- Serine Phosphorylation of L-Selectin Regulates ERM Binding, Clustering, and Monocyte Protrusion in Transendothelial Migration.Frontiers in immunology · 2019Article
- L-selectin: A Major Regulator of Leukocyte Adhesion, Migration and Signaling.Frontiers in immunology · 2019Review
- Sequential binding of ezrin and moesin to L-selectin regulates monocyte protrusive behaviour during transendothelial migration.Journal of cell science · 2018Article
- Molecular Dynamics of the Association of L-Selectin and FERM Regulated by PIP2.Biophysical journal · 2018Article
- Moesin expression by tumor cells is an unfavorable prognostic biomarker for oral cancer.BMC cancer · 2018Article
- The cytoplasmic tail of L-selectin interacts with the adaptor-protein complex AP-1 subunit μ1A via a novel basic binding motif.The Journal of biological chemistry · 2017Article
- Juxtamembrane contribution to transmembrane signaling.Biopolymers · 2015Review
- Basic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles.Journal of virology · 2015Article
- 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
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Moesin and calmodulin (CaM) jointly associate with the cytoplasmic domain of l-selectin in the cell to modulate the function and ectodomain shedding of l-selectin. Using fluorescence spectroscopy, we have examined the association of moesin FERM domain with the recombinant transmembrane and cytoplasmic domains of l-selectin (CLS) reconstituted in model phospholipid liposomes. The dissociation constant of moesin FERM domain to CLS in the phosphatidylcholine liposome is about 300nM. In contrast to disrupting the CaM association with CLS, inclusion of anionic phosphatidylserine lipids in the phosphatidylcholine liposome increased the apparent binding affinity of moesin FERM domain for CLS. Using the environmentally sensitive fluorescent probe attached to the cytoplasmic domain of CLS and the nitroxide quencher attached to the lipid bilayer, we showed that the association of moesin FERM domain induced the desorption of the basic-rich cytoplasmic domain of CLS from the anionic membrane surface, which enabled subsequent association of CaM to the cytoplasmic domain of CLS. These results have elucidated the molecular basis for the moesin/l-selectin/CaM ternary complex and suggested an important role of phospholipids in modulating l-selectin function and shedding.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.