Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation

被引:8
作者
Cowell, Alana R. [1 ]
Jacquemet, Guillaume [2 ,3 ,4 ]
Singh, Abhimanyu K. [1 ,7 ]
Varela, Lorena [1 ]
Nylund, Anna S. [2 ,3 ,4 ]
Ammon, York-Christoph [5 ]
Brown, David G. [1 ]
Akhmanova, Anna [5 ]
Ivaska, Johanna [2 ,3 ,6 ]
Goult, Benjamin T. [1 ]
机构
[1] Univ Kent, Sch Biosci, Canterbury, Kent, England
[2] Univ Turku, Turku Ctr Biotechnol, Turku, Finland
[3] Abo Akad Univ, Turku, Finland
[4] Abo Akad Univ, Fac Sci & Engn, Cell Biol, Turku, Finland
[5] Univ Utrecht, Fac Sci, Dept Biol, Cell Biol Neurobiol & Biophys, Utrecht, Netherlands
[6] Univ Turku, Dept Biochem, Turku, Finland
[7] Katholieke Univ Leuven, Rega Inst Med Res, Leuven, Belgium
基金
英国生物技术与生命科学研究理事会; 芬兰科学院;
关键词
ADHESION; REVEALS; IDENTIFICATION; RECOGNITION; VINCULIN; FEATURES; IMAGE; MOTIF; RIAM;
D O I
10.1083/jcb.202005214
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 a-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.
引用
收藏
页数:17
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