ArticleThe Journal of biological chemistry2008
Kinetic analysis of L1 homophilic interaction: role of the first four immunoglobulin domains and implications on binding mechanism.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
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Who cites it
26 citing papers in PubMed, 1 synthesis or guideline pooled it.
- L1 Cell Adhesion Molecule in Cancer, a Systematic Review on Domain-Specific Functions.International journal of molecular sciences · 2019Pooled it
- Development of Antibody-Drug Conjugates Targeting L1CAM to Treat Metastatic Cancer.Molecular cancer therapeutics · 2026Article
- Structural insights into the contactin 1 - neurofascin 155 adhesion complex.Nature communications · 2022Article
- Article
- A conserved Neurite Outgrowth and Guidance motif with biomimetic potential in neuronal Cell Adhesion Molecules.Computational and structural biotechnology journal · 2021Article
- Different Shades of L1CAM in the Pathophysiology of Cancer Stem Cells.Journal of clinical medicine · 2020Review
- Investigating LGALS3BP/90 K glycoprotein in the cerebrospinal fluid of patients with neurological diseases.Scientific reports · 2020Article
- EpCAM homo-oligomerization is not the basis for its role in cell-cell adhesion.Scientific reports · 2018Article
- Article
- ACAM, a novel member of the neural IgCAM family, mediates anterior neural tube closure in a primitive chordate.Developmental biology · 2016Article
- Article
- Neural cell adhesion molecule NrCAM regulates Semaphorin 3F-induced dendritic spine remodeling.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Mitogen-activated protein kinase modulates ethanol inhibition of cell adhesion mediated by the L1 neural cell adhesion molecule.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Homophilic interaction of the L1 family of cell adhesion molecules.Experimental & molecular medicine · 2012Review
- Assessment of selective toxicity of insect cell expressed recombinant A1-GMCSF protein toward GMCSF receptor bearing tumor cells.Research in pharmaceutical sciences · 2012Article
- A chimeric antibody to L1 cell adhesion molecule shows therapeutic effect in an intrahepatic cholangiocarcinoma model.Experimental & molecular medicine · 2012Article
- Article
- Two alcohol binding residues interact across a domain interface of the L1 neural cell adhesion molecule and regulate cell adhesion.The Journal of biological chemistry · 2011Article
- Full-length L1CAM and not its Δ2Δ27 splice variant promotes metastasis through induction of gelatinase expression.PloS one · 2011Article
- Homophilic adhesion mechanism of neurofascin, a member of the L1 family of neural cell adhesion molecules.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
L1 is a cell adhesion molecule of the immunoglobulin (Ig) superfamily, critical for central nervous system development, and involved in several neuronal biological events. It is a type I membrane glycoprotein. The L1 ectodomain, composed of six Ig-like and five fibronectin (Fn) type-III domains, is involved in homophilic binding. Here, co-immunoprecipitation studies between recombinant truncated forms of human L1 expressed and purified from insect Spodoptera frugiperda Sf9 cells, and endogenous full-length L1 from human NT2N neurons, showed that the L1 ectodomain (L1/ECD) and L1/Ig1-4 interacted homophilically in trans, contrary to mutants L1/Ig1-3 and L1/Ig2-Fn5. All mutants were correctly folded as evaluated by combination of far-UV CD and fluorescence spectroscopy. Surface plasmon resonance analysis showed comparable dissociation constants of 116 +/- 2 and 130 +/- 6 nm for L1/ECD-L1/ECD and L1/ECD-L1/Ig1-4, respectively, whereas deletion mutants for Ig1 or Ig4 did not interact. Accordingly, in vivo, Sf9 cells stably expressing L1 were found to adhere only to L1/ECD- and L1/Ig1-4-coated surfaces. Furthermore, only these mutants bound to HEK293 cells overexpressing L1 at the cell surface. Enhancement of neurite outgrowth, which is the consequence of signaling events caused by L1 homophilic binding, was comparable between L1/ECD and L1/Ig1-4. Altogether, these results showed that domains Ig1 to Ig4 are necessary and sufficient for L1 homophilic binding in trans, and that the rest of the molecule does not contribute to the affinity under the conditions of the current study. Furthermore, they are compatible with a cooperative interaction between modules Ig1-Ig4 in a horseshoe conformation.
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