Learning from the COVID-19 Pandemic: How Faculty Experiences Can Prepare Us for Future System-Wide Disruption

The COVID-19 pandemic provided education researchers with a natural experiment: an opportunity to investigate the impacts of a system-wide, involuntary move to online teaching and to assess the characteristics of individuals who adapted more readily. To capture the impacts in real time, our team recruited college-level geoscience instructors through the National Association of Geoscience Teachers (NAGT) and American Geophysical Union (AGU) communities to participate in our study in the spring of 2020. Each weekday for three successive weeks, participants (n = 262) were asked to rate their experienced disruption in four domains: teaching, research, ability to communicate with their professional community, and work-life balance. The rating system (a scale of 1–5, with 5 as severely disrupted) was designed to assess (a) where support needs were greatest, (b) how those needs evolved over time, and (c) respondents’ capacity to adapt. In addition, participants were asked two open-response questions, designed to provide preliminary insights into how individuals were adapting—what was their most important task that day and what was their greatest insight from the previous day. Participants also provided information on their institution type, position, discipline, gender, race, dependents, and online teaching experience (see supplemental material)

Hedgehog-Interacting Protein is a multimodal antagonist of Hedgehog signalling

Hedgehog (HH) morphogen signalling, crucial for cell growth and tissue patterning in animals, is initiated by the binding of dually lipidated HH ligands to cell surface receptors. Hedgehog-Interacting Protein (HHIP), the only reported secreted inhibitor of Sonic Hedgehog (SHH) signalling, binds directly to SHH with high nanomolar affinity, sequestering SHH. Here, we report the structure of the HHIP N-terminal domain (HHIP-N) in complex with a glycosaminoglycan (GAG). HHIP-N displays a unique bipartite fold with a GAG-binding domain alongside a Cysteine Rich Domain (CRD). We show that HHIP-N is required to convey full HHIP inhibitory function, likely by interacting with the cholesterol moiety covalently linked to HH ligands, thereby preventing this SHH-attached cholesterol from binding to the HH receptor Patched (PTCH1). We also present the structure of the HHIP C-terminal domain in complex with the GAG heparin. Heparin can bind to both HHIP-N and HHIP-C, thereby inducing clustering at the cell surface and generating a high-avidity platform for SHH sequestration and inhibition. Our data suggest a multimodal mechanism, in which HHIP can bind two specific sites on the SHH morphogen, alongside multiple GAG interactions, to inhibit SHH signalling