Functional and structural characterization of the talin F0F1 domain.
The globular head domain of talin, a large multi-domain cytoplasmic protein, is required for inside-out activation of the integrins, a family of heterodimeric transmembrane cell adhesion molecules. Talin head contains a FERM domain that is composed of F1, F2, and F3 subdomains. A F0 subdomain is located N-terminus to F1. The F3 contains a canonical phosphotyrosine binding (PTB) fold that directly interacts with the membrane proximal NPxY/F motif in the integrin beta cytoplasmic tail. This interaction is stabilized by the F2 that interacts with the lipid head-groups of the plasma membrane. In comparison to F2 and F3, the properties of the F0F1 remains poorly characterized. Here, we showed that F0F1 is essential for talin-induced activation of integrin alphaLbeta2 (LFA-1). F0F1 has a high content of beta-sheet secondary structure, and it tends to homodimerize that may provide stability against proteolysis and chaotrope induced unfolding.
Domadia
Prerna N
PN
School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore.
Li
Yan-Feng
YF
Bhunia
Anirban
A
Mohanram
Harini
H
Tan
Suet-Mien
SM
Bhattacharjya
Surajit
S
D002460:Cell Line; D006801:Humans; D016169:Lymphocyte Function-Associated Antigen-1 / Q000378:metabolism*; D017510:Protein Folding; D055550:Protein Stability; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016608:Talin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*
D016169:Lymphocyte Function-Associated Antigen-1; C518832:TLN1 protein, human; D016608:Talin