RCEA: Real-time, Continuous Emotion Annotation for collecting precise mobile video ground truth labels

Collecting accurate and precise emotion ground truth labels for mobile video watching is essential for ensuring meaningful predictions. However, video-based emotion annotation techniques either rely on post-stimulus discrete self-reports, or allow real-time, continuous emotion annotations (RCEA) only for desktop settings. Following a user-centric approach, we designed an RCEA technique for mobile video watching, and validated its usability and reliability in a controlled, indoor (N=12) and later outdoor (N=20) study. Drawing on physiological measures, interaction logs, and subjective workload reports, we show that (1) RCEA is perceived to be usable for annotating emotions while mobile video watching, without increasing users' mental workload (2) the resulting time-variant annotations are comparable with intended emotion attributes of the video stimuli (classification error for valence: 8.3%; arousal: 25%). We contribute a validated annotation technique and associated annotation fusion method, that is suitable for collecting fine-grained emotion annotations while users watch mobile videos

Ring closure activates yeast γTuRC for species-specific microtubule nucleation

The γ-tubulin ring complex (γTuRC) is the primary microtubule nucleator in cells. γTuRC is assembled from repeating γ-tubulin small complex (γTuSC) subunits and is thought to function as a template by presenting a γ-tubulin ring that mimics microtubule geometry. However, a previous yeast γTuRC structure showed γTuSC in an open conformation that prevents matching to microtubule symmetry. By contrast, we show here that γ-tubulin complexes are in a closed conformation when attached to microtubules. To confirm its functional importance we trapped the closed state and determined its structure, showing that the γ-tubulin ring precisely matches microtubule symmetry and providing detailed insight into γTuRC architecture. Importantly, the closed state is a stronger nucleator, suggesting this conformational switch may allosterically control γTuRC activity. Finally, we demonstrate that γTuRCs have a profound preference for tubulin from the same species

The molecular architecture of the yeast spindle pole body core determined by Bayesian integrative modeling

Microtubule-organizing centers (MTOCs) form, anchor, and stabilize the polarized network of microtubules in a cell. The central MTOC is the centrosome that duplicates during the cell cycle and assembles a bipolar spindle during mitosis to capture and segregate sister chromatids. Yet, despite their importance in cell biology, the physical structure of MTOCs is poorly understood. Here we determine the molecular architecture of the core of the yeast spindle pole body (SPB) by Bayesian integrative structure modeling based on in vivo fluorescence resonance energy transfer (FRET), small-angle x-ray scattering (SAXS), x-ray crystallography, electron microscopy, and two-hybrid analysis. The model is validated by several methods that include a genetic analysis of the conserved PACT domain that recruits Spc110, a protein related to pericentrin, to the SPB. The model suggests that calmodulin can act as a protein cross-linker and Spc29 is an extended, flexible protein. The model led to the identification of a single, essential heptad in the coiled-coil of Spc110 and a minimal PACT domain. It also led to a proposed pathway for the integration of Spc110 into the SPB