6XZ3

Crystal structure of TLNRD1 4-helix bundle

Summary for 6XZ3

• Entry DOI: 10.2210/pdb6xz3/pdb
• Descriptor: Talin rod domain-containing protein 1, 1,2-ETHANEDIOL (3 entities in total)
• Functional Keywords: actin binding protein, protein complex, 4-helix bundle, cytoskeleton, cell adhesion
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 14523.80

Authors

Cowell, A.,Singh, A.K.,Brown, D.G.,Goult, B.T. (deposition date: 2020-02-01, release date: 2020-05-27, Last modification date: 2024-01-24)

Primary citation

Cowell, A.R.,Jacquemet, G.,Singh, A.K.,Varela, L.,Nylund, A.S.,Ammon, Y.C.,Brown, D.G.,Akhmanova, A.,Ivaska, J.,Goult, B.T.
Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation.
J.Cell Biol., 220:-, 2021

PubMed 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.

PubMed: 34264272
DOI: 10.1083/jcb.202005214

Experimental method

X-RAY DIFFRACTION (2.19 Å)