Muscle Research Unit, Department of Anatomy, Bosch Institute, The University of Sydney, Sydney, Australia.
Proteomics. 2012 Jan;12(2):203-25. doi: 10.1002/pmic.201100492. Epub 2012 Jan 4.
LIM domain proteins all contain at least one double zinc-finger motif. They belong to a large family and here we review those expressed mainly in mammalian hearts, but particularly in cardiomyocytes. These proteins contain between one and five LIM domains and usually these proteins contain other domains that have specific functions such as actin-binding, kinases and nuclear translocation motifs. While several recent reviews have summarised the importance of individual LIM domain proteins, this is the first review of its kind to cover all LIMs associated with the heart. Here we examine 33 LIM proteins (including three that bind to, but do not themselves contain, LIM domains) that are implicated in either the development of the heart, heart disorders and failure, or both. Our analysis is consistent with the view that cardiac LIM domain proteins form multiple extensive networks of multi-protein complexes within the myocardium. This multiplicity of binding partners probably protects the heart as it is challenged to maintain cardiac output, until the imbalance reaches a turning point that results in failure. We believe that the complexity of LIM interactions is properly described by the term LIM interactome.
LIM 结构域蛋白均至少含有一个双锌指基序。它们属于一个大家族，在这里我们主要综述那些在哺乳动物心脏中表达的，但特别在心肌细胞中表达的 LIM 结构域蛋白。这些蛋白包含一个到五个 LIM 结构域，通常这些蛋白还含有其他具有特定功能的结构域，如肌动蛋白结合、激酶和核转位基序。虽然最近有几篇综述总结了个别 LIM 结构域蛋白的重要性，但这是第一份涵盖与心脏相关的所有 LIM 结构域的综述。在这里，我们研究了 33 种 LIM 蛋白（包括三种与 LIM 结构域结合但自身不包含 LIM 结构域的蛋白），这些蛋白与心脏的发育、心脏疾病和衰竭或两者均有关。我们的分析与以下观点一致，即心脏 LIM 结构域蛋白在心肌内形成多个广泛的多蛋白复合物网络。这种多配体结合可能保护心脏，因为它在维持心输出量方面受到挑战，直到失衡达到导致衰竭的转折点。我们认为 LIM 相互作用的复杂性可以用 LIM 相互作用组这一术语来恰当描述。
