PNAS and other interpretations! Scientists reveal new features of integrated and ankle proteins

In the cell membrane, the integratant forms a connection between the cytostebrae and the extracellular substation, and the regulation of the activity of the integrated protein is very important for the function of the tissue and the single cell.
In this study, researchers investigated the structure and function of the ankle protein, a cytostoprotein protein that is important for regulating the activity of the integrator's subject, through which the ankle protein binds to the cytosome through its "head" and connects it to the cytostic skeleton, thus acting as part of the cell's mechanical signaling network, which in turn affects cell adhesion, migration, and gene expression.
paper, researchers used X-ray crystallology to reveal the atomic structure of the ankle protein's head, giving scientists unprecedented understanding of how ankle protein binds to an integrator. Professor Nen says, for example, that the activation of an integrator mediated by ankle protein is critical for many cancers, so understanding the detailed structure of ankle protein may help develop inhibitors that prevent the interaction between ankle protein and allicin, thereby helping to successfully fight cancer.
structure of the ankle protein was discovered by researcher Jinhua Wu, while the latter cell biology findings were carried out by a team led by Professor Bernhard Wehrle-Haller at the University of Geneva in Switzerland and published in the journal PNAS.
researchers point out that ankle protein is a cytoskeletal protein that, like molecular hinges, connects the contractional myostin that forms the cytoskeletal frame with the integration of extracellular and substring binding.
the importance and significance of the structure of the ankle protein for the activation of the integrator gives scientists a new perspective, in which the researchers used molecular dynamics to simulate the interaction between the ankle protein and the integrator pair.
from the University of Eastern Finland, Janne J? Writing in the journal Journal of Cell Science, professor Nis said their findings provide new details about the mechanisms by which proteins interact.
Kukkurainen noted that the F1 sub-unit of the ankle protein is important for the activation of the integrated protein.
now at the University of Tanpere, researcher Latifeh Azizi is currently studying how mutations in ankle proteins affect protein function.
study, published in the international journal Scientific Reports, researcher Azizi et al. revealed how mutations observed in the body of cancer patients affect the structure, interaction and biological activity of ankle proteins in cells.
the researchers were screened out of the sequence database using structural data and bio-informational methods.
am interested me that a single mutation in a large protein may have such an effect on cell function, ' says Azizi, a director of the University of American States.
The results, which affect cell movement and cell communication, could help scientists move further toward the development of individualized therapies, and could also use information about tumors in cancer patients to help select more appropriate treatments, the researchers said.
(Bioon .com) Resources: Pingfeng Zhang et al. Crystal structure of the FERM-folded talin head reveals the determinants for integrin binding, Proceedings of the National Academy of Sciences (2020). DOI： 10.1073/pnas.2014583117 【2】Sampo Kukkurainen et al. The F1 loop of the talin head domain acts as a gatekeeper in integrin activation and clustering, Journal of Cell Science (2020). DOI： 10.1242/jcs.239202 【3】Latifeh Azizi et al. Cancer associated talin point mutations disorganise cell adhesion and migration, Scientific Reports (2021). DOI： 10.1038/s41598-020-77911-4 【4】New functions of integrin and talin discovered by an international research network by Tampere University