报告题目： Rod-like force-bearing proteins as a molecular shock absorber
报告人: Prof. Jie Yan
Department of Physics and Mechanobiology Institute, National University of Singapore
Many force-bearing proteins have a large rod domain consisting of a linear array of tandem repeats of protein domains. Such proteins often serve as mechanical linkages in cells, and play an important mechanosensing function through force-dependent interactions with other cellular factors. I will present our recent studies that have revealed a new function of such proteins, acting as a molecular shock absorber that buffers force within certain range during stochastic stretching and relaxation of the proteins (1, 2). A tightly controlled tension range by such force-buffering proteins has an apparent advantage of allowing robust mechanosensitive interactions to take place. I will demonstrate the force-buffering function of such proreins using talin and titin as two examples, one keeping forces in 7-10 pN at cell-ECM adherence sites, and the other keeping forces in 40 - 50 pN in sarcomere during muscle extensin and contraction.
 Yao, et al., (2016). "The mechanical response of talin." Nature Communications, 7: 11966.
 Yuan et al., (2016). " Elasticity of transition state leads to an unexpected mechanical stabilization of titin immunoglobulin domains." Submitted for peer review.
Jie Yan is currently a professor in the department of physics and a principal investigator in the Mechanobiology Institute, National University of Singapore. He is also a Fellow of American Physical Society and a Singapore NRF Investigator. His laboratory has focused on understanding micromechanics of DNA, protein, and their interactions, at a single-molecule level, to address important questions covering a broad spectrum of areas such as DNA organization and gene regulation, DNA damage repair, and mechanosensing of cells.