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RIAM的磷酸化激活其在介导整合素信号传导中的衔接子功能。

Phosphorylation of RIAM Activates Its Adaptor Function in Mediating Integrin Signaling.

作者信息

Su Baihao, Wu Jinhua

机构信息

Molecular Therapeutics Program, Fox Chase Cancer Center, Philadelphia, PA 19111, USA.

出版信息

J Cell Signal. 2021;2(2):103-110. doi: 10.33696/signaling.2.041.

Abstract

Integrins are cellular receptors that regulate cell adhesion and many other cellular functions. Integrins can be activated via an "inside-out pathway" that is promoted by RAP1 GTPase. RAP1-GTP-Interacting Adaptor Molecular (RIAM) mediates integrin activation by linking RAP1 GTPase to talin, an integrin activator. RIAM's function in integrin signaling is tightly regulated. In this commentary, we review recent studies of the molecular mechanisms underlying RIAM autoinhibition via both intramolecular interaction and oligomer assembly, and the phosphorylation-dependent activation of RIAM.

摘要

整合素是调节细胞黏附及许多其他细胞功能的细胞受体。整合素可通过由RAP1 GTP酶促进的“由内向外途径”被激活。RAP1-GTP相互作用衔接分子(RIAM)通过将RAP1 GTP酶与整联蛋白激活剂踝蛋白相连来介导整合素激活。RIAM在整合素信号传导中的功能受到严格调控。在本述评中,我们综述了关于RIAM通过分子内相互作用和寡聚体组装实现自身抑制以及RIAM磷酸化依赖性激活的分子机制的近期研究。

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