Journal Article

A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth

Wu, Yehui, Johnsson, Nils, Dünkler, Alexander, Gronemeyer, Thomas, Brenner, Philipp, Mulaw, Medhanie A, Grinhagens, Sören, Rieger, Lucia

2020

Overview

Cdc42 organizes cellular polarity and directs the formation of cellular structures in many organisms. By locating Cdc24, the source of active Cdc42, to the growing front of the yeast cell, the scaffold protein Bem1, is instrumental in shaping the cellular gradient of Cdc42. This gradient instructs bud formation, bud growth, or cytokinesis through the actions of a diverse set of effector proteins. To address how Bem1 participates in these transformations, we systematically tracked its protein interactions during one cell cycle to define the ensemble of Bem1 interaction states for each cell cycle stage. Mutants of Bem1 that interact with only a discrete subset of the interaction partners allowed to assign specific functions to different interaction states and identified the determinants for their cellular distributions. The analysis characterizes Bem1 as a cell cycle–specific shuttle that distributes active Cdc42 from its source to its effectors. It further suggests that Bem1 might convert the PAKs Cla4 and Ste20 into their active conformations.

• Publisher: Life Science Alliance,Life Science Alliance LLC
• Subject: Adaptor Proteins, Signal Transducing - chemistry / Adaptor Proteins, Signal Transducing - metabolism / Adaptor Proteins, Signal Transducing - physiology / Amino Acid Sequence - genetics / Bem1 protein / Binding sites / cdc42 GTP-Binding Protein - genetics / cdc42 GTP-Binding Protein - metabolism / cdc42 GTP-Binding Protein - physiology / cdc42 GTP-Binding Protein, Saccharomyces cerevisiae - genetics / cdc42 GTP-Binding Protein, Saccharomyces cerevisiae - metabolism / Cdc42 protein / Cell Cycle / Cell Cycle Proteins - chemistry / Cell Division / Cell growth / Cell Polarity / Cytokinesis / Guanine Nucleotide Exchange Factors - metabolism / Kinases / Protein Binding - physiology / Protein interaction / Protein Serine-Threonine Kinases - chemistry / Proteins / Saccharomyces cerevisiae - metabolism / Saccharomyces cerevisiae Proteins - metabolism / Saccharomyces cerevisiae Proteins - physiology / Saccharomycetales - metabolism / Yeast