THE 102 KD CADHERIN-ASSOCIATED PROTEIN - SIMILARITY TO VINCULIN AND POSTTRANSCRIPTIONAL REGULATION OF EXPRESSION

THE 102 KD CADHERIN-ASSOCIATED PROTEIN - SIMILARITY TO VINCULIN AND POSTTRANSCRIPTIONAL REGULATION OF EXPRESSION
复制标题

DOI:
10.1016/0092-8674(91)90392-c
复制
发表时间:
1991-05-31
期刊:
影响因子:
64.5
通讯作者:
TSUKITA, S
TSUKITA, S
中科院分区:
生物学1区
文献类型:
--
作者:
NAGAFUCHI, A;TAKEICHI, M;TSUKITA, S

文献摘要

被引文献

相似文献

E-钙粘蛋白细胞粘附分子与细胞质多肽结合,这种结合对其细胞结合功能至关重要。 使用分离的肝脏粘附连接,我们纯化了一种可以与 E-钙粘蛋白 (CAP102) 结合的 102 kd 蛋白,并分离了编码该蛋白的 cDNA。 cDNA 的序列分析表明该蛋白与纽蛋白相似。 不表达内源钙粘蛋白的 L 细胞表达 CAP102 的 mRNA,但仅含有微量的 CAP102 蛋白。 然而,将外源性E-钙粘蛋白引入这些细胞中,诱导了CAP102蛋白的高表达,而不影响其mRNA的量,这表明该分子存在转录后调节机制。 通过将N-或P-钙粘蛋白引入L细胞中观察到相同的效果。
The E-cadherin cell adhesion molecule is associated with cytoplasmic polypeptides, and this association is essential for its cell-binding function. Using isolated adherens junctions of the liver, we purified a 102 kd protein that can associate with E-cadherin (CAP102) and isolated cDNAs encoding this protein. Sequence analysis of the cDNAs revealed that this protein has a similarity to vinculin. L cells not expressing endogenous cadherin express the mRNA for CAP102 but have only a trace amount of CAP102 protein. Introducing exogenous E-cadherin into these cells, however, induced a high expression of CAP102 protein without affecting the amount of its mRNA, suggesting that there is a posttranscriptional regulatory mechanism for this molecule. The same effect was observed by introducing N- or P-cadherin into L cells.