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 and others. (2021) Talin rod domain–containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation. Journal of Cell Biology, 220 (9). Article Number e202005214. ISSN 0021-9525. (doi:10.1083/jcb.202005214) (KAR id:89331)
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Official URL: https://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.
Item Type: | Article |
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DOI/Identification number: | 10.1083/jcb.202005214 |
Uncontrolled keywords: | talin, tlnrd1, filopodia, integrin, kank, riam, adhesion, migration, |
Subjects: | Q Science > QH Natural history > QH301 Biology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Ben Goult |
Date Deposited: | 16 Jul 2021 15:03 UTC |
Last Modified: | 03 May 2024 03:14 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/89331 (The current URI for this page, for reference purposes) |
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