Symmetry is closely intertwined with the function, genetics, and chemical properties of multiprotein complexes. Here, we explore the relation between structural symmetry and the ability of membrane proteins to sense and induce membrane curvature, which is a key factor for modulating the shape URLanization of cell membranes. Using coarse-grained simulations and elasticity theory, we show that the potential for direction-dependent membrane curvature sensing is limited to asymmetric proteins, dimers, and tetramers  . Odd and higher-order symmetries strongly suppress directional curvature sensing. This classification gives a new perspective on the structure-function relation for membrane proteins, and simplifies the task of translating between molecular sensing mechanisms and  large-scale cellular consequences.
Symmetry is closely intertwined with the function, genetics, and chemical properties of multiprotein complexes. Here, we explore the relation between structural symmetry and the ability of membrane proteins to sense and induce membrane curvature, which is a key factor for modulating the shape URLanization of cell membranes. Using coarse-grained simulations and elasticity theory, we show that the potential for direction-dependent membrane curvature sensing is limited to asymmetric proteins, dimers, and tetramers , and argue that one should expect this anisotropy to be strongest for dimers . Odd and higher-order symmetries strongly suppress directional curvature sensing. This classification gives a new perspective on the structure-function relation for membrane proteins, and simplifies the task of translating between molecular sensing mechanisms and their large-scale cellular consequences.
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, and argue that one should expect this anisotropy to be strongest for dimers
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their