Sho1p connects the plasma membrane with proteins of the cytokinesis network through multiple isomeric interaction states.

An understanding of cytokinesis at the molecular level requires a detailed description of the protein complexes that perform central activities during this process. The proteins Hof1p, Cyk3p, Inn1p and Myo1p each represent one of the four genetically defined and partially complementary pathways of cytokinesis in the yeast Saccharomyces cerevisiae. Here we show that the osmosensor Sho1p is required for correct cell-cell separation. Shortly before cytokinesis Sho1p sequentially assembles with Hof1p, Inn1p and Cyk3p, into a complex (the HICS complex) that might help to connect the membrane with the actin-myosin ring. The HICS complex is formed exclusively through interactions between three SH3 domains located in Cyk3p, Hof1p and Sho1p, and five acceptor sites found in Cyk3p, Hof1p and Inn1p. Owing to the overlapping binding specificities of its members the HICS complex is best described as ensembles of isomeric interaction states that precisely coordinate the different functions of the interactors during cytokinesis.

A constraint network of interactions: protein-protein interaction analysis of the yeast type II phosphatase Ptc1p and its adaptor protein Nbp2p.

We used a generally applicable strategy to collect and structure the protein interactions of the yeast type II protein phosphatase Ptc1p and its binding partner Nbp2p. The procedure transformed primary unstructured protein interaction data into an ensemble of alternative interaction states. Certain combinations of proteins are allowed in different network configurations. Nbp2p serves as the network hub and brings seven kinases in close contact to Ptc1p. As a consequence, the deletion of NBP2 affects several cellular processes including organelle inheritance and the responses to mating hormone, cell wall stress and high osmolarity; it also impairs the proper execution of the morphogenetic program. Our constraint interaction map provides a basis for understanding a subset of the observed phenotypes and assigns the Ptc1p-Nbp2p module a role in synchronizing the associated kinases during the cell cycle.