University of Edinburgh, School of Biological Sciences, Darwin Building, Kings Buildings, Edinburgh EH9 3JR, Scotland, UK.
Semin Cell Dev Biol. 2011 Sep;22(7):673-80. doi: 10.1016/j.semcdb.2011.08.003. Epub 2011 Aug 12.
14-3-3 is now well established as a family of dimeric proteins that can modulate interaction between proteins involved in a wide range of functions. In many cases, these proteins show a distinct preference for a particular isoform(s) of 14-3-3 and in many cases a specific repertoire of dimer formation influences the particular proteins that 14-3-3 interact. Well over 200 proteins have been shown to interact with 14-3-3. The purpose of this review is to give an overview of the recently identified post-translational modifications of 14-3-3 isoforms and how this regulates function, interaction, specificity of dimerisation between isoforms and cellular location of target proteins. The association between 14-3-3 and its targets usually involves phosphorylation of the interacting protein which has been the subject of many reviews and discussion of this is included in other reviews in this series. However, it is now realised that in some cases the phosphorylation and a number of other, novel covalent modifications of 14-3-3 isoforms may modulate interaction and dimerisation of 14-3-3. Since this aspect is now emerging to be of major importance in the mechanism of regulation by 14-3-3 isoforms and has not been the focus of previous reviews, this will be detailed here.
14-3-3 现已被广泛认为是一种二聚体蛋白家族，能够调节涉及广泛功能的蛋白质之间的相互作用。在许多情况下，这些蛋白质对特定的 14-3-3 同工型表现出明显的偏好，并且在许多情况下，特定的二聚体形成谱影响 14-3-3 相互作用的特定蛋白质。已经证明有超过 200 种蛋白质与 14-3-3 相互作用。本文综述的目的是概述最近鉴定的 14-3-3 同工型的翻译后修饰以及它们如何调节功能、相互作用、同工型二聚化的特异性和靶蛋白的细胞定位。14-3-3 与其靶标的结合通常涉及相互作用蛋白的磷酸化，这已经是许多综述的主题，并且在本系列中的其他综述中也对此进行了讨论。然而，现在已经意识到，在某些情况下，磷酸化和其他一些新的 14-3-3 同工型的共价修饰可能会调节 14-3-3 的相互作用和二聚化。由于这一方面现在在 14-3-3 同工型的调节机制中变得非常重要，并且不是以前综述的重点，因此将在这里详细介绍。
