Clustering of lipids driven by integrin.

Integrin is an important transmembrane receptor protein which remodels the actin network and anchors the cell membrane towards the extracellular matrix via mechanochemical pathways. The clustering of specific lipids and lipid-anchored proteins, which is essential for a certain type of endocytosis process, is facilitated at integrin-mediated active regions. To study this, we propose a minimal exactly solvable model which includes the interplay of stochastic shuttling between integrin on and off states with the intrinsic dynamics of the membrane. We propose a two-step mechanism in which the integrin induces an aster-like arrangement in the actin network, followed by clustering of lipids in that region. We obtain an analytic expression for the deformation and local membrane velocity, and thereby the evolution of clustering mediated by a single integrin. The deformation evolves nonmonotonically and its dependence on the stochastic shuttling timescales and membrane properties is elucidated. Our estimates of the area of the deformed region and the number of lipids in it indicate strong clustering.