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非透明的formin蛋白delphilin作为一种肌动蛋白丝正极封端蛋白发挥作用。

Non diaphanous formin delphilin acts as a barbed end capping protein.

作者信息

Dutta Priyanka, Das Swagata, Maiti Sankar

机构信息

Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata, India; Department of Biology, Indian Institute of Science Education and Research, Pune, India.

Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata, India.

出版信息

Exp Cell Res. 2017 Aug 15;357(2):163-169. doi: 10.1016/j.yexcr.2017.05.014. Epub 2017 May 17.

Abstract

Formins are multi domain proteins present ubiquitously in all eukaryotes from lower fungi to higher vertebrates. Formins are characterized by the presence of formin homology domain-2 (FH2) and formin homology domain-1 (FH1). There are fifteen different formins present in mouse and human. Among these metazoan formins, Delphilin is a unique formin having two PDZ domains at the N-terminus and FH1, FH2 domain at the C-terminus respectively. In this study we observed that Delphilin binds to actin filaments, and Delphilin inhibits actin filament elongation like barbed end capping protein CapZ. In vitro, Delphilin stabilized actin filaments by inhibiting actin filament depolymerisation. Therefore, our study demonstrates Delphilin as an actin-filament capping protein.

摘要

formin蛋白是多结构域蛋白,普遍存在于从低等真菌到高等脊椎动物的所有真核生物中。formin蛋白的特征是存在formin同源结构域2(FH2)和formin同源结构域1(FH1)。小鼠和人类中有15种不同的formin蛋白。在这些后生动物formin蛋白中,Delphilin是一种独特的formin蛋白,其N端有两个PDZ结构域,C端分别有FH1和FH2结构域。在本研究中,我们观察到Delphilin与肌动蛋白丝结合,并且Delphilin像带刺末端封端蛋白CapZ一样抑制肌动蛋白丝的伸长。在体外,Delphilin通过抑制肌动蛋白丝解聚来稳定肌动蛋白丝。因此,我们的研究证明Delphilin是一种肌动蛋白丝封端蛋白。

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