Work

Atypical interactions of integrin α V β 8 with pro-TGF-β1

Year: 2017

Type: article

Abstract: Significance Integrins are cell-surface molecules that link extracellular ligands to the cytoskeleton. Force exerted by the cytoskeleton that is resisted by the ligand is thought to be important in activating the integrin by stabilizing an extended-open conformational state with high affinity for ligand. However, integrin α V β 8 does not interact with the cytoskeleton in the same way. Here, we show that, although the closely related integrins α V β 8 and α V β 6 bind the same ligand, pro-TGF-β1, their conformational responses to ligand binding and regulation by metal ions are quite different. These differences correlate with their distinct linkage to the cytoskeleton.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1705129114

Authors: Jianchuan Wang, Xianchi Dong, Bo Zhao, Jing Li, Chafen Lu, Timothy A. Springer

Institutions: Boston Children's Hospital, Harvard University

Language: English

Topic: Cell Adhesion Molecules Research

Subfield: Immunology and Allergy

Field: Medicine

Domain: Health Sciences

SDG: Good health and well-being

Open Access status: green

Funders: National Heart, Lung, and Blood Institute, National Institute of Arthritis and Musculoskeletal and Skin Diseases