Global gene expression control mechanisms are modeled using a large dataset consisting of absolute-quantitative proteomics, transcriptomics, and partial metabolomics of Saccharomyces cerevisiae at a wide range of growth conditions.
Friederike E Kohrs, Ilsa-Maria Daumann ... P Robin Hiesinger
The first complete null mutant collection of all rab GTPase genes in a multicellular organism uncovers neuronal development and function sensitive to environmental challenges in Drosophila.
Agnieszka Fatalska, Emma Stepinac ... David M Glover
The dual functional protein, Gorab, associates with the Golgi as a dimer but as a monomer with the procentriole cartwheel protein, Sas6, to mediate centriole duplication.
Lise M Sjøgaard-Frich, Andreas Prestel ... Stine Falsig Pedersen
NHE1-CaM complexes of multiple stoichiometries regulate cellular Ca2+-dependent NHE1 activity and can contribute to NHE1 dimerization, the latter shown by the NMR structure of CaM linking two NHE1 cytosolic tails.
Sangyoon J Han, Evgenia V Azarova ... Gaudenz Danuser
Pre-complexation of vinculin with talin’s R8 domain facilitates nascent adhesion maturation by unfolding talin, increasing vinculin binding, and thereby transmitting traction forces to the environment.
Margaret E Torrence, Michael R MacArthur ... Brendan D Manning
ATF4 is a metabolic effector of mTORC1 signaling, co-opted to induce gene targets involved in amino acid synthesis, uptake, and tRNA charging, contributing to mTORC1-driven protein and glutathione synthesis.
Viplendra PS Shakya, William A Barbeau ... Adam L Hughes
During times of mitochondrial impairment, non-imported mitochondrial precursor proteins are targeted to the nucleus for proteasome-dependent degradation.
Dominik Schumacher, Andrea Harms ... Lotte Søgaard-Andersen
In the PomX/Y/Z cell division regulatory system, PomX is a PomZ ATPase activating protein, a scaffold for PomX/Y/Z complex formation, and important for fission of the PomX/Y/Z complex during division.
eIF2-P activates the integrated stress response by inducing a conformational change in eIF2B that decreases substrate (eIF2) binding and reduces eIF2B's catalytic activity.