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

Alana R. Cowell, Guillaume Jacquemet, Abhimanyu K. Singh, Lorena Varela, Anna S. Nylund, York-Christoph Ammon, David G. Brown, Anna Akhmanova, Johanna Ivaska, Benjamin T. Goult

Research output: Contribution to journalArticleScientificpeer-review

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Article numbere202005214
JournalJournal of Cell Biology
Volume220
Issue number9
DOIs
Publication statusPublished - 6 Sep 2021
MoE publication typeA1 Journal article-refereed

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