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核纤层蛋白的磷酸化决定了它们的结构特性和信号传导功能。

Phosphorylation of lamins determine their structural properties and signaling functions.

作者信息

Torvaldson Elin, Kochin Vitaly, Eriksson John E

机构信息

a Department of Biosciences; Åbo Akademi University ; Turku , Finland.

出版信息

Nucleus. 2015;6(3):166-71. doi: 10.1080/19491034.2015.1017167. Epub 2015 Mar 20.

Abstract

Lamin A/C is part of the nuclear lamina, a meshwork of intermediate filaments underlying the inner nuclear membrane. The lamin network is anchoring a complex set of structural and linker proteins and is either directly or through partner proteins also associated or interacting with a number of signaling protein and transcription factors. During mitosis the nuclear lamina is dissociated by well established phosphorylation- dependent mechanisms. A-type lamins are, however, also phosphorylated during interphase. A recent study identified 20 interphase phosphorylation sites on lamin A/C and explored their functions related to lamin dynamics; movements, localization and solubility. Here we discuss these findings in the light of lamin functions in health and disease.

摘要

核纤层蛋白A/C是核纤层的一部分,核纤层是位于内核膜下方的中间丝网络。核纤层网络锚定着一组复杂的结构蛋白和连接蛋白,并且直接或通过伴侣蛋白与许多信号蛋白和转录因子相关联或相互作用。在有丝分裂期间,核纤层通过成熟的磷酸化依赖性机制解离。然而,A型核纤层蛋白在间期也会发生磷酸化。最近的一项研究确定了核纤层蛋白A/C上的20个间期磷酸化位点,并探讨了它们与核纤层动态变化(运动、定位和溶解性)相关的功能。在此,我们根据核纤层蛋白在健康和疾病中的功能来讨论这些发现。

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