Institut de Pharmacologie et Biologie Structurale, IPBS, Université de Toulouse, CNRS, UPS, Toulouse, France.
Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
Structure. 2021 Apr 1;29(4):305-307. doi: 10.1016/j.str.2021.03.009.
In this issue of Structure, Cho et al. (2020) identified an intermolecular interaction between two RIAM pleckstrin homology (PH) domains that masks the phosphoinositide-binding site, and that phosphorylation by Src unmasks the PH domain. This provides an explanation of how RIAM plasma membrane translocation is regulated to promote integrin activation.
在本期《结构》杂志中,Cho 等人(2020 年)发现了 RIAM 两个蛋白激酶 3(Src)pleckstrin 同源(PH)结构域之间的一种分子间相互作用,该相互作用掩盖了磷酸肌醇结合位点,而 Src 的磷酸化则暴露出 PH 结构域。这解释了 RIAM 如何通过质膜易位来调节整合素激活。