The function of biological membranes is controlled by the interaction of the fluid lipid bilayer with various proteins, some of which induce or react to curvature. These proteins can preferentially bind or diffuse towards curved regions of the membrane, induce or stabilize membrane curvature and sequester membrane area into protein-rich curved domains. The resulting tight interplay between mechanics and chemistry is thought to control organelle morphogenesis and dynamics, including traffic, membrane mechanotransduction, or membrane area regulation and tension buffering. Despite all these processes are fundamentally dynamical, previous work has largely focused on equilibrium and a self-consistent theoretical treatment of the dynamics of curvature sensing and generation has been lacking. Here, we develop a general theoretical and computational framework based on a nonlinear Onsager's formalism of irreversible thermodynamics for the dynamics of curved proteins and membranes. We develop variants of the model, one of which accounts for membrane curving by asymmetric crowding of bulky off-membrane protein domains. As illustrated by a selection of test cases, the resulting governing equations and numerical simulations provide a foundation to understand the dynamics of curvature sensing, curvature generation, and more generally membrane curvature mechano-chemistry.To quantitatively understand these phenomena, various biophysical studies have exposed artificial lipid membranes to purified proteins in controlled conditions [14]. At high concentration, curved proteins can induce severe membrane curvature when incubated with liposomes [15], can stabilize membrane tubes [10,16], and can dynamically trigger protein-rich tubular protrusions out of tense vesicles [17][18][19]. At lower concentrations, proteins sense curvature and preferentially adsorb or migrate to favorably curved membranes, as probed in assays involving polydisperse vesicle suspensions [20], vesicles with membrane tethers [18,21] or supported lipid bilayers on wavy substrates [22]. Since protein-rich curved domains sequester apparent membrane area from the adjacent planar membrane, their formation perform work against membrane tension, and thus can be hindered if tension is large enough. This kind of mechano-chemical coupling, tested in vitro by exposing aspirated vesicles to BAR proteins [19], has physiological implications during the mechano-protection of stressed cells by the release of membrane area through disassembly of caveolae [4], or in the regulation of clathrin-mediated endocytosis by membrane tension [23].A number of theoretical and computational studies at various scales have been developed to understand the interaction between curved proteins and membranes. At the nanoscale, all-atom molecular dynamics have described curvature generation by single domains [24] and curvature maintenance by multiple proteins [25]. Reaching a micron, coarse-grained molecular dynamics simulations, treating the membrane either molecularly or as a continuum object, hav...