THE GLYPIATED NEURONAL CELL-ADHESION MOLECULE CONTACTIN/F11 COMPLEXES WITH SRC-FAMILY PROTEIN-TYROSINE KINASE FYN
THE GLYPIATED NEURONAL CELL-ADHESION MOLECULE CONTACTIN/F11 COMPLEXES WITH SRC-FAMILY PROTEIN-TYROSINE KINASE FYN
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DOI：
10.1006/mcne.1995.1021
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发表时间：
1995-06-01
影响因子：
3.5
通讯作者：
VAUGHAN, L
中科院分区：
文献类型：
--
作者：
ZISCH, AH;DALESSANDRI, L;VAUGHAN, L
免疫球蛋白超家族的糖基磷脂酰肌醇锚定糖蛋白在发育过程中神经元网络的形成中发挥重要作用。神经元 GPI 连接分子转导识别信号的机制仍有待建立。对去污剂抗性免疫复合物的分析表明，糖化神经元细胞粘附分子 contactin/F11 与细胞质非受体型 src 家族酪氨酸激酶 Fyn 特异性复合。胚胎鸡神经元细胞上抗体介导的 contactin/F11 交联导致与 contactin/F11 共沉淀的 Fyn 活性增加，并提高 contactin/F11 免疫复合物内额外 75/80 K 成分的磷酸化。此外，配体，即contactin/F11特异性抗体或tenascin-R（contactin/F11的天然配体）与表达contactin/F11的HeLa转染子表面的结合，引起contactin/F11的加帽以及细胞内激酶Fyn分布的伴随变化，从而证实了它们的物理关联。这表明 contactin/F11 介导的信号传导需要 Fyn。
Glycosyl phosphatidylinositol-anchored glycoproteins of the immunoglobulin superfamily play an important role in the formation of neuronal networks during development. The mechanism whereby neuronal GPI-linked molecules transduce recognition signals remains to be established. Analysis of detergent-resistant immune-complexes reveals that the glypiated neuronal cell adhesion molecule contactin/F11 specifically complexes with the cytoplasmic, nonreceptor type src-family tyrosine kinase Fyn. Antibody-mediated cross-linking of contactin/F11 on embryonic chick neuronal cells leads to an increase of the Fyn-activity coprecipitated with contactin/F11, and elevates phosphorylation of an additional 75/80 K component within the contactin/F11-immune-complex. Additionally, binding of ligands, i.e., contactin/F11-specific antibody or tenascin-R, a natural ligand of contactin/F11, to the surface of HeLa transfectants expressing contactin/F11, causes capping of contactin/F11 and a concomitant change in the distribution of the intracellular kinase Fyn, thus confirming their physical association. This indicates that contactin/F11-mediated signaling requires Fyn.