6xz3
From Proteopedia
Crystal structure of TLNRD1 4-helix bundle
Structural highlights
FunctionTLRN1_HUMAN Actin-binding protein which may have an oncogenic function and regulates cell proliferation, migration and invasion in cancer cells.[1] Publication Abstract from PubMedTalin 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 alpha-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. Talin rod domain-containing protein 1 (TLNRD1) is a novel actin-bundling protein which promotes filopodia formation.,Cowell AR, Jacquemet G, Singh AK, Varela L, Nylund AS, Ammon YC, Brown DG, Akhmanova A, Ivaska J, Goult BT J Cell Biol. 2021 Sep 6;220(9). pii: 212472. doi: 10.1083/jcb.202005214. Epub, 2021 Jul 15. PMID:34264272[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
