Quantitative Biology at Community Colleges, a Network of Biology and Mathematics Faculty Focused on Improving Numerical and Quantitative Skills of Students.

Mastery of quantitative skills is increasingly critical for student success in life sciences, but few curricula adequately incorporate quantitative skills. Quantitative Biology at Community Colleges (QB@CC) is designed to address this need by building a grassroots consortium of community college faculty to 1) engage in interdisciplinary partnerships that increase participant confidence in life science, mathematics, and statistics domains; 2) generate and publish a collection of quantitative skills-focused open education resources (OER); and 3) disseminate these OER and pedagogical practices widely, in turn expanding the network. Currently in its third year, QB@CC has recruited 70 faculty into the network and created 20 modules.

Small molecules that inhibit the late stage of Munc13-4-dependent secretory granule exocytosis in mast cells.

Ca-dependent secretory granule fusion with the plasma membrane is the final step for the exocytic release of inflammatory mediators, neuropeptides, and peptide hormones. Secretory cells use a similar protein machinery at late steps in the regulated secretory pathway, employing protein isoforms from the Rab, Sec1/Munc18, Munc13/CAPS, SNARE, and synaptotagmin protein families. However, no small-molecule inhibitors of secretory granule exocytosis that target these proteins are currently available but could have clinical utility.

The Vesicle Priming Factor CAPS Functions as a Homodimer via C2 Domain Interactions to Promote Regulated Vesicle Exocytosis.

Neurotransmitters and peptide hormones are secreted by regulated vesicle exocytosis. CAPS (also known as CADPS) is a 145-kDa cytosolic and peripheral membrane protein required for vesicle docking and priming steps that precede Ca-triggered vesicle exocytosis. CAPS binds phosphatidylinositol 4,5-bisphosphate (PI(4,5)P) and SNARE proteins and is proposed to promote SNARE protein complex assembly for vesicle docking and priming.

Munc13-4 reconstitutes calcium-dependent SNARE-mediated membrane fusion.

Munc13-4 is a widely expressed member of the CAPS/Munc13 protein family proposed to function in priming secretory granules for exocytosis. Munc13-4 contains N- and C-terminal C2 domains (C2A and C2B) predicted to bind Ca(2+), but Ca(2+)-dependent regulation of Munc13-4 activity has not been described. The C2 domains bracket a predicted SNARE-binding domain, but whether Munc13-4 interacts with SNARE proteins is unknown.