Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation.
Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation.
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DOI：
10.1083/jcb.202005214
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发表时间：
2021-09-06
期刊：
影响因子：
--
通讯作者：
Goult BT
中科院分区：
文献类型：
--
作者：
Cowell AR;Jacquemet G;Singh AK;Varela L;Nylund AS;Ammon YC;Brown DG;Akhmanova A;Ivaska J;Goult BT
Cowell等人表明，含有talin杆结构域的蛋白1（TLNRD 1），一种与整联蛋白调节剂talin的中心区域具有同源性的蛋白，保留了talin R7 R8的多种相互作用，但发展了作为促进丝状伪足组装的肌动蛋白捆绑蛋白的独特功能。Talin是一种机械敏感性衔接蛋白，其将整合素偶联至细胞骨架。Talin rod domain-containing protein 1（TLNRD 1）与talin R7 R8 rod domains有22%的同源性，在脊椎动物进化过程中高度保守，但其功能尚不清楚。在这里，我们表明TLNRD 1是一个α-螺旋蛋白结构同源talin R7 R8。像talin R7 R8一样，TLNRD 1结合F-肌动蛋白，但因为它形成一种新的反平行二聚体，它也捆绑F-肌动蛋白。此外，它与talin R7 R8结合相同的含LD基序的蛋白质RIAM和KANK。在细胞中，TLNRD 1定位于肌动蛋白束以及丝状伪足。增加TLNRD 1表达增强丝状伪足形成和细胞在2D底物上的迁移，而TLNRD 1下调具有相反的效果。总之，我们的研究结果表明，TLNRD 1保留了塔林R7 R8的多种相互作用，但已开发出独特的功能作为肌动蛋白捆绑蛋白，促进丝状伪足组装。
Cowell et al. show that talin rod domain–containing protein 1 (TLNRD1), a protein with homology to the central region of the integrin regulator, talin, has retained the diverse interactions of talin R7R8 but has developed distinct functionality as an actin-bundling protein that promotes filopodia assembly. Talin is a mechanosensitive adapter protein that couples integrins to the cytoskeleton. Talin rod domain–containing protein 1 (TLNRD1) shares 22% homology with the talin R7R8 rod domains, and is highly conserved throughout vertebrate evolution, although little is known about its function. Here we show that TLNRD1 is an α-helical protein structurally homologous to talin R7R8. Like talin R7R8, TLNRD1 binds F-actin, but because it forms a novel antiparallel dimer, it also bundles F-actin. In addition, it binds the same LD motif–containing proteins, RIAM and KANK, as talin R7R8. In cells, TLNRD1 localizes to actin bundles as well as to filopodia. Increasing TLNRD1 expression enhances filopodia formation and cell migration on 2D substrates, while TLNRD1 down-regulation has the opposite effect. Together, our results suggest that TLNRD1 has retained the diverse interactions of talin R7R8, but has developed distinct functionality as an actin-bundling protein that promotes filopodia assembly.
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DOI：
10.1107/s090744491003982x
发表时间：
2011-04
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Evans PR
通讯作者：
Evans PR
影响因子：
64.5
作者：
Hsieh, JC;Lee, L;Holdener, BC
通讯作者：
Holdener, BC
影响因子：
7.5
作者：
Jacquemet, Guillaume;Hamidi, Hellyeh;Ivaska, Johanna
通讯作者：
Ivaska, Johanna
DOI：
10.1016/j.jbc.2021.100837
发表时间：
2021-07
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Gough RE;Jones MC;Zacharchenko T;Le S;Yu M;Jacquemet G;Muench SP;Yan J;Humphries JD;Jørgensen C;Humphries MJ;Goult BT
通讯作者：
Goult BT
影响因子：
3.2
作者：
Khurana, Seema;George, Sudeep P.
通讯作者：
George, Sudeep P.