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

DOI: 10.1083/jcb.202005214 DOI Help

Authors: Alana R. Cowell (University of Kent) , Guillaume Jacquemet (University of Turku; Åbo Akademi University) , Abhimanyu Singh (University of Kent) , Lorena Varela (University of Kent) , Anna S. Nylund (University of Turku; Åbo Akademi University) , York-Christoph Ammon (Utrecht University) , David Brown (University of Kent) , Anna Akhmanova (Utrecht University) , Johanna Ivaska (University of Turku; Åbo Akademi University) , Benjamin T. Goult (University of Kent)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Cell Biology , VOL 220

State: Published (Approved)
Published: September 2021
Diamond Proposal Number(s): 16207

Open Access Open Access

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.

Journal Keywords: Adhesion; Biochemistry; Cytoskeleton; Structural Biology

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: B21-High Throughput SAXS

Documents:
jcb_202005214.pdf

Discipline Tags:

Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Scattering Small Angle X-ray Scattering (SAXS)