神经黏附分子L1在酪氨酸和丝氨酸残基上发生磷酸化。
The neural adhesion molecule L1 is phosphorylated on tyrosine and serine residues.
作者信息
Heiland P C, Hertlein B, Traub O, Griffith L S, Schmitz B
机构信息
Biochemical Department of the Institute of Animal Physiology and Anatomy, University of Bonn, Germany.
出版信息
Neuroreport. 1996 Nov 4;7(15-17):2675-8. doi: 10.1097/00001756-199611040-00053.
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.
神经细胞黏附分子L1在物种间其胞外结构域具有高度同源性，而胞质结构域则完全相同。我们在此报告，通过单克隆磷酸酪氨酸抗体和磷酸氨基酸分析确定，L1的酪氨酸残基除了丝氨酸残基外也会发生磷酸化。这一结果支持了L1的胞质结构域可能参与信号转导的推测。
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