Md Sorique Aziz Momin

Cellular membranes are dynamic molecular landscapes in which lipid composition, transbilayer asymmetry, membrane curvature, thickness and mechanics collectively shape protein organization and function, while proteins can in turn remodel lipid organization and membrane architecture. Yet lipid-protein interactions are often treated as discrete binding events, obscuring the extent to which the physical organization of the membrane itself constitutes an active determinant of protein conformational states and cellular activity. Here, we investigate lipid-protein reciprocal coupling by integrating quantitative analyses of curvature-dependent protein-membrane association and hydrophobic-run organization with established structural, lipidomic and biochemical evidence. Our analysis reveals substantial variation in protein association with curved versus flat membrane environments and highlights how membrane curvature, together with lipid composition, cholesterol and asymmetry, can regulate protein structure and function, including in disease-associated systems. We further examine emerging lipid sensors, spatial proteomics and advanced biomimetic membrane platforms that are beginning to bridge molecular mechanisms with protein-lipid organization in cells. In particular, suspended membranes, pore-spanning systems and nanopillar architectures offer opportunities to independently control lipid composition, leaflet asymmetry, curvature and mechanics while directly interrogating protein behaviour. Together, these findings support a model in which membrane architecture encodes physical information that is read by proteins and reciprocally reshaped by protein activity to regulate cellular function.

Cellular memory is the competence of cells to preserve information from past experiences and respond aptly. This memory is maintained and controlled by gene regulatory networks (GRNs). GRNs are crucial for understanding why some cells are resistant to treatment, particularly for cancer. In our study, we created a new mathematical model to understand how “noise” affects cellular memory in GRNs, focusing on a “double positive feedback loop”. Our theoretical perspective article equipped with mathematical modeling exhibits how noise and feedback loops interact in GRNs. It also proposes a potential theoretical avenue for future therapy. By targeting the mechanisms that maintain drug resistance in cells, we aim to develop therapies that can restore the sensitivity of cancer cells to treatment.

SUMMARY: How cytoskeletal structures control their assembly while sharing a common pool of their constituent parts is an open question in biology. Experiments indicate that mechanisms promoting the disassembly of these structures and replenishing the pool may play a vital role. Here, we compare the role of two modes of disassembly: monomer loss and loss of fragments (severing), in the assembly of bare filaments and bundles, modeled as a collection of linear filaments. Using analytical calculations and simulations, we show that severing can accelerate the assembly of these structures and ensure their precise size control in a shared pool. We also examine their length fluctuations and find that the decay in the autocorrelation function is faster with severing. Our study identifies parameters that influence assembly kinetics as well as the decay in autocorrelations of length fluctuations. These findings provide a framework for designing experiments that can differentiate between size control mechanisms in cytoskeletal structures.