Abstract
Polarized states on the membranes are characterized by focal accumulation of proteins and lipids at local concentrations far exceeding their levels typically found outside of these dense clusters. Principles of thermodynamics argue that formation and maintenance of such structures require continuous expenditure of cellular energy to combat the effect of molecular diffusion that relentlessly dissipates the clusters in favor of the spatially homogeneous state. Small GTPases are known to play a crucial role in the formation of several such polarized states. Their ability to consume stored energy and convert it into a potentially useful work by cyclically hydrolyzing GTP and coupling to various effectors in a nucleotide-dependent way, makes them eligible candidates to fulfill the requirements for the molecules involved in the mechanisms responsible for the maintenance of polarized states. Consistently, continuous nucleotide cycling of small GTPases has been found required for the emergence of structures in several well characterized cases. Despite this general awareness, the detailed molecular mechanisms remain largely unknown. In a recent study, not directly involving small GTPases, we proposed a mechanism explaining the emergence and maintenance of the stable cell-polarity landmark that manifests itself as a protein cluster positioned on the plasma membrane at the growing ends of fission yeast cells. Unexpectedly, this study has suggested a number of striking parallels with the mechanisms based on the activity of small GTPases. These findings highlight common design principles of cellular pattern-forming mechanisms that have been mixed and matched in various combinations in the course of evolution to achieve the same desired outcome-tightly controlled in space and time formation of dense protein clusters.