ArticleThe Journal of cell biology1989
Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis.
Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 194 citations in OpenAlex.
- Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025Article
- Novel inter-domain CaJournal of muscle research and cell motility · 2020Review
- Biophysical properties of human β-cardiac myosin with converter mutations that cause hypertrophic cardiomyopathy.Science advances · 2017Article
- The molecular chaperone CCT modulates the activity of the actin filament severing and capping protein gelsolin in vitro.Cell stress & chaperones · 2016Article
- Contractility parameters of human β-cardiac myosin with the hypertrophic cardiomyopathy mutation R403Q show loss of motor function.Science advances · 2015Article
- Flightless I interacts with NMMIIA to promote cell extension formation, which enables collagen remodeling.Molecular biology of the cell · 2015Article
- Global shapes of F-actin depolymerization-competent minimal gelsolins: insight into the role of g2-g3 linker in pH/Ca2+ insensitivity of the first half.The Journal of biological chemistry · 2013Article
- Molecular consequences of the R453C hypertrophic cardiomyopathy mutation on human β-cardiac myosin motor function.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Regulatory role of the second gelsolin-like domain of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) in its calcium-dependent conformation and actin-regulatory activities.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Collagen remodeling by phagocytosis is determined by collagen substrate topology and calcium-dependent interactions of gelsolin with nonmuscle myosin IIA in cell adhesions.Molecular biology of the cell · 2013Article
- Functional characterization of the human α-cardiac actin mutations Y166C and M305L involved in hypertrophic cardiomyopathy.Cellular and molecular life sciences : CMLS · 2012Article
- Arabidopsis VILLIN2 and VILLIN3 are required for the generation of thick actin filament bundles and for directional organ growth.Plant physiology · 2012Article
- Gelsolin and non-muscle myosin IIA interact to mediate calcium-regulated collagen phagocytosis.The Journal of biological chemistry · 2011Article
- Conformational dynamics of actin: effectors and implications for biological function.Cytoskeleton (Hoboken, N.J.) · 2010Review
- A llama-derived gelsolin single-domain antibody blocks gelsolin-G-actin interaction.Cellular and molecular life sciences : CMLS · 2010Article
- Caenorhabditis elegans gelsolin-like protein 1 is a novel actin filament-severing protein with four gelsolin-like repeats.The Journal of biological chemistry · 2008Article
- The unique insert at the end of the myosin VI motor is the sole determinant of directionality.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Structural analysis of an Echinococcus granulosus actin-fragmenting protein by small-angle x-ray scattering studies and molecular modeling.Biophysical journal · 2006Article
- Separate functions of gelsolin mediate sequential steps of collagen phagocytosis.Molecular biology of the cell · 2005Article
- Gelsolin binds to polyphosphoinositide-free lipid vesicles and simultaneously to actin microfilaments.The Biochemical journal · 2005Article
3 more citing papers are in PubMed but not listed here.
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Human plasma gelsolin has been expressed in high yield and soluble form in Escherichia coli. The protein has nucleating and severing activities identical to those of plasma gelsolin and is fully calcium sensitive in its interactions with monomeric actin. A number of deletion mutants have been expressed to explore the function of the three actin binding sites. Their design is based on the sixfold segmental repeat in the protein sequence. (These sites are located in segment 1, segments 2-3, and segments 4-6). Two mutants, S1-3 and S4-6, are equivalent to the NH2- and COOH-terminal halves of the molecule obtained by limited proteolysis. S1-3 binds two actin monomers in the presence or absence of calcium, it severs and caps filaments but does not nucleate polymerization. S4-6 binds a single actin monomer but only in calcium. These observations confirm and extend current knowledge on the properties of the two halves of gelsolin. Two novel constructs have also been studied that provide a different pairwise juxtaposition of the three sites. S2-6, which lacks the high affinity site of segment 1 (equivalent to the 14,000-Mr proteolytic fragment) and S1,4-6, which lacks segments 2-3 (the actin filament binding domain previously identified using the 28,000-Mr proteolytic fragment). S2-6 binds two actin monomers in calcium and nucleates polymerization; it associates laterally with filaments in the presence or absence of calcium and has a weak calcium-dependent fragmenting activity. S1,4-6 also binds two actin monomers in calcium and one in EGTA, has weak severing activity but does not nucleate polymerization. A model is presented for the involvement of the three binding sites in the various activities of gelsolin.
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