Sabo S L, Ikin A F, Buxbaum J D, Greengard P
Laboratory of Molecular and Cellular Neuroscience and the Zachary and Elizabeth M. Fisher Center, The Rockefeller University, New York, New York 10021, USA.
J Cell Biol. 2001 Jun 25;153(7):1403-14. doi: 10.1083/jcb.153.7.1403.
FE65 binds to the Alzheimer amyloid precursor protein (APP), but the function of this interaction has not been identified. Here, we report that APP and FE65 are involved in regulation of cell movement. APP and FE65 colocalize with actin and Mena, an Abl-associated signaling protein thought to regulate actin dynamics, in lamellipodia. APP and FE65 specifically concentrate with beta 1-integrin in dynamic adhesion sites known as focal complexes, but not in more static adhesion sites known as focal adhesions. Overexpression of APP accelerates cell migration in an MDCK cell wound--healing assay. Coexpression of APP and FE65 dramatically enhances the effect of APP on cell movement, probably by regulating the amount of APP at the cell surface. These data are consistent with a role for FE65 and APP, possibly in a Mena-containing macromolecular complex, in regulation of actin-based motility.
FE65与阿尔茨海默病淀粉样前体蛋白（APP）结合，但其相互作用的功能尚未明确。在此，我们报告APP和FE65参与细胞运动的调节。在片足中，APP和FE65与肌动蛋白及Mena共定位，Mena是一种与Abl相关的信号蛋白，被认为可调节肌动蛋白动力学。APP和FE65在称为粘着斑复合体的动态粘附位点与β1整合素特异性聚集，但在称为粘着斑的更稳定的粘附位点则不然。在MDCK细胞伤口愈合试验中，APP的过表达加速了细胞迁移。APP和FE65的共表达显著增强了APP对细胞运动的影响，这可能是通过调节细胞表面APP的量来实现的。这些数据与FE65和APP可能在含Mena的大分子复合物中调节基于肌动蛋白的运动性的作用一致。
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