A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth
| Autor: | Grinhagens, Sören, Dünkler, Alexander, Wu, Yehui, Rieger, Lucia, Brenner, Philipp, Gronemeyer, Thomas, Mulaw, Medhanie Assmelash, Johnsson, Nils |
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| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
DDC 540 / Chemistry & allied sciences
Saccharomyces cerevisiae Proteins KINASE CLA4 Protein-protein interactions DISTINCT ROLES Protein-Protein-Wechselwirkung Cell Cycle Proteins Saccharomyces cerevisiae Protein Serine-Threonine Kinases SPLIT-UBIQUITIN SYMMETRY-BREAKING Guanine Nucleotide Exchange Factors Amino Acid Sequence SH3 DOMAIN skin and connective tissue diseases cdc42 GTP-Binding Protein IN-VIVO Research Articles Adaptor Proteins Signal Transducing cdc42 GTP-Binding Protein Saccharomyces cerevisiae Cell Cycle Cell Polarity ddc:540 Saccharomycetales RHO-TYPE GTPASES Broken symmetry (Physics) sense organs EXCHANGE FACTOR CDC24P Cell Division Research Article Protein Binding |
| Zdroj: | Life Science Alliance |
| ISSN: | 2575-1077 |
| Popis: | 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. publishedVersion |
| Databáze: | OpenAIRE |
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