Factors associated with depression, anxiety, stress, PTSD, and fatigue of medical staff during the COVID-19 pandemic in Shanghai: a two-phase cross-sectional study.

During the COVID-19 pandemic in Shanghai, medical workers were more vulnerable to psychological problems. This two-phase cross-sectional survey was conducted by online questionnaires to investigate the symptoms of depression, anxiety, stress, post-traumatic stress disorder (PTSD), and fatigue in healthcare workers during the outbreak of COVID-19 and after the resumption of work and production in Shanghai. The questionnaire included the Depression Anxiety Stress Scale-21 (DASS-21), the Impact of Event Scale-Revised (IES-R), and the Fatigue Assessment Instrument (FAI).

Phase separation in the multi-compartment organization of synapses.

A neuronal synapse is formed by juxtaposition of a transmitter releasing presynaptic bouton of one neuron with a transmitter receiving postsynaptic compartment such as a spine protrusion of another neuron. Each presynaptic bouton and postsynaptic spine, though very small in their volumes already, are further compartmentalized to micro-/nano-domains with distinct molecular organizations and synaptic functions. This review summarizes studies in recent years demonstrating that multivalent protein-protein interaction-induced phase separation underlies formation and coexistence of multiple distinct molecular condensates within tiny synapses.

Demixing is a default process for biological condensates formed via phase separation.

Excitatory and inhibitory synapses do not overlap even when formed on one submicron-sized dendritic protrusion. How excitatory and inhibitory postsynaptic cytomatrices or densities (e/iPSDs) are segregated is not understood. Broadly, why membraneless organelles are naturally segregated in cellular subcompartments is unclear.

Phase separation-mediated actin bundling by the postsynaptic density condensates.

The volume and the electric strength of an excitatory synapse is near linearly correlated with the area of its postsynaptic density (PSD). Extensive research in the past has revealed that the PSD assembly directly communicates with actin cytoskeleton in the spine to coordinate activity-induced spine volume enlargement as well as long-term stable spine structure maintenance. However, the molecular mechanism underlying the communication between the PSD assembly and spine actin cytoskeleton is poorly understood.

Differential roles of CaMKII isoforms in phase separation with NMDA receptors and in synaptic plasticity.

Calcium calmodulin-dependent kinase II (CaMKII) is critical for synaptic transmission and plasticity. Two major isoforms of CaMKII, CaMKIIα and CaMKIIβ, play distinct roles in synaptic transmission and long-term potentiation (LTP) with unknown mechanisms. Here, we show that the length of the unstructured linker between the kinase domain and the oligomerizing hub determines the ability of CaMKII to rescue the basal synaptic transmission and LTP defects caused by removal of both CaMKIIα and CaMKIIβ (double knockout [DKO]).

[Effects of CeO nanoparticles on the viabilities of neural PC12 and SH-SY5Y cells].

Objective: To investigate the effects of cerium oxide (CeO) nanoparticles on the viabilities of nerve cells PC12 and SH-SY5Y.

Methods: CeO nanoparticles were synthesized, structures were characterized and properties were evaluated. PC12 cells and SH-SY5Y cells were treated with CeO nanoparticles at different concentrations (1, 2.

Structural Basis for the High-Affinity Interaction between CASK and Mint1.

CASK forms an evolutionarily conserved tripartite complex with Mint1 and Veli critical for neuronal synaptic transmission and cell polarity. The CASK CaM kinase (CaMK) domain, in addition to interacting with Mint1, can also bind to many different target proteins, although the mechanism governing CASK-CaMK/target interaction selectivity is unclear. Here, we demonstrate that an extended sequence in the N-terminal unstructured region of Mint1 binds to CASK-CaMK with a dissociation constant of ∼7.