(Q28140282)

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The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling between neurons and glial cells

scientific article (publication date: April 1999)

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The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling between neurons and glial cells (English)

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author name string

J M Revest

1

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C Faivre-Sarrailh

2

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N Maeda

3

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M Noda

4

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M Schachner

5

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G Rougon

6

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language of work or name

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publication date

April 1999

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European Journal of Neuroscience

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11

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4

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1134-47

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Basic local alignment search tool

1 reference

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CAM-FGF receptor interactions: a model for axonal growth

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A soluble form of the F3 neuronal cell adhesion molecule promotes neurite outgrowth.

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Axonal molecules of the immunoglobulin superfamily bearing a GPI anchor: their role in controlling neurite outgrowth.

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The mouse neuronal cell surface protein F3: a phosphatidylinositol-anchored member of the immunoglobulin superfamily related to chicken contactin

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Transfected F3/F11 neuronal cell surface protein mediates intercellular adhesion and promotes neurite outgrowth

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Developmental mechanisms that generate precise patterns of neuronal connectivity

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Bidirectional signalling through the EPH-family receptor Nuk and its transmembrane ligands

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Axon guidance molecules

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A human transmembrane protein-tyrosine-phosphatase, PTP zeta, is expressed in brain and has an N-terminal receptor domain homologous to carbonic anhydrases

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MUC18, a marker of tumor progression in human melanoma, shows sequence similarity to the neural cell adhesion molecules of the immunoglobulin superfamily

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J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth

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Purification, characterization and developmental expression of a brain-specific chondroitin sulfate proteoglycan, 6B4 proteoglycan/phosphacan.

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Multiple receptor-like protein tyrosine phosphatases in the form of chondroitin sulfate proteoglycan

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Phosphacan, a chondroitin sulfate proteoglycan of brain that interacts with neurons and neural cell-adhesion molecules, is an extracellular variant of a receptor-type protein tyrosine phosphatase

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Interactions of the chondroitin sulfate proteoglycan phosphacan, the extracellular domain of a receptor-type protein tyrosine phosphatase, with neurons, glia, and neural cell adhesion molecules

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TAG-1/axonin-1 is a high-affinity ligand of neurocan, phosphacan/protein-tyrosine phosphatase-zeta/beta, and N-CAM

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Protein tyrosine phosphatases in signal transduction.

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Characterization and developmental regulation of proteoglycan-type protein tyrosine phosphatase zeta/RPTPbeta isoforms

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The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin

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Identification of a novel contactin-associated transmembrane receptor with multiple domains implicated in protein-protein interactions

1 reference

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The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180

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Sequence of contactin, a 130-kD glycoprotein concentrated in areas of interneuronal contact, defines a new member of the immunoglobulin supergene family in the nervous system

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Induction of neurite outgrowth through contactin and Nr-CAM by extracellular regions of glial receptor tyrosine phosphatase beta

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Growth factor signaling by receptor tyrosine kinases

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Making the connection: Cytoskeletal rearrangements during growth cone guidance

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The molecular biology of axon guidance

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Expression of high levels of the extracellular matrix glycoprotein, tenascin-C, in the normal adult hypothalamoneurohypophysial system

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Activity-dependent neuronal-glial and synaptic plasticity in the adult mammalian hypothalamus

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Transient intercellular adhesion: the importance of weak protein-protein interactions

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Isolation of a tenascin-R binding protein from mouse brain membranes. A phosphacan-related chondroitin sulfate proteoglycan

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Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11

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Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains

1 reference

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10.1046/J.1460-9568.1999.00521.X

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