Yuefeng Guo

© 2015 Macmillan Publishers Limited. All rights reserved.One of the primary goals of nuclear physics is to understand the force between nucleons, which is a necessary step for understanding the structure of nuclei and how nuclei interact with each other. Rutherford discovered the atomic nucleus in 1911, and the large body of knowledge about the nuclear force that has since been acquired was derived from studies made on nucleons or nuclei. Although antinuclei up to antihelium-4 have been discovered and their masses measured, little is known directly about the nuclear force between antinucleons. Here, we study antiproton pair correlations among data collected by the STAR experiment at the Relativistic Heavy Ion Collider, where gold ions are collided with a centre-of-mass energy of 200 gigaelectronvolts per nucleon pair. Antiprotons are abundantly produced in such collisions, thus making it feasible to study details of the antiproton-antiproton interaction. By applying a technique similar to Hanbury Brown and Twiss intensity interferometry, we show that the force between two antiprotons is attractive. In addition, we report two key parameters that characterize the corresponding strong interaction: the scattering length and the effective range of the interaction. Our measured parameters are consistent within errors with the corresponding values for proton-proton interactions. Our results provide direct information on the interaction between two antiprotons, one of the simplest systems of antinucleons, and so are fundamental to understanding the structure of more-complex antinuclei and their properties.

© 2015 Macmillan Publishers Limited. Matrix stiffness potently regulates cellular behaviour in various biological contexts. In breast tumours, the presence of dense clusters of collagen fibrils indicates increased matrix stiffness and correlates with poor survival. It is unclear how mechanical inputs are transduced into transcriptional outputs to drive tumour progression. Here we report that TWIST1 is an essential mechanomediator that promotes epithelial-mesenchymal transition in response to increasing matrix stiffness. High matrix stiffness promotes nuclear translocation of TWIST1 by releasing TWIST1 from its cytoplasmic binding partner G3BP2. Loss of G3BP2 leads to constitutive TWIST1 nuclear localization and synergizes with increasing matrix stiffness to induce EMT and promote tumour invasion and metastasis. In human breast tumours, collagen fibre alignment, a marker of increasing matrix stiffness, and reduced expression of G3BP2 together predict poor survival. Our findings reveal a TWIST1-G3BP2 mechanotransduction pathway that responds to biomechanical signals from the tumour microenvironment to drive EMT, invasion and metastasis.