Cellular membranes are highly dynamic in shape. They can rapidly and precisely regulate their shape to perform various
cellular functions. The protein’s ability to sense membrane curvature is essential in various biological events such as cell
signaling and membrane trafficking. As they are bound, these curvature-sensing proteins may also change the local membrane
shape by one or more curvature driving mechanisms. Established curvature-sensing/driving mechanisms rely on proteins
with specific structural features such as amphipathic helices and intrinsically curved shapes. However, the recent discovery
and characterization of many proteins have shattered the protein structure–function paradigm, believing that the protein
functions require a unique structural feature. Typically, such structure-independent functions are carried either entirely by
intrinsically disordered proteins or hybrid proteins containing disordered regions and structured domains. It is becoming
more apparent that disordered proteins and regions can be potent sensors/inducers of membrane curvatures. In this article,
we outline the basic features of disordered proteins and regions, the motifs in such proteins that encode the function, mem-
brane remodeling by disordered proteins and regions, and assays that may be employed to investigate curvature sensing and
generation by ordered/disordered proteins.