ci-group/revolve2: 1.0.0rc1

<p><strong>New features</strong></p> <ul> <li>Reworked interface for simulation and modular robot simulation.</li> <li>Added feedback for brains. Implemented for active hinge positions.</li> <li>Added v2 hardware support in simulation.</li> <li>Armature, kv, and kp can now be set directly in ActiveHinge.</li> <li>RPi controller has been reworked to be a lot easier to use. Remote has been removed temporarily but we will be added again soon in better shape.</li> </ul> <p><strong>Documentation and general project things</strong></p> <ul> <li>Many and various improvements to documentation.</li> <li><ul> <li>Various improvements and fixes to the CI.</li> </ul> </li> <li><ul> <li>Improved and added examples.</li> </ul> </li> <li><ul> <li>Updated project layout and pyproject.toml files.</li> </ul> </li> </ul> <p><strong>Bug fixes and minor updates</strong></p> <ul> <li>Fixed bug in geometries where colors were not properly initialized.</li> <li>Added Vector2d and replaced Vector3d wherever applicable.</li> <li>Removed warning message for NamedTemporaryFile on Windows, as the applied backup strategy turns out to be reliable, making the * Various minor refactors and cleanups.message superfluous.</li> </ul> <p><strong>Regressions</strong> RPi controller remote has been removed, but will be added again in the next version in an improved form.</p&gt

Loss of HAUSP-mediated deubiquitination contributes to DNA damage-induced destabilization of Hdmx and Hdm2

The p53 tumor suppressor protein has a major role in protecting the integrity of the genome. In unstressed cells, p53 is maintained at low levels by the ubiquitin-proteasome pathway. A balance between ubiquitin ligase activity (Hdm2, COP1, and Pirh2) and the ubiquitin protease activity of the Herpes virus-associated ubiquitin-specific protease (HAUSP) determines the half-life of p53. HAUSP also modulates p53 stability indirectly by deubiquitination and stabilization of Hdm2. The Hdmx protein affects p53 stability as well through its interaction with and regulation of Hdm2. Vice versa, Hdmx is a target for Hdm2-mediated ubiquitination and degradation. Here, we show that HAUSP also interacts with Hdmx, resulting in its direct deubiquitination and stabilization. HAUSP activity is required to maintain normal Hdmx protein levels. Therefore, the balance between HAUSP and Hdm2 activity determines Hdmx protein stability. Importantly, impaired deubiquitination of Hdmx/Hdm2 by HAUSP contributes to the DNA damage-induced degradation of Hdmx and transient instability of Hdm2