Petit Marleen M R, Crombez Koen R M O, Vervenne Hilke B V K, Weyns Nancy, Van de Ven Wim J M
Laboratory for Molecular Oncology, Department of Human Genetics, University of Leuven and Flanders Interuniversity Institute for Biotechnology VIB, Herestraat 49, B-3000 Leuven, Belgium.
FEBS Lett. 2005 Sep 12;579(22):5061-8. doi: 10.1016/j.febslet.2005.08.012.
The zyxin family of proteins consists of five members, ajuba, LIMD1, LPP, TRIP6 and zyxin, which localize at cell adhesion sites and shuttle to the nucleus. Previously, we established that LPP interacts with the tumor suppressor Scrib, a member of the leucine-rich repeat and PDZ (LAP) family of proteins. Here, we demonstrate that Scrib also interacts with TRIP6, but not with zyxin, ajuba, or LIMD1. We show that TRIP6 directly binds to the third PDZ domain of Scrib via its carboxy-terminus. Both proteins localize in cell-cell contacts but are not responsible to target each other to these structures. In the course of our experiments, we also characterized the nuclear export signal of human TRIP6, and show that LIMD1 is localized in focal adhesions. The binding between two of zyxin's family members and Scrib links Scrib to a communication pathway between cell-cell contacts and the nucleus, and implicates these zyxin family members in Scrib-associated functions.
zyxin蛋白家族由五个成员组成,即ajuba、LIMD1、LPP、TRIP6和zyxin,它们定位于细胞黏附位点并穿梭进入细胞核。此前,我们证实LPP与肿瘤抑制因子Scrib相互作用,Scrib是富含亮氨酸重复序列和PDZ(LAP)蛋白家族的成员。在此,我们证明Scrib也与TRIP6相互作用,但不与zyxin、ajuba或LIMD1相互作用。我们发现TRIP6通过其羧基末端直接与Scrib的第三个PDZ结构域结合。这两种蛋白都定位于细胞间接触部位,但并非彼此定位到这些结构的原因。在我们的实验过程中,我们还对人TRIP6的核输出信号进行了表征,并表明LIMD1定位于粘着斑。zyxin家族的两个成员与Scrib之间的结合将Scrib连接到细胞间接触与细胞核之间的通讯途径,并表明这些zyxin家族成员参与了与Scrib相关的功能。