The neural adhesion molecule L1 is phosphorylated on tyrosine and serine residues

被引：11

作者：

Heiland, PC

Hertlein, B

Traub, O

Griffith, LS

Schmitz, B

机构：

[1] UNIV BONN,INST ANIM PHYSIOL & ANAT,DEPT BIOCHEM,D-53115 BONN,GERMANY

[2] UNIV ROME,INST GENET,D-53117 BONN,GERMANY

来源：

NEUROREPORT | 1996年 / 7卷 / 15-17期

关键词：

neural cell adhesion molecule L1; serine and tyrosine phosphorylation;

D O I：

10.1097/00001756-199611040-00053

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

THE neural cell adhesion molecule L1 is highly homologous in its extracellular domain between species and completely identical in its cytoplasmic domain. We report here that tyrosine residues of L1 are phosphorylated in addition to serine residues, as determined by monoclonal phosphotyrosine antibodies and phosphoamino acid analysis. This result supports the suggestion that the cytoplasmic domain of L1 might be involved in signal transduction.

引用

页码：2675 / 2678

页数：4

共 26 条

[1] ANKYRIN-BINDING PROTEINS RELATED TO NERVOUS-SYSTEM CELL-ADHESION MOLECULES - CANDIDATES TO PROVIDE TRANSMEMBRANE AND INTERCELLULAR CONNECTIONS IN ADULT BRAIN [J].