ArticleBMC biochemistry2002
Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding site.
Article in BMC biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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37 citing papers in PubMed, 89 citations in OpenAlex.
- Cytoskeleton dysfunction of motor neuron in spinal muscular atrophy.Journal of neurology · 2024Review
- Quantitative analysis of septin Cdc10 & Cdc3-associated proteome during stress response in the fungal pathogen Cryptococcus neoformans.PloS one · 2024Article
- Structure of the Monkeypox virus profilin-like protein A42R reveals potential functional differences from cellular profilins.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Taro raphide-associated proteins: Allergens and crystal growth.Plant direct · 2022Article
- Visualizing molecules of functionaleLife · 2022Article
- Detection of structural and conformational changes in ALS-causing mutant profilin-1 with hydrogen/deuterium exchange mass spectrometry and bioinformatics techniques.Metabolic brain disease · 2022Article
- Profilin2 regulates actin rod assembly in neuronal cells.Scientific reports · 2021Article
- The role of profilin-1 in cardiovascular diseases.Journal of cell science · 2021Review
- Profilin Isoforms in Health and Disease - All the Same but Different.Frontiers in cell and developmental biology · 2021Review
- Profilin: many facets of a small protein.Biophysical reviews · 2020Review
- Characterization of a profilin-like protein fromPeerJ · 2020Article
- Interplay between integrins and PI4P5K Sktl is crucial for cell polarization and reepithelialisation during Drosophila wound healing.Scientific reports · 2019Article
- Changes in biophysical characteristics of PFN1 due to mutation causing amyotrophic lateral sclerosis.Metabolic brain disease · 2018Article
- Cofilin and profilin: partners in cancer aggressiveness.Biophysical reviews · 2018Review
- Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.The Journal of biological chemistry · 2018Article
- Quantitative image mean squared displacement (iMSD) analysis of the dynamics of profilin 1 at the membrane of live cells.Methods (San Diego, Calif.) · 2018Article
- Mechanistic principles underlying regulation of the actin cytoskeleton by phosphoinositides.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mutant Profilin1 transgenic mice recapitulate cardinal features of motor neuron disease.Human molecular genetics · 2017Article
- Protein interaction patterns in different cellular environments are revealed by in-cell NMR.Scientific reports · 2015Article
- The Folding process of Human Profilin-1, a novel protein associated with familial amyotrophic lateral sclerosis.Scientific reports · 2015Article
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5 authors at 2 institutions in 1 country.
Funding
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Abstract
backgroundProfilin is a small cytoskeletal protein which interacts with actin, proline-rich proteins and phosphatidylinositol 4,5-bisphosphate (PI(4,5)-P2). Crystallography, NMR and mutagenesis of vertebrate profilins have revealed the amino acid residues that are responsible for the interactions with actin and poly(L-proline) peptides. Although Arg88 of human profilin I was shown to be involved in PI(4,5)-P2-binding, it was suggested that carboxy terminal basic residues may be involved as well.
resultsUsing site directed mutagenesis we have refined the PI(4,5)-P2 binding site of human profilin I. For each mutant we assessed the stability and studied the interactions with actin, a proline-rich peptide and PI(4,5)-P2 micelles. We identified at least two PI(4,5)-P2-binding regions in human profilin I. As expected, one region comprises Arg88 and overlaps with the actin binding site. The second region involves Arg136 in the carboxy terminal helix and neighbours the poly(L-proline) binding site. In addition, we show that adding a small protein tag to the carboxy terminus of profilin strongly reduces binding to poly(L-proline), suggesting local conformational changes of the carboxy terminal alpha-helix may have dramatic effects on ligand binding.
conclusionsThe involvement of the two terminal alpha-helices of profilin in ligand binding imposes important structural constraints upon the functions of this region. Our data suggest a model in which the competitive interactions between PI(4,5)-P2 and actin and PI(4,5)-P2 and poly(L-proline) regulate profilin functions.
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