ArticleThe Journal of biological chemistry2012
Structural insights into calmodulin-regulated L-selectin ectodomain shedding.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
- The Structural Basis of the Farnesylated and Methylated KRas4B Interaction with Calmodulin.Structure (London, England : 1993) · 2019Article
- Structure and function insights garnered from in silico modeling of the thrombospondin type-1 domain-containing 7A antigen.Proteins · 2019Article
- L-selectin: A Major Regulator of Leukocyte Adhesion, Migration and Signaling.Frontiers in immunology · 2019Review
- Molecular Dynamics of the Association of L-Selectin and FERM Regulated by PIP2.Biophysical journal · 2018Article
- A head-to-tail view of L-selectin and its impact on neutrophil behaviour.Cell and tissue research · 2018Review
- Over-expression of a human CD62L ecto-domain and a potential role of RNA pseudoknot structures in recombinant protein expression.Protein expression and purification · 2017Article
- The Recognition of Calmodulin to the Target Sequence of Calcineurin-A Novel Binding Mode.Molecules (Basel, Switzerland) · 2017Article
- Thrombin-derived host defence peptide modulates neutrophil rolling and migration in vitro and functional response in vivo.Scientific reports · 2017Article
- Juxtamembrane contribution to transmembrane signaling.Biopolymers · 2015Review
- Gap junction regulation by calmodulin.FEBS letters · 2014Review
- A disintegrin and metalloprotease (ADAM) 10 and ADAM17 are major sheddases of T cell immunoglobulin and mucin domain 3 (Tim-3).The Journal of biological chemistry · 2013Article
- Comparing the calcium binding abilities of two soybean calmodulins: towards understanding the divergent nature of plant calmodulins.The Plant cell · 2013Article
- Calmodulin adopts an extended conformation when interacting with L-selectin in membranes.PloS one · 2013Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The L-selectin glycoprotein receptor mediates the initial steps of leukocyte migration into secondary lymphoid organs and sites of inflammation. Following cell activation through the engagement of G-protein-coupled receptors or immunoreceptors, the extracellular domains of L-selectin are rapidly shed, a process negatively controlled via the binding of the ubiquitous eukaryotic calcium-binding protein calmodulin to the cytoplasmic tail of L-selectin. Here we present the solution structure of calcium-calmodulin bound to a peptide encompassing the cytoplasmic tail and part of the transmembrane domain of L-selectin. The structure and accompanying biophysical study highlight the importance of both calcium and the transmembrane segment of L-selectin in the interaction between these two proteins, suggesting that by binding this region, calmodulin regulates in an "inside-out" fashion the ectodomain shedding of the receptor. Our structure provides the first molecular insight into the emerging new role for calmodulin as a transmembrane signaling partner.
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Registered trials
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.