ArticlePLoS biology2009
Bayesian modeling of the yeast SH3 domain interactome predicts spatiotemporal dynamics of endocytosis proteins.
Article in PLoS biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 109 papers.
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Who cites it
109 citing papers in PubMed, 199 citations in OpenAlex.
- Article
- A protein-fragment complementation assay to quantify synthetic protein scaffold efficiency.Synthetic biology (Oxford, England) · 2026Article
- Article
- Beyond Clathrin: Decoding the Mechanism of Ultrafast Endocytosis.Physiology (Bethesda, Md.) · 2025Review
- Agent-based modelling of the early stages of actin polymerisation required to drive endocytosis in Saccharomyces cerevisiae.Scientific reports · 2025Article
- A global genetic interaction map of a human cell reveals conserved principles of genetic networks.bioRxiv : the preprint server for biology · 2025Article
- Competitive binding of actin and SH3 domains at proline-rich regions of Las17/WASP regulates actin polymerisation.Communications biology · 2025Article
- 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
- Cryptic genetic variation shapes the fate of gene duplicates in a protein interaction network.Nature communications · 2025Article
- Article
- Mechanistic divergences of endocytic clathrin-coated vesicle formation in mammals, yeasts and plants.Journal of cell science · 2024Review
- Cryptic genetic variation shapes the fate of gene duplicates in a protein interaction network.bioRxiv : the preprint server for biology · 2024Article
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 2024Article
- Dissection of the role of a Src homology 3 domain in the evolution of binding preference of paralogous proteins.Genetics · 2024Article
- Parallel Nonfunctionalization of CK1δ/ε Kinase Ohnologs Following a Whole-Genome Duplication Event.Molecular biology and evolution · 2023Article
- Parallel nonfunctionalization of CK1δ/ε kinase ohnologs following a whole-genome duplication event.bioRxiv : the preprint server for biology · 2023Article
- Spatio-temporal regulation of endocytic protein assembly by SH3 domains in yeast.Molecular biology of the cell · 2023Article
- BefA, a microbiota-secreted membrane disrupter, disseminates to the pancreas and increases β cell mass.Cell metabolism · 2022Article
- Essential role of the endocytic site-associated protein Ecm25 in stress-induced cell elongation.Cell reports · 2021Article
- Lipid flippases in polarized growth.Current genetics · 2021Review
49 more citing papers are in PubMed but not listed here.
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Authors and funding
21 authors at 7 institutions in 5 countries.
Funding
Abstract
SH3 domains are peptide recognition modules that mediate the assembly of diverse biological complexes. We scanned billions of phage-displayed peptides to map the binding specificities of the SH3 domain family in the budding yeast, Saccharomyces cerevisiae. Although most of the SH3 domains fall into the canonical classes I and II, each domain utilizes distinct features of its cognate ligands to achieve binding selectivity. Furthermore, we uncovered several SH3 domains with specificity profiles that clearly deviate from the two canonical classes. In conjunction with phage display, we used yeast two-hybrid and peptide array screening to independently identify SH3 domain binding partners. The results from the three complementary techniques were integrated using a Bayesian algorithm to generate a high-confidence yeast SH3 domain interaction map. The interaction map was enriched for proteins involved in endocytosis, revealing a set of SH3-mediated interactions that underlie formation of protein complexes essential to this biological pathway. We used the SH3 domain interaction network to predict the dynamic localization of several previously uncharacterized endocytic proteins, and our analysis suggests a novel role for the SH3 domains of Lsb3p and Lsb4p as hubs that recruit and assemble several endocytic complexes.
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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.