THE NEURAL ADHESION MOLECULE L1 IS PHOSPHORYLATED ON TYROSINE AND SERINE RESIDUES

Authors
HEILAND PC HERTLEIN B TRAUB O GRIFFITH LS SCHMITZ B
Citation
Pc. Heiland et al., THE NEURAL ADHESION MOLECULE L1 IS PHOSPHORYLATED ON TYROSINE AND SERINE RESIDUES, NeuroReport, 7(15-17), 1996, pp. 2675-2678
Citations number
26
Categorie Soggetti
Neurosciences
Journal title
NeuroReport → ACNP
ISSN journal
09594965
Volume
7
Issue
15-17
Year of publication
1996
Pages
2675 - 2678
Database
ISI
SICI code
0959-4965(1996)7:15-17<2675:TNAMLI>2.0.ZU;2-C
Abstract
THE neural cell adhesion molecule L1 is highly homologous in its extra cellular domain between species and completely identical in its cytopl asmic domain. We report here that tyrosine residues of L1 are phosphor ylated in addition to serine residues, as determined by monoclonal pho sphotyrosine antibodies and phosphoamino acid analysis. This result su pports the suggestion that the cytoplasmic domain of L1 might be invol ved in signal transduction.