6XZ3

Crystal structure of TLNRD1 4-helix bundle

6XZ3 の概要

• エントリーDOI: 10.2210/pdb6xz3/pdb
• 分子名称: Talin rod domain-containing protein 1, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: actin binding protein, protein complex, 4-helix bundle, cytoskeleton, cell adhesion
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14523.80

構造登録者

Cowell, A.,Singh, A.K.,Brown, D.G.,Goult, B.T. (登録日: 2020-02-01, 公開日: 2020-05-27, 最終更新日: 2024-01-24)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.19 Å)