ArticleThe EMBO journal2001
Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions.
Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 184 citations in OpenAlex.
- Negative feedback equalizes polarity sites in a multi-budding yeast.Current biology : CB · 2025Article
- Roles for the canonical polarity machinery in the de novo establishment of polarity in budding yeast spores.Molecular biology of the cell · 2025Article
- Roles for the canonical polarity machinery in thebioRxiv : the preprint server for biology · 2025Article
- Characterization of a novel TFG variant causing autosomal recessive pure hereditary spastic paraplegia.Annals of clinical and translational neurology · 2024Article
- MoScd2 is involved in appressorium formation and pathogenicity via the Pmk1 MAPK pathway in Magnaporthe oryzae.Crop health · 2023Article
- Effect of Flavoring with Rosemary, Lemon and Orange on the Quality, Composition and Biological Properties of Olive Oil: Comparative Study of Extraction Processes.Foods (Basel, Switzerland) · 2023Article
- Vault RNA1-1 riboregulates the autophagic function of p62 by binding to lysine 7 and arginine 21, both of which are critical for p62 oligomerization.RNA (New York, N.Y.) · 2022Article
- Rapid Divergence of Key Spermatogenesis Genes in nasuta-Subgroup of Drosophila.Journal of molecular evolution · 2022Article
- Polarization and cell-fate decision facilitated by the adaptor Ste50p in Saccharomyces cerevisiae.PloS one · 2022Article
- The role of cell division control protein 42 in tumor and non-tumor diseases: A systematic review.Journal of Cancer · 2022Review
- NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology.Antioxidants (Basel, Switzerland) · 2021Review
- Article
- Functions for Cdc42p BEM adaptors in regulating a differentiation-type MAP kinase pathway.Molecular biology of the cell · 2020Article
- Deep Evolutionary History of the Phox and Bem1 (PB1) Domain Across Eukaryotes.Scientific reports · 2020Article
- Optogenetics reveals Cdc42 local activation by scaffold-mediated positive feedback and Ras GTPase.PLoS biology · 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
- Polarity establishment by Cdc42: Key roles for positive feedback and differential mobility.Small GTPases · 2019Review
- Avidity-driven polarity establishment via multivalent lipid-GTPase module interactions.The EMBO journal · 2019Article
- Cell Polarity in Yeast.Annual review of cell and developmental biology · 2017Review
- Cell cycle entry triggers a switch between two modes of Cdc42 activation during yeast polarization.eLife · 2017Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modular domains mediating specific protein-protein interactions play central roles in the formation of complex regulatory networks to execute various cellular activities. Here we identify a novel domain PB1 in the budding yeast protein Bem1p, which functions in polarity establishment, and mammalian p67(phox), which activates the microbicidal phagocyte NADPH oxidase. Each of these specifically recognizes an evolutionarily conserved PC motif to interact directly with Cdc24p (an essential protein for cell polarization) and p40(phox) (a component of the signaling complex for the oxidase), respectively. Swapping the PB1 domain of Bem1p with that of p67(phox), which abolishes its interaction with Cdc24p, confers on cells temperature- sensitive growth and a bilateral mating defect. These phenotypes are suppressed by a mutant Cdc24p harboring the PC motif-containing region of p40(phox), which restores the interaction with the altered Bem1p. This domain-swapping experiment demonstrates that Bem1p function requires interaction with Cdc24p, in which the PB1 domain and the PC motif participate as responsible modules.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.