ArticleThe Journal of cell biology1986
Definition of an N-terminal actin-binding domain and a C-terminal Ca2+ regulatory domain in human brevin.
Article in The Journal of cell biology, 1986. 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, 73 citations in OpenAlex.
- 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
- Calcium-sensitive activity and conformation of Caenorhabditis elegans gelsolin-like protein 1 are altered by mutations in the first gelsolin-like domain.The Journal of biological chemistry · 2011Article
- 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
- A CapG gain-of-function mutant reveals critical structural and functional determinants for actin filament severing.The EMBO journal · 2006Article
- Mini-thin filaments regulated by troponin-tropomyosin.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Visualizing the Ca2+-dependent activation of gelsolin by using synchrotron footprinting.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Purification of native myosin filaments from muscle.Biophysical journal · 2001Article
- Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin.Biophysical journal · 1998Article
- Determination of the gelsolin binding site on F-actin: implications for severing and capping.Biophysical journal · 1998Article
- The Ca(2+)-induced conformational change of gelsolin is located in the carboxyl-terminal half of the molecule.Biophysical journal · 1993Article
- Direct observation of actin filament severing by gelsolin and binding by gCap39 and CapZ.The Journal of cell biology · 1991Article
- Characterization of actin filament severing by actophorin from Acanthamoeba castellanii.The Journal of cell biology · 1991Article
- Gel electrophoresis of native gelsolin and gelsolin-actin complexes.Journal of muscle research and cell motility · 1990Article
- Elastic filaments in skeletal muscle revealed by selective removal of thin filaments with plasma gelsolin.The Journal of cell biology · 1990Article
- Expression of human plasma gelsolin in Escherichia coli and dissection of actin binding sites by segmental deletion mutagenesis.The Journal of cell biology · 1989Article
- Identification of critical functional and regulatory domains in gelsolin.The Journal of cell biology · 1989Article
- Villin sequence and peptide map identify six homologous domains.Proceedings of the National Academy of Sciences of the United States of America · 1988Article
- Gelsolin has three actin-binding sites.The Journal of cell biology · 1988Article
- Localization and mobility of gelsolin in cells.The Journal of cell biology · 1988Article
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Authors and funding
2 authors.
Funding
Abstract
Brevin is a Ca2+-modulated actin-associated protein that will sever F-actin and cap barbed filament ends. Limited proteolysis with chymotrypsin or subtilisin cleaves the molecule approximately in half. Cleavage is approximately 10-fold more rapid in Ca2+ than in EGTA. The two fragments are readily separated from each other and from undigested brevin by high pressure liquid chromatography on a DEAE resin. A 40,000-mol-wt fragment from the N-terminal is not retained by DEAE, while a 45,000-mol-wt C-terminal fragment binds more tightly than brevin. The N-terminal fragment retains approximately 10% of the nucleation activity, caps barbed ends, and retains 50% of the total severing activity defined by dilution induced depolymerization of pyrenyl actin, but, in contrast to brevin, none of these functions are affected by Ca2+. Fluorescent actin binding studies and gel-filtration demonstrate that the 40,000-mol-wt fragment binds two actin monomers. The 45,000-mol-wt C-terminal fragment has no severing, nucleating, or capping activity. Cross-reaction with two monoclonal antibodies against two specific Ca2+-induced conformations of human platelet gelsolin suggest that both Ca2+ binding sites are located on the carboxyl half of the brevin molecule. One epitope, defined as the rapidly exchanging Ca2+ binding site in the gelsolin-actin complex, is lost when a 20,000-mol-wt fragment is cleaved from the carboxyl terminal. The second epitope, related to the poorly exchanging Ca2+ binding site in the complex, is nearer the middle of the brevin molecule.
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