A1 Journal article – refereed

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




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

Publisher: Rockefeller University Press

Publication year: 2021

Journal: Journal of Cell Biology

Journal name in source: The Journal of cell biology

Journal acronym: J Cell Biol

Volume number: 220

Issue number: 9

ISSN: 0021-9525

eISSN: 1540-8140

DOI: http://dx.doi.org/10.1083/jcb.202005214


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.

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Last updated on 2021-02-09 at 12:41