ArticleMolecular and cellular biology2005
Interaction with the SH3 domain protein Bem1 regulates signaling by the Saccharomyces cerevisiae p21-activated kinase Ste20.
Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 56 citations in OpenAlex.
- Agent-based modelling of the early stages of actin polymerisation required to drive endocytosis in Saccharomyces cerevisiae.Scientific reports · 2025Article
- Gain- and loss-of-function alleles within signaling pathways lead to phenotypic diversity among individuals.iScience · 2024Article
- A Protein-Protein Interaction Analysis Suggests a Wide Range of New Functions for the p21-Activated Kinase (PAK) Ste20.International journal of molecular sciences · 2023Article
- A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth.Life science alliance · 2020Article
- Nonstructural NS5A Protein Regulates LIM and SH3 Domain Protein 1 to Promote Hepatitis C Virus Propagation.Molecules and cells · 2020Article
- Functions for Cdc42p BEM adaptors in regulating a differentiation-type MAP kinase pathway.Molecular biology of the cell · 2020Article
- Polarity establishment by Cdc42: Key roles for positive feedback and differential mobility.Small GTPases · 2019Review
- Cell-cycle control of cell polarity in yeast.The Journal of cell biology · 2019Article
- Short linear motifs in intrinsically disordered regions modulate HOG signaling capacity.BMC systems biology · 2018Article
- Heterotrimeric G Protein-coupled Receptor Signaling in Yeast Mating Pheromone Response.The Journal of biological chemistry · 2016Review
- The robustness of a signaling complex to domain rearrangements facilitates network evolution.PLoS biology · 2014Article
- Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways.The Journal of biological chemistry · 2012Article
- A framework for mapping, visualisation and automatic model creation of signal-transduction networks.Molecular systems biology · 2012Article
- 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
- Solution structure of a novel Cdc42 binding module of Bem1 and its interaction with Ste20 and Cdc42.The Journal of biological chemistry · 2010Article
- The Cdc42 effectors Ste20, Cla4, and Skm1 down-regulate the expression of genes involved in sterol uptake by a mitogen-activated protein kinase-independent pathway.Molecular biology of the cell · 2009Article
- Symmetry breaking in the life cycle of the budding yeast.Cold Spring Harbor perspectives in biology · 2009Review
- p21-activated kinases Cla4 and Ste20 regulate vacuole inheritance in Saccharomyces cerevisiae.Eukaryotic cell · 2009Article
- Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex.Current biology : CB · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae PAK (p21-activated kinase) family kinase Ste20 functions in several signal transduction pathways, including pheromone response, filamentous growth, and hyperosmotic resistance. The GTPase Cdc42 localizes and activates Ste20 by binding to an autoinhibitory motif within Ste20 called the CRIB domain. Another factor that functions with Ste20 and Cdc42 is the protein Bem1. Bem1 has two SH3 domains, but target ligands for these domains have not been described. Here we identify an evolutionarily conserved binding site for Bem1 between the CRIB and kinase domains of Ste20. Mutation of tandem proline-rich (PxxP) motifs in this region disrupts Bem1 binding, suggesting that it serves as a ligand for a Bem1 SH3 domain. These PxxP motif mutations affect signaling additively with CRIB domain mutations, indicating that Bem1 and Cdc42 make separable contributions to Ste20 function, which cooperate to promote optimal signaling. This PxxP region also binds another SH3 domain protein, Nbp2, but analysis of bem1Delta versus nbp2Delta strains shows that the signaling defects of PxxP mutants result from impaired binding to Bem1 rather than from impaired binding to Nbp2. Finally, the PxxP mutations also reduce signaling by constitutively active Ste20, suggesting that postactivation functions of PAKs can be promoted by SH3 domain proteins, possibly by colocalizing PAKs with their substrates. The overall results also illustrate how the final signaling function of a protein can be governed by combinatorial addition of multiple, independent protein-protein interaction modules.
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