New insights into Fat cadherins
New insights into Fat cadherins
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DOI：
10.1242/jcs.02398
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发表时间：
2005-06-01
影响因子：
4
通讯作者：
Takeichi, M
中科院分区：
文献类型：
--
作者：
Tanoue, T;Takeichi, M
细胞间粘附是多细胞结构的基础。几类粘附分子用于实现这一点，钙粘蛋白代表了这类分子的主要家族。钙粘蛋白家族有多个亚家族。脂肪钙粘蛋白亚家族的成员在物种间是保守的，具有非常大的胞外区，包括34个重复结构域，使其成为最大的钙粘蛋白分子。在果蝇中鉴定的经典脂肪已知调节细胞增殖和平面细胞极性。最近对其哺乳动物同系物之一Fat 1的研究揭示了该分子的新功能。Fat 1与Ena/VASP蛋白结合，并在细胞-细胞接触和前缘调节肌动蛋白动力学。这些观察结果表明，Fat 1是肌动蛋白动力学的重要调节因子，并通过这种活性控制细胞-细胞相互作用。
Cell-cell adhesion is fundamental to multicellular architecture. Several classes of adhesion molecule are used to achieve this, and cadherins represent a major family of such molecules. The cadherin family has multiple subfamilies. Members of the Fat cadherin subfamily, which is conserved across species, have an extraordinarily large extracellular region, comprising 34 repeated domains, making them the largest cadherin molecules. Classic Fat, identified in Drosophila, is known to regulate cell proliferation and planar cell polarity. Recent studies of one of its mammalian homologs, Fat1, have revealed novel functions of this molecule. Fat1 binds to Ena/VASP proteins and regulates actin dynamics at both cell-cell contacts and leading edges. These observations suggest that Fat1 is an important regulator of actin dynamics and controls cell-cell interactions through this activity.