ArticleJournal of neuroscience research2008
Interactions between the L1 cell adhesion molecule and ezrin support traction-force generation and can be regulated by tyrosine phosphorylation.
Article in Journal of neuroscience research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Adhesion-clutch between DCC and netrin-1 mediates netrin-1-induced axonal haptotaxis.Frontiers in molecular neuroscience · 2024Article
- Proteomic analysis of six- and twelve-month hippocampus and cerebellum in a murine Down syndrome model.Neurobiology of aging · 2018Article
- Inhibition of N1-Src kinase by a specific SH3 peptide ligand reveals a role for N1-Src in neurite elongation by L1-CAM.Scientific reports · 2017Article
- Local Arp2/3-dependent actin assembly modulates applied traction force during apCAM adhesion site maturation.Molecular biology of the cell · 2017Article
- Review
- L1CAM/Neuroglian controls the axon-axon interactions establishing layered and lobular mushroom body architecture.The Journal of cell biology · 2015Article
- Interactome analysis reveals ezrin can adopt multiple conformational states.The Journal of biological chemistry · 2013Article
- Ubiquitination within the membrane-proximal ezrin-radixin-moesin (ERM)-binding region of the L1 cell adhesion molecule.Communicative & integrative biology · 2013Article
- Hepatoma polarization limits CD81 and hepatitis C virus dynamics.Cellular microbiology · 2013Article
- Rabex-5 protein regulates the endocytic trafficking pathway of ubiquitinated neural cell adhesion molecule L1.The Journal of biological chemistry · 2012Article
- Activation of ezrin/radixin/moesin mediates attractive growth cone guidance through regulation of growth cone actin and adhesion receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012Article
- Medulloblastoma exosome proteomics yield functional roles for extracellular vesicles.PloS one · 2012Article
- Adhesion molecule signalling: not always a sticky business.Nature reviews. Molecular cell biology · 2011Review
- Flotillin-mediated endocytic events dictate cell type-specific responses to semaphorin 3A.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Trafficking guidance receptors.Cold Spring Harbor perspectives in biology · 2010Review
- Nuclear factor-kappaB signaling and ezrin are essential for L1-mediated metastasis of colon cancer cells.Journal of cell science · 2010Article
- Role of the cytoplasmic domain of the L1 cell adhesion molecule in brain development.The Journal of comparative neurology · 2010Article
- Matrix metalloproteinase-dependent shedding of intercellular adhesion molecule-5 occurs with long-term potentiation.Neuroscience · 2010Article
- Cell adhesion molecules in context: CAM function depends on the neighborhood.Cell adhesion & migrationReview
Corrections and comments
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Authors and funding
10 authors at 1 institution in 1 country.
Funding
Abstract
An Ig superfamily cell-adhesion molecule, L1, forms an adhesion complex at the cell membrane containing both signaling molecules and cytoskeletal proteins. This complex mediates the transduction of extracellular signals and generates actin-mediated traction forces, both of which support axon outgrowth. The L1 cytoplasmic region binds ezrin, an adapter protein that interacts with the actin cytoskeleton. In this study, we analyzed L1-ezrin interactions in detail, assessed their role in generating traction forces by L1, and identified potential regulatory mechanisms controlling ezrin-L1 interactions. The FERM domain of ezrin binds to the juxtamembrane region of L1, demonstrated by yeast two-hybrid interaction traps and protein binding analyses in vitro. A lysine-to-leucine substitution in this domain of L1 (K1147L) shows reduced binding to the ezrin FERM domain. Additionally, in ND7 cells, the K1147L mutation inhibits retrograde movement of L1 on the cell surface that has been linked to the generation of the traction forces necessary for axon growth. A membrane-permeable peptide consisting of the juxtamembrane region of L1 that can disrupt endogenous L1-ezrin interactions inhibits neurite extension of cerebellar cells on L1 substrates. Moreover, the L1-ezrin interactions can be modulated by tyrosine phosphorylation of the L1 cytoplasmic region, namely, Y1151, possibly through Src-family kinases. Replacement of this tyrosine together with Y1176 with either aspartate or phenylalanine changes ezrin binding and alters colocalization with ezrin in ND7 cells. Collectively, these data suggest that L1-ezrin interactions mediated by the L1 juxtamembrane region are involved in traction-force generation and can be regulated by the phosphorylation of L1.
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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.