Mouillet-Richard S, Ermonval M, Chebassier C, Laplanche J L, Lehmann S, Launay J M, Kellermann O
Différenciation Cellulaire, CNRS-Institut Pasteur, 75724 Paris Cedex 15, France.
Science. 2000 Sep 15;289(5486):1925-8. doi: 10.1126/science.289.5486.1925.
The cellular prion protein PrPc is a glycosylphosphatidylinositol-anchored cell-surface protein whose biological function is unclear. We used the murine 1C11 neuronal differentiation model to search for PrPc-dependent signal transduction through antibody-mediated cross-linking. A caveolin-1-dependent coupling of PrPc to the tyrosine kinase Fyn was observed. Clathrin might also contribute to this coupling. The ability of the 1C11 cell line to trigger PrPc-dependent Fyn activation was restricted to its fully differentiated serotonergic or noradrenergic progenies. Moreover, the signaling activity of PrPc occurred mainly at neurites. Thus, PrPc may be a signal transduction protein.
细胞朊蛋白PrPc是一种糖基磷脂酰肌醇锚定的细胞表面蛋白，其生物学功能尚不清楚。我们使用小鼠1C11神经元分化模型，通过抗体介导的交联来寻找依赖PrPc的信号转导。观察到PrPc与酪氨酸激酶Fyn存在一种依赖小窝蛋白-1的偶联。网格蛋白可能也参与了这种偶联。1C11细胞系触发依赖PrPc的Fyn激活的能力仅限于其完全分化的血清素能或去甲肾上腺素能子代细胞。此外，PrPc的信号传导活性主要发生在神经突。因此，PrPc可能是一种信号转导蛋白。
