RT Journal Article
SR Electronic
T1 A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth
JF Life Science Alliance
JO Life Sci. Alliance
FD Life Science Alliance LLC
SP e202000813
DO 10.26508/lsa.202000813
VO 3
IS 9
A1 Grinhagens, Sören
A1 Dünkler, Alexander
A1 Wu, Yehui
A1 Rieger, Lucia
A1 Brenner, Philipp
A1 Gronemeyer, Thomas
A1 Mulaw, Medhanie A
A1 Johnsson, Nils
YR 2020
UL http://www.life-science-alliance.org/content/3/9/e202000813.abstract
AB 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.