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

Autor:	Cowell AR; School of Biosciences, University of Kent, Canterbury, UK., Jacquemet G; Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland., Singh AK; School of Biosciences, University of Kent, Canterbury, UK., Varela L; School of Biosciences, University of Kent, Canterbury, UK., Nylund AS; Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.; Faculty of Science and Engineering, Cell Biology, Åbo Akademi University, Turku, Finland., Ammon YC; Cell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands., Brown DG; School of Biosciences, University of Kent, Canterbury, UK., Akhmanova A; Cell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands., Ivaska J; Turku Centre for Biotechnology, University of Turku and Åbo Akademi University, Turku, Finland.; Department of Biochemistry, University of Turku, Turku, Finland., Goult BT; School of Biosciences, University of Kent, Canterbury, UK.
Jazyk:	angličtina
Zdroj:	The Journal of cell biology [J Cell Biol] 2021 Sep 06; Vol. 220 (9). Date of Electronic Publication: 2021 Jul 15.
DOI:	10.1083/jcb.202005214
Abstrakt:	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. (© 2021 Cowell et al.)
Databáze:	MEDLINE
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