ArticleGenetics2007
The biologically relevant targets and binding affinity requirements for the function of the yeast actin-binding protein 1 Src-homology 3 domain vary with genetic context.
Article in Genetics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- In silico evaluation and therapeutic targeting of LVDD9B protein for WSSV inhibition: molecular and ecological insights for aquaculture solutions.In silico pharmacology · 2025Article
- Activation of caspase-9 on the apoptosome as studied by methyl-TROSY NMR.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Exploiting conformational dynamics to modulate the function of designed proteins.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Spatio-temporal regulation of endocytic protein assembly by SH3 domains in yeast.Molecular biology of the cell · 2023Article
- A disordered encounter complex is central to the yeast Abp1p SH3 domain binding pathway.PLoS computational biology · 2020Article
- Measurement of protein backboneJournal of biomolecular NMR · 2017Article
- Article
- Fractional enrichment of proteins using [2-(13)C]-glycerol as the carbon source facilitates measurement of excited state 13Cα chemical shifts with improved sensitivity.Journal of biomolecular NMR · 2015Article
- Actin and endocytosis in budding yeast.Genetics · 2015Review
- A semi-automated method for purification of milligram quantities of proteins on the QIAcube.Protein expression and purification · 2014Article
- The importance of conserved features of yeast actin-binding protein 1 (Abp1p): the conditional nature of essentiality.Genetics · 2012Article
- Yeast adaptor protein, Nbp2p, is conserved regulator of fungal Ptc1p phosphatases and is involved in multiple signaling pathways.The Journal of biological chemistry · 2012Article
- Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R(1ρ): an application to αB-crystallin.Journal of biomolecular NMR · 2012Article
- Differential dynamic engagement within 24 SH3 domain: peptide complexes revealed by co-linear chemical shift perturbation analysis.PloS one · 2012Article
- Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods.Journal of biomolecular NMR · 2010Article
- Structural, functional, and bioinformatic studies demonstrate the crucial role of an extended peptide binding site for the SH3 domain of yeast Abp1p.The Journal of biological chemistry · 2009Article
- Measuring 13Cbeta chemical shifts of invisible excited states in proteins by relaxation dispersion NMR spectroscopy.Journal of biomolecular NMR · 2009Article
- The SH3 domains of two PCH family members cooperate in assembly of the Schizosaccharomyces pombe contractile ring.The Journal of cell biology · 2009Article
- Isotope labeling methods for studies of excited protein states by relaxation dispersion NMR spectroscopy.Nature protocols · 2009Article
- Measurement of carbonyl chemical shifts of excited protein states by relaxation dispersion NMR spectroscopy: comparison between uniformly and selectively (13)C labeled samples.Journal of biomolecular NMR · 2008Article
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Authors and funding
6 authors.
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Abstract
Many protein-protein interaction domains bind to multiple targets. However, little is known about how the interactions of a single domain with many proteins are controlled and modulated under varying cellular conditions. In this study, we investigated the in vivo effects of Abp1p SH3 domain mutants that incrementally reduce target-binding affinity in four different yeast mutant backgrounds in which Abp1p activity is essential for growth. Although the severity of the phenotypic defects observed generally increased as binding affinity was reduced, some genetic backgrounds (prk1 Delta and sla1 Delta) tolerated large affinity reductions while others (sac6 Delta and sla2 Delta) were much more sensitive to these reductions. To elucidate the mechanisms behind these observations, we determined that Ark1p is the most important Abp1p SH3 domain interactor in prk1 Delta cells, but that interactions with multiple targets, including Ark1p and Scp1p, are required in the sac6 Delta background. We establish that the Abp1p SH3 domain makes different, functionally important interactions under different genetic conditions, and these changes in function are reflected by changes in the binding affinity requirement of the domain. These data provide the first evidence of biological relevance for any Abp1p SH3 domain-mediated interaction. We also find that considerable reductions in binding affinity are tolerated by the cell with little effect on growth rate, even when the actin cytoskeletal morphology is significantly perturbed.
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