This grant supports an annual $150,000 First Feature Production Award at New York University Tisch School of the Arts (NYU) to provide students the opportunity to produce and release their first full-length feature film that dramatizes scientific and technological themes or characters. Students submit one-page pitches for science films annually. A dozen quarter finalists are selected to write step-by-step breakdowns of their films, and from this group, six semi-finalists are chosen to meet with scientists and film faculty to improve the science content, narrative, and design of their films, before submitting revised treatments. In the finalist stage, three students are selected and awarded $5,000 each to develop their treatments into full-scale feature screenplays. Finally, one winner is selected and receives a $150,000 production award to produce their first feature film.

This grant supports Film Independent (FIND) to host the 2025 Sloan Film Summit, a convening of all Alfred P. Sloan Foundation film and media-related grantees held every three years, from film schools to film festivals and from film development and film distribution partners to theater, gaming, and social media partners. At the summit, FIND will highlight 25 years of the Sloan Foundation’s film program, looking back at where the program started and what has changed in the science and film landscape, as well as the media and broader culture. In addition to anticipated attendance by 200 members of the Sloan film community—including all the winning screenwriters, filmmakers, episodic writers, gamers, and animators from the past three years—FIND will invite members of the general public to participate in several public-facing events, adding an estimated 1000 attendees.  Funded activities include introductions and updates from Sloan award recipients; case studies of successful collaborations between filmmakers and scientists; networking opportunities that connect filmmakers with scientists, agents, casting directors, distributors, film festivals, production companies, entrepreneurs, and executives; live reading of excerpts from Sloan-winning screenplays; panels that will feature scientists expounding on underappreciated scientific stories and discoveries, and keynote addresses.

Compartmentalization is a key feature of living systems. Cells are separated from their environment by a membrane, and intracellular compartments are widely used to carry out the biochemistry upon which life relies. Biomolecular condensates are transient intracellular compartments formed when molecules within the cytoplasm undergo a condensing phase transition. The transition produces a region within the cytoplasm that’s typically denser and/or more viscous than the surrounding fluid and the transition is often referred to as liquid-liquid phase separation (LLPS). Molecules co-located within a condensate can more readily react with one another and biologists have learned that the formation and eventual dissolution of biomolecular condensates is ubiquitous across life. While much has been learned about the functions facilitated by these transient organelles, there are many open questions about how the basic physics of LLPS is impacted by the complex, heterogeneous cellular environment within which LLPS occurs. This grant funds work by Jennifer Ross and Jennifer Schwarz, professors of experimental and theoretical physics, respectively, at Syracuse University to study how two specific features of the intracellular microenvironment—the presence of an enzyme-driven ‘active bath’ that modifies the local energy landscape, and the presence of viscoelastic polymers that modify the local entropy landscape—influence the formation and dissolution of protein condensates. The phrase ‘active bath’ refers to a fluid that has been perturbed from its equilibrium thermal state by some type of activity that leads to fluid regions with local fluctuations (e.g. position fluctuations of water molecules) that exceed those associated with the fluid’s overall (equilibrium) thermal state. In this project, the relevant activity is ‘background’ enzyme reactions; chemical reactions that do not directly involve the proteins that condense during LLPS, but which may nonetheless influence LLPS. The cellular entropy feature to be explored by Ross and Schwarz is the presence of a cytoskeleton, a network of viscoelastic (i.e. both viscous and elastic) protein filaments that act to constrain the motion of molecules within a cell via crowding. The team will create cytoskeletal-like networks of varying density and stiffness by using the cytoskeletal biopolymers actin and tubulin. Experiments will vary both the overall polymer density and the actin-to-tubulin ratio. Temperature and condensing-polymer concentration are two key parameters that will be used to experimentally characterize the LLPS phase transition, and Ross and Schwarz plan to study two types of condensing proteins and—for each type of condensing protein—two types of phase transition.