Marty Isabelle, Fauré Julien, Fourest-Lieuvin Anne, Vassilopoulos Stéphane, Oddoux Sarah, Brocard Julie
INSERM U, Grenoble Institut des Neurosciences, France.
J Physiol. 2009 Jul 1;587(Pt 13):3117-21. doi: 10.1113/jphysiol.2009.171892. Epub 2009 Apr 29.
During the last 20 years, the identification of triadin function in cardiac and skeletal muscle has been the focus of numerous studies. First thought of as the missing link between the ryanodine receptor and the dihydropyridine receptor and responsible of skeletal type excitation-contraction coupling, the current hypothesis on triadin function has slowly evolved, and triadin is envisaged now as a regulator of calcium release, both in cardiac and skeletal muscle. Nevertheless, none of the experiments performed up to now has given a clear cut view of what triadin really does in muscle. The problem became more complex with the identification of multiple triadin isoforms, having possibly multiple functions. Using a different approach from what has been done previously, we have obtained new clues about the function of triadin. Our data point to a possible involvement of triadin in reticulum structure, in relation with the microtubule network.
在过去20年里,三联蛋白在心肌和骨骼肌中的功能鉴定一直是众多研究的焦点。三联蛋白最初被认为是兰尼碱受体和二氢吡啶受体之间缺失的环节,负责骨骼肌型兴奋-收缩偶联,目前关于三联蛋白功能的假说已逐渐演变,现在认为三联蛋白是心肌和骨骼肌中钙释放的调节因子。然而,迄今为止所进行的实验均未清晰地揭示三联蛋白在肌肉中究竟发挥着何种作用。随着多种可能具有多种功能的三联蛋白亚型的鉴定,这个问题变得更加复杂。通过采用与以往不同的方法,我们获得了关于三联蛋白功能的新线索。我们的数据表明三联蛋白可能与微管网络相关,参与内质网结构的形成。