PROTEIN-TYROSINE PHOSPHATASES AS ADHESION RECEPTORS
PROTEIN-TYROSINE PHOSPHATASES AS ADHESION RECEPTORS
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DOI：
10.1016/0955-0674(95)80106-5
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发表时间：
1995-10-01
影响因子：
7.5
通讯作者：
TONKS, NK
中科院分区：
文献类型：
--
作者：
BRADYKALNAY, SM;TONKS, NK
经典粘附分子如N-CAM的细胞内片段与任何已知的信号分子都没有显示出结构相似性。这表明它们对信号应答的影响必须通过相关蛋白间接发挥。相反，许多受体蛋白酪氨酸磷酸酶（RPTP）具有与细胞粘附分子同源的细胞外区段，所述细胞粘附分子直接连接至包含一个或两个蛋白酪氨酸磷酸酶催化结构域的细胞内区段。因此，RPTP具有通过细胞外片段的接合直接调节催化功能的潜力，这表明它们可能是细胞接触现象的直接信号转导子。在过去的几年中，已经显示一些RPTP直接通过嗜同性结合或通过与已知的细胞粘附分子结合而间接影响细胞-细胞粘附。此外，RPTP已定位于细胞-细胞或细胞-基质接触点，表明其调节这些结构的潜力。
The intracellular segments of classic adhesion molecules such as N-CAM do not show structural similarity to any known signaling molecules. This suggests that their effects on signaling responses must be exerted indirectly through associated proteins. In contrast, many receptor protein tyrosine phosphatases (RPTPs) possess extracellular segments with homology to cell adhesion molecules linked directly to intracellular segments comprising one or two protein tyrosine phosphatase catalytic domains. Therefore, the RPTPs have the potential for direct modulation of catalytic function through engagement of the extracellular segment, suggesting they could be direct signal transducers of cell contact phenomena. in the past few years, some RPTPs have been shown to effect cell-cell adhesion directly via homophilic binding or indirectly by association with known cell adhesion molecules. In addition, RPTPs have been localized to points of cell-cell or cell-matrix contact, indicating their potential to regulate these structures.