ArticleThe Journal of cell biology1988
Identification of a polyphosphoinositide-modulated domain in gelsolin which binds to the sides of actin filaments.
Article in The Journal of cell biology, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 149 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
- Dysregulation of the actin scavenging system and inhibition of DNase activity following severe thermal injury.The British journal of surgery · 2020Article
- Gelsolin-Like Domain 3 Plays Vital Roles in Regulating the Activities of the Lily Villin/Gelsolin/Fragmin Superfamily.PloS one · 2015Article
- Article
- S100A11 is required for efficient plasma membrane repair and survival of invasive cancer cells.Nature communications · 2014Article
- Overexpression of Rhodobacter sphaeroides PufX-bearing maltose-binding protein and its effect on the stability of reconstituted light-harvesting core antenna complex.Photosynthesis research · 2012Article
- ACTIN BINDING PROTEIN 29 from Lilium pollen plays an important role in dynamic actin remodeling.The Plant cell · 2007Article
- H-prune-nm23-H1 protein complex and correlation to pathways in cancer metastasis.Journal of bioenergetics and biomembranes · 2006Article
- Mutational analysis of human profilin I reveals a second PI(4,5)-P2 binding site neighbouring the poly(L-proline) binding site.BMC biochemistry · 2002Article
- Actin dynamics in platelets.International review of cytology · 2002Review
- Determination of the gelsolin binding site on F-actin: implications for severing and capping.Biophysical journal · 1998Article
- Gelsolin modulates phospholipase C activity in vivo through phospholipid binding.The Journal of cell biology · 1997Article
- Refined structure of villin 14T and a detailed comparison with other actin-severing domains.Protein science : a publication of the Protein Society · 1997Article
- A role for gelsolin in actuating epidermal growth factor receptor-mediated cell motility.The Journal of cell biology · 1996Article
- A gelsolin-related protein from lobster muscle: cloning, sequence analysis and expression.The Biochemical journal · 1995Article
- Molecular cloning and functional expression of chromaffin cell scinderin indicates that it belongs to the family of Ca(2+)-dependent F-actin severing proteins.Molecular and cellular biochemistry · 1994Article
- Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis.The Journal of cell biology · 1994Article
- SAC1p is an integral membrane protein that influences the cellular requirement for phospholipid transfer protein function and inositol in yeast.The Journal of cell biology · 1993Article
- Changes in mobility of chromaffin granules in actin network with its assembly and Ca(2+)-dependent disassembly by gelsolin.Biophysical journal · 1993Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
Gelsolin is a Ca2+- and polyphosphoinositide-modulated actin-binding protein which severs actin filaments, nucleates actin assembly, and caps the "barbed" end of actin filaments. Proteolytic cleavage analysis of human plasma gelsolin has shown that the NH2-terminal half of the molecule severs actin filaments almost as effectively as native gelsolin in a Ca2+-insensitive but polyphosphoinositide-inhibited manner. Further proteolysis of the NH2-terminal half generates two unique fragments (CT14N and CT28N), which have minimal severing activity. Under physiological salt conditions, CT14N binds monomeric actin coupled to Sepharose but CT28N does not. In this paper, we show that CT28N binds stoichiometrically and with high affinity to actin subunits in filaments, suggesting that it preferentially recognizes the conformation of polymerized actin. Analysis of the binding data shows that actin filaments have one class of CT28N binding sites with Kd = 2.0 X 10(-7) M, which saturates at a CT28N/actin subunit ratio of 0.8. Binding of CT28N to actin filaments is inhibited by phosphatidylinositol 4,5-bisphosphate micelles. In contrast, neither CT14N nor another actin-binding domain located in the COOH-terminal half of gelsolin form stable stoichiometric complexes with actin along the filaments, and their binding to actin monomers is not inhibited by PIP2. Based on these observations, we propose that CT28N is the polyphosphoinositide-regulated actin-binding domain which allows gelsolin to bind to actin subunits within a filament before serving.
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