ArticleThe Journal of biological chemistry2010
Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- The Yeast Gsk-3 Kinase Mck1 Is Necessary for Cell Wall Remodeling in Glucose-Starved and Cell Wall-Stressed Cells.International journal of molecular sciences · 2025Article
- Article
- Generation and characterization of conditional yeast mutants affecting each of the 2 essential functions of the scaffolding proteins Boi1/2 and Bem1.G3 (Bethesda, Md.) · 2022Article
- Deficiency of GPI Glycan Modification by Ethanolamine Phosphate Results in Increased Adhesion and Immune Resistance ofFrontiers in cellular and infection microbiology · 2021Article
- A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth.Life science alliance · 2020Article
- Functions for Cdc42p BEM adaptors in regulating a differentiation-type MAP kinase pathway.Molecular biology of the cell · 2020Article
- Temporal regulation of cell polarity via the interaction of the Ras GTPase Rsr1 and the scaffold protein Bem1.Molecular biology of the cell · 2019Article
- Short linear motifs in intrinsically disordered regions modulate HOG signaling capacity.BMC systems biology · 2018Article
- Article
- Many roads to symmetry breaking: molecular mechanisms and theoretical models of yeast cell polarity.Molecular biology of the cell · 2017Review
- Heterotrimeric G Protein-coupled Receptor Signaling in Yeast Mating Pheromone Response.The Journal of biological chemistry · 2016Review
- Experimental and computational analysis of a large protein network that controls fat storage reveals the design principles of a signaling network.PLoS computational biology · 2015Article
- Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR.Scientific reports · 2013Article
- SH3 domains: modules of protein-protein interactions.Biophysical reviews · 2013Review
- Distinct peptide binding specificities of Src homology 3 (SH3) protein domains can be determined by modulation of local energetics across the binding interface.The Journal of biological chemistry · 2012Article
- A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.The Journal of biological chemistry · 2011Article
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5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bem1 is a scaffold protein essential for the establishment of cell polarity in Saccharomyces cerevisiae. This work reports the solution structure of a Cdc42 binding module of Bem1 comprising the second SH3 domain (SH3b) and its C-terminal flanking region termed Cdc42 interacting (CI). First, the structure of Bem1 SH3b-CI was determined by NMR spectroscopy, which shows that Bem1 SH3b-CI is a structurally and functionally related domain that binds Cdc42. Next, the solution structure of Bem1 SH3b-CI in complex with the proline-rich region of p21-activated kinase Ste20 (Ste20 PRR) was determined. Finally, the interaction surface of Bem1 SH3b-CI with Cdc42 was identified based on chemical shift perturbation studies which reveals that Bem1 SH3b-CI interacts simultaneously with both Ste20 PRR and Cdc42 using the opposite surfaces. Thus, Bem1 can tether Cdc42 and Ste20 in close proximity so that Cdc42 can efficiently interact with Ste20 Cdc42 and Rac interactive binding (CRIB). Based on the present results together with the previous biochemical studies (Lamson, R. E., Winters, M. J., and Pryciak, P. M. (2002) Mol. Cell. Biol. 22, 2939-2951 and Winters, M. J., and Pryciak, P. M. (2005) Mol. Cell. Biol. 25, 2177-2190), a model was suggested that the autoinhibition of Ste20 kinase activity by CRIB is released through the Cdc42-CRIB interaction, which is mediated by Bem1, and Ste20 is subsequently activated, an initial step for the establishment of the cell polarity.
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