The appearance of an L1-like molecule in the chick primary visual pathway

Lemmon, Vance; McLoon, Steven C.

doi:10.1523/jneurosci.06-10-02987.1986

Cited by 157 publications

(109 citation statements)

References 20 publications

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“…The monoclonal anti-human L1 antibodies (7B5) were described previously . The polyclonal anti-chicken L1 (8D9) antibodies were described previously (Lemmon and McLoon, 1986). Fluorescent secondary antibodies were purchased from Molecular Probes (Eugene, OR).…”

Section: Methodsmentioning

confidence: 99%

L1-Mediated Branching Is Regulated by Two Ezrin-Radixin-Moesin (ERM)-Binding Sites, the RSLE Region and a Novel Juxtamembrane ERM-Binding Region

2005

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We investigated how the neural cell adhesion molecule L1 mediates neurite outgrowth through L1-L1 homophilic interactions. Wild-type L1 and L1 with mutations in the cytoplasmic domain (CD) were introduced into L1 knock-out neurons, and transfected neurons were grown on an L1 substrate. Neurite length and branching were compared between wild-type L1 and L1CD mutations. Surprisingly, the L1CD is not required for L1-mediated neurite outgrowth but plays a critical role in neurite branching, through both the juxtamembrane region and the RSLE region. We demonstrate that both regions serve as ezrin-moesin-radixin-binding sites. A truncation mutant that deletes 110 of 114 amino acids of the L1CD still supports neurite outgrowth on an L1 substrate, suggesting that a coreceptor binds to L1 in cis and mediates neurite outgrowth and that L1-ankyrin interactions are not essential for neurite initiation or outgrowth. These data are consistent with a model in which L1 can influence L1-mediated neurite outgrowth and branching through both the L1CD and a coreceptor.

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Section: Methodsmentioning

confidence: 99%

L1-Mediated Branching Is Regulated by Two Ezrin-Radixin-Moesin (ERM)-Binding Sites, the RSLE Region and a Novel Juxtamembrane ERM-Binding Region

2005

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“…Secondary antibody was Alexa Fluor 680 goat anti-rabbit IgG (Molecular Probes, Eugene, OR). After rinsing, blots were incubated with anti-chick L1 cell adhesion molecule (L1CAM) (Lemmon and McLoon, 1986), followed by infrared dye 800-conjugated anti-mouse IgG (Rockland, Gilbertsville, PA). Bound antibody was visualized, and band intensity was quantified using the LI-COR (Lincoln, NE) Odyssey Infrared Imaging System.…”

Section: Methodsmentioning

confidence: 99%

Receptor Tyrosine Phosphatases Guide Vertebrate Motor Axons during Development

Stepanek¹,

Stoker²,

Stoeckli³

et al. 2005

J. Neurosci.

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“…One group includes glycoproteins with six Ig and five FNIII domains, such as mouse L1 (Rathjen and Schachner, 1984), rat NILE (Prince et al, 1989), chicken Ng-CAM (Burgoon et al, 1991), chicken Nr-CAM (Grumet et al, 1991) and Drosophilu neuroglian (Bieber et al, 1989). Information derived from N-terminal sequencing and immunological comparisons indicate that chicken G4 (Rathjen et al, 1987), 8D9 (Lemmon and McLoon, 1986) and Bravo (de la Rosa et al, 1990) are further members of this subgroup. The members of the other subgroup of AxCAMs with Ig/FNIIi subfamily traits are composed of six Ig and four FNIII domains, viz.…”

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confidence: 99%

The axonally secreted cell adhesion molecule, axonin‐1

Zuellig

Rader

Schroeder

et al. 1992

European Journal of Biochemistry

120

111

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Axonin-I is an axon-associated cell adhesion molecule (AxCAM) of the chicken, which promotes neurite outgrowth by interaction with the AxCAM Ll(G4) of the neuritic membrane. Here we report the cloning and sequence determination of a cDNA encoding axonin-I, Peptides generated by enzymatic cleavage showed similarity to the AxCAM F11. Degenerated polymerase chain reaction (PCR) primers were designed and an axonin-I fragment was amplified from mRNA of embryonic retina. Screening of a cDNA library from embryonic brain resulted in the isolation of a 4.0-kb cDNA insert with an open reading frame of 3108 nucleotides. The deduced polypeptide of 1036 amino acids includes a putative hydrophobic N-terminal signal sequence of 23 or 25 amino acids and a C-terminal hydrophobic sequence of 29 amino acids which is suggestive of sequences serving as signal for the attachment of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) anchor. The putative mature form of axonin-1 comprises six immunoglobulin-like repeats, followed by four fibronectin-type I11 repeats.Axonin-1 exhibits 75% amino acid identity with the AxCAM TAG-1 of the rat, suggesting that it is the chicken homologue of TAG-1. Like TAG-1, axonin-I is glycosyl-PtdIns-anchored to the neuronal membrane; in contrast to TAG-1, it does not exhibit an Arg-Gly-Asp sequence.The interconnection of neurons by processes forming synaptic contacts is one of the crucial developmental stages of neurogenesis. In order to span long distances, bundles of axons are formed in a process which is thought to be driven by the tendency of growing axons to adhere specifically to and elongate along preexisting axons. The consistency with which

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The appearance of an L1-like molecule in the chick primary visual pathway

Cited by 157 publications

References 20 publications

L1-Mediated Branching Is Regulated by Two Ezrin-Radixin-Moesin (ERM)-Binding Sites, the RSLE Region and a Novel Juxtamembrane ERM-Binding Region

L1-Mediated Branching Is Regulated by Two Ezrin-Radixin-Moesin (ERM)-Binding Sites, the RSLE Region and a Novel Juxtamembrane ERM-Binding Region

Receptor Tyrosine Phosphatases Guide Vertebrate Motor Axons during Development

The axonally secreted cell adhesion molecule, axonin‐1

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