Tran M Khang, Kurakula Kondababu, Koenis Duco S, de Vries Carlie J M
Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
Department of Medical Biochemistry, Academic Medical Center, University of Amsterdam, Amsterdam, The Netherlands.
Biochim Biophys Acta. 2016 Feb;1863(2):219-28. doi: 10.1016/j.bbamcr.2015.11.002. Epub 2015 Nov 6.
FHL2 belongs to the LIM-domain only proteins and contains four and a half LIM domains, each of which are composed of two zinc finger structures. FHL2 exhibits specific interaction with proteins exhibiting diverse functions, including transmembrane receptors, transcription factors and transcription co-regulators, enzymes, and structural proteins. The function of these proteins is regulated by FHL2, which modulates intracellular signal transduction pathways involved in a plethora of cellular tasks. The present review summarizes the current knowledge on the protein interactome of FHL2 and provides an overview of the functional implication of these interactions in apoptosis, migration, and regulation of nuclear receptor function. FHL2 was originally identified in the heart and there is extensive literature available on the role of FHL2 in the cardiovascular system, which is also summarized in this review.
FHL2属于仅含LIM结构域的蛋白质,含有四个半LIM结构域,每个结构域由两个锌指结构组成。FHL2与具有多种功能的蛋白质表现出特异性相互作用,这些蛋白质包括跨膜受体、转录因子和转录共调节因子、酶以及结构蛋白。这些蛋白质的功能受FHL2调节,FHL2可调节参与众多细胞任务的细胞内信号转导途径。本综述总结了目前关于FHL2蛋白质相互作用组的知识,并概述了这些相互作用在细胞凋亡、迁移和核受体功能调节中的功能意义。FHL2最初是在心脏中发现的,关于FHL2在心血管系统中的作用已有大量文献,本综述也对此进行了总结。