Several extracellular domains of the neural cell adhesion molecule L1 are involved in homophilic interactions

J. Holm, F. Appel, Melitta Camartin

Research output: Contribution to journalArticle

24 Citations (Scopus)

Abstract

The neural cell adhesion molecule L1 is a multidomain protein that plays important roles in cell adhesion, migration, and neurite outgrowth. It can interact with itself by a self‐binding, i.e., homophilic adhesion mechanism (Kadmon et al.: J Cell Biol 110: 193‐208, 1990a). To determine the domains of L1 involved in homophilic binding, we have generated protein fragments of Ll in a prokaryotic and a eukaryotic expression system and used these covalently coupled to fluorescent microspheres to quantify aggregation between them by cytofluorometric analysis. Protein fragments containing the first and second Ig‐like domains and the third fibronectin type III homologous repeat showed avid self‐binding. Ig‐like domains III and IV also showed some self‐binding, whereas Ig‐like domains V and VI and fibronectin type III homologous repeats 1 and 2 as well as 4 and 5 were less or not active. Binding between different domains was also observed: fibronectin type III homologous repeats 4 and 5 interacted with Ig‐like domains I and II, and fibronectin type III homologous repeats 3‐5 interacted with all Ig‐like domains. These results were confirmed by experiments testing the binding of fragment‐conjugated microspheres to substrate‐coated L1 or to cell surface‐expressed L1 on cultured neurons. Binding of L1 to itself was interfered with by all protein fragments tested, suggesting that also less avidly binding domains of L1 contribute to homophilic binding. These observations indicate prominent functional roles of both Ig‐like domains and fibronectin type III homologous repeats in homophilic binding of L1. © 1995 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)9-20
Number of pages12
JournalJournal of Neuroscience Research
Volume42
Issue number1
DOIs
StatePublished - Jan 1 1995
Externally publishedYes

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Neural Cell Adhesion Molecule L1
Fibronectins
Microspheres
Proteins
Cell Adhesion
Cell Movement
Neurons

All Science Journal Classification (ASJC) codes

  • Cellular and Molecular Neuroscience

Cite this

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title = "Several extracellular domains of the neural cell adhesion molecule L1 are involved in homophilic interactions",
abstract = "The neural cell adhesion molecule L1 is a multidomain protein that plays important roles in cell adhesion, migration, and neurite outgrowth. It can interact with itself by a self‐binding, i.e., homophilic adhesion mechanism (Kadmon et al.: J Cell Biol 110: 193‐208, 1990a). To determine the domains of L1 involved in homophilic binding, we have generated protein fragments of Ll in a prokaryotic and a eukaryotic expression system and used these covalently coupled to fluorescent microspheres to quantify aggregation between them by cytofluorometric analysis. Protein fragments containing the first and second Ig‐like domains and the third fibronectin type III homologous repeat showed avid self‐binding. Ig‐like domains III and IV also showed some self‐binding, whereas Ig‐like domains V and VI and fibronectin type III homologous repeats 1 and 2 as well as 4 and 5 were less or not active. Binding between different domains was also observed: fibronectin type III homologous repeats 4 and 5 interacted with Ig‐like domains I and II, and fibronectin type III homologous repeats 3‐5 interacted with all Ig‐like domains. These results were confirmed by experiments testing the binding of fragment‐conjugated microspheres to substrate‐coated L1 or to cell surface‐expressed L1 on cultured neurons. Binding of L1 to itself was interfered with by all protein fragments tested, suggesting that also less avidly binding domains of L1 contribute to homophilic binding. These observations indicate prominent functional roles of both Ig‐like domains and fibronectin type III homologous repeats in homophilic binding of L1. {\circledC} 1995 Wiley‐Liss, Inc.",
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Several extracellular domains of the neural cell adhesion molecule L1 are involved in homophilic interactions. / Holm, J.; Appel, F.; Camartin, Melitta.

In: Journal of Neuroscience Research, Vol. 42, No. 1, 01.01.1995, p. 9-20.

Research output: Contribution to journalArticle

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