The role of intrinsic disorder in binding of plant microtubule‐associated proteins to the cytoskeleton

Abstract

AbstractMicrotubules (MTs) represent one of the main components of the eukaryotic cytoskeleton and support numerous critical cellular functions. MTs are in principle tube‐like structures that can grow and shrink in a highly dynamic manner; a process largely controlled by microtubule‐associated proteins (MAPs). Plant MAPs are a phylogenetically diverse group of proteins that nonetheless share many common biophysical characteristics and often contain large stretches of intrinsic protein disorder. These intrinsically disordered regions are determinants of many MAP–MT interactions, in which structural flexibility enables low‐affinity protein–protein interactions that enable a fine‐tuned regulation of MT cytoskeleton dynamics. Notably, intrinsic disorder is one of the major obstacles in functional and structural studies of MAPs and represents the principal present‐day challenge to decipher how MAPs interact with MTs. Here, we review plant MAPs from an intrinsic protein disorder perspective, by providing a complete and up‐to‐date summary of all currently known members, and address the current and future challenges in functional and structural characterization of MAPs.