ArticleThe Journal of cell biology1992
Are the conserved sequences in segment 1 of gelsolin important for binding actin?
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 45 citations in OpenAlex.
- DeActs: genetically encoded tools for perturbing the actin cytoskeleton in single cells.Nature methods · 2017Article
- Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping.PLoS biology · 2010Article
- A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.Cellular and molecular life sciences : CMLS · 2010Article
- Recruitment of the SWI/SNF chromatin remodeling complex to steroid hormone-regulated promoters by nuclear receptor coactivator flightless-I.The Journal of biological chemistry · 2009Article
- The actin binding domain of ACF7 binds directly to the tetratricopeptide repeat domains of rapsyn.Neuroscience · 2007Article
- Separate functions of gelsolin mediate sequential steps of collagen phagocytosis.Molecular biology of the cell · 2005Article
- Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity.Molecular and cellular biology · 2004Article
- The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Article
- A 205 kDa protein from non-neuronal cells in culture contains tubulin binding epitopes.Molecular and cellular biochemistry · 1995Article
- A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.The Biochemical journal · 1995Article
- Identification of secreted and cytosolic gelsolin in Drosophila.The Journal of cell biology · 1994Article
- The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity.The Journal of cell biology · 1994Article
- Solution structure of villin 14T, a domain conserved among actin-severing proteins.Protein science : a publication of the Protein Society · 1994Article
- The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule.Biophysical journal · 1993Article
- Definition of the EGTA-independent interface involved in the serum gelsolin-actin complex.The Biochemical journal · 1993Article
- Dominant negative mutation in cell surface beta 1,4-galactosyltransferase inhibits cell-cell and cell-matrix interactions.The Journal of cell biology · 1993Article
- Evidence for functional homology in the F-actin binding domains of gelsolin and alpha-actinin: implications for the requirements of severing and capping.The Journal of cell biology · 1992Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The minimal region required for actin binding in the smallest of the three domains of gelsolin (termed Segment 1 or S1) was previously defined by deletion mutagenesis as residues 37-126. Further analysis of NH2-terminal deletions here redefines the minimal functional core as residues 41-126. Amino acid substitutions within this core further elucidate the nature of the interaction of segment 1 with actin. Of 26 point mutants analyzed, 14 reduced the affinity for actin. The charged residues His 119, Arg 120, Glu 121, and Gln 123 appear to be involved in direct interaction with actin. Substitutions of Leu 108, Leu 112, and Val 117 by polar groups all affect the structural stability of segment 1 and thereby reduce binding affinity. In addition replacement of Glu 126 by aspartic acid modifies the physical properties of segment 1 and weakens binding. We have further shown that changing charged residues within the highly conserved pentapeptide sequence LDDYL (residues 108-112) has no effect on actin binding. This sequence, found in a number of different actin binding proteins, does not therefore constitute part of the interaction site. Similarly, substitution of the two acidic residues by basic ones within the DESG motif of segment 1 (residues 96-99, but also found near the COOH terminus of actin) does not impair binding. These results show the dangers of predicting functional sites on the basis of conserved sequences.
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