Service Learning as Inquiry in an Undergraduate Science Course

To engage students in applying scientific process skills to real-world issues, we implemented a service-learning project model in our undergraduate introductory biology course for science majors. This model illustrates how we integrate inquiry inside and outside of the classroom through four steps: service, learning, classroom, and community. Out-of-class activities engaged students in serving the community (Service step) while deepening their learning experience beyond what they would learn in a classroom (Learning step). To connect the service-learning project with scientific process skills, students were asked to identify problems that our community partners were trying to solve, identify proposed solutions, and design ways to evaluate those solutions (Classroom step). Additionally, students connected their service-learning topic with core concepts in Biology. After their service, students used metrics to analyze their impact. Students then synthesized the connection between their service, learning, and classroom projects by presenting their findings to the scientific and lay communities through a poster session (Community step). Here we provide details of the model, recommendations, and examples for others to execute an inquiry-based service-learning project

A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability

Intermediate filaments (IFs) are fibrous polymers encoded by a large family of differentially expressed genes that provide crucial structural support in the cytoplasm and nucleus in higher eukaryotes. The mechanisms involved in bringing together ∼16 elongated coiled-coil dimers to form an IF are poorly defined. Available evidence suggests that tetramer subunits play a key role during IF assembly and regulation. Through molecular modeling and site-directed mutagenesis, we document a hitherto unnoticed hydrophobic stripe exposed at the surface of coiled-coil keratin heterodimers that contributes to the extraordinary stability of heterotetramers. The inability of K16 to form urea-stable tetramers in vitro correlates with an increase in its turnover rate in vivo. The data presented support a specific conformation for the assembly competent IF tetramer, provide a molecular basis for their differential stability in vitro, and point to the physiological relevance associated with this property in vivo

Panel Discussion: Building Structural Equity and Inclusion

The theme for International Open Access Week focuses on the need for action on equity and inclusion in open research and scholarship. Join us for a panel discussion on what actions have been taken on the NC A&T campus to build equity and inclusion in STEM research. Panelists will discuss programs that help build the foundation for equity and inclusion, challenges and opportunities, and ways individuals can contribute to the cause

Dynamic Movement of the Calcium Sensor STIM1 and the Calcium Channel Orai1 in Activated T-Cells: Puncta and Distal Caps

The proteins STIM1 and Orai1 are the long sought components of the store-operated channels required in T-cell activation. However, little is known about the interaction of these proteins in T-cells after engagement of the T-cell receptor. We found that T-cell receptor engagement caused STIM1 and Orai1 to colocalize in puncta near the site of stimulation and accumulate in a dense structure on the opposite side of the T-cell. FRET measurements showed a close interaction between STIM1 and Orai1 both in the puncta and in the dense cap-like structure. The formation of cap-like structures did not entail rearrangement of the entire endoplasmic reticulum. Cap formation depended on TCR engagement and tyrosine phosphorylation, but not on channel activity or Ca2+ influx. These caps were very dynamic in T-cells activated by contact with superantigen pulsed B-cells and could move from the distal pole to an existing or a newly forming immunological synapse. One function of this cap may be to provide preassembled Ca2+ channel components to existing and newly forming immunological synapses