ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregation Article Swipe
Mahmoud Kiaei
,
Meenakshisundaram Balasubramaniam
,
Vivek Govind Kumar
,
Robert J. Shmookler Reis
,
Mahmoud Moradi
,
Kottayil I. Varughese
·
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-018-31199-7
YOU?
·
· 2018
· Open Access
·
· DOI: https://doi.org/10.1038/s41598-018-31199-7
Profilin-1 (PFN1) is a 140-amino-acid protein with two distinct binding sites―one for actin and one for poly-L-proline (PLP). The best-described function of PFN1 is to catalyze actin elongation and polymerization. Thus far, eight DNA mutations in the PFN1 gene encoding the PFN1 protein are associated with human amyotrophic lateral sclerosis (ALS). We and others recently showed that two of these mutations (Gly118Val or G118V and Cys71Gly or C71G) cause ALS in rodents. In vitro studies suggested that Met114Thr and Thr109Met cause the protein to behave abnormally and cause neurotoxicity. The mechanism by which a single amino acid change in human PFN1 causes the degeneration of motor neurons is not known. In this study, we investigated the structural perturbations of PFN1 caused by each ALS-associated mutation. We used molecular dynamics simulations to assess how these mutations alter the secondary and tertiary structures of human PFN1. Herein, we present our in silico data and analysis on the effect of G118V and T109M mutations on PFN1 and its interactions with actin and PLP. The substitution of valine for glycine reduces the conformational flexibility of the loop region between the α-helix and β-strand and enhances the hydrophobicity of the region. Our in silico analysis of T109M indicates that this mutation alters the shape of the PLP-binding site and reduces the flexibility of this site. Simulation studies of PFN1 in its wild type (WT) and mutant forms (both G118V and T109M mutants) revealed differential fluctuation patterns and the formation of salt bridges and hydrogen bonds between critical residues that may shed light on differences between WT and mutant PFN1. In particular, we hypothesize that the flexibility of the actin- and PLP-binding sites in WT PFN1 may allow the protein to adopt slightly different conformations in its free and bound forms. These findings provide new insights into how each of these mutations in PFN1 might increase its propensity for misfolding and aggregation, leading to its dysfunction.
Related Topics
Concepts
In silico
Mutant
Mutation
Tropomyosin
Mutagenesis
Chemistry
Point mutation
Biophysics
Amino acid
Actin
Biochemistry
Gene
Biology
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1038/s41598-018-31199-7
- https://www.nature.com/articles/s41598-018-31199-7.pdf
- OA Status
- gold
- Cited By
- 19
- References
- 31
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W2888551664
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W2888551664Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1038/s41598-018-31199-7Digital Object Identifier
- Title
-
ALS-causing mutations in profilin-1 alter its conformational dynamics: A computational approach to explain propensity for aggregationWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
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2018Year of publication
- Publication date
-
2018-08-24Full publication date if available
- Authors
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Mahmoud Kiaei, Meenakshisundaram Balasubramaniam, Vivek Govind Kumar, Robert J. Shmookler Reis, Mahmoud Moradi, Kottayil I. VarugheseList of authors in order
- Landing page
-
https://doi.org/10.1038/s41598-018-31199-7Publisher landing page
- PDF URL
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https://www.nature.com/articles/s41598-018-31199-7.pdfDirect link to full text PDF
- Open access
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YesWhether a free full text is available
- OA status
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goldOpen access status per OpenAlex
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https://www.nature.com/articles/s41598-018-31199-7.pdfDirect OA link when available
- Concepts
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In silico, Mutant, Mutation, Tropomyosin, Mutagenesis, Chemistry, Point mutation, Biophysics, Amino acid, Actin, Biochemistry, Gene, BiologyTop concepts (fields/topics) attached by OpenAlex
- Cited by
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19Total citation count in OpenAlex
- Citations by year (recent)
-
2025: 1, 2023: 2, 2022: 5, 2021: 6, 2019: 5Per-year citation counts (last 5 years)
- References (count)
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31Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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| cited_by_percentile_year.max | 98 |
| cited_by_percentile_year.min | 91 |
| corresponding_author_ids | https://openalex.org/A5048852196 |
| countries_distinct_count | 1 |
| institutions_distinct_count | 6 |
| corresponding_institution_ids | https://openalex.org/I79620101 |
| citation_normalized_percentile.value | 0.84658307 |
| citation_normalized_percentile.is_in_top_1_percent | False |
| citation_normalized_percentile.is_in_top_10_percent | False |