The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
Human actin depolymerizing factor mediates a pH-sensitive destruction of actin filaments
Abstract
ADF (actin depolymerizing factor) is an M(r) 19,000 actin-binding protein present in many vertebrate tissues and particularly abundant in neuronal cells. We have cloned human ADF and here show it to be identical in sequence to porcine destrin. Human ADF expressed in Escherichia coli behaves like native ADF from porcine brain. It binds to G-actin at pH 8 with a 1:1 stoichiometry and Kd approximately 0.2 microM, thereby sequestering monomers and preventing polymerization. It does not cosediment with F-actin at this pH, but severs actin filaments in a calcium-insensitive manner. The severing activity is only about 0.1% efficient. By contrast, at pH values below 7, ADF binds to actin filaments in a highly cooperative manner and at a 1:1 ratio to filament subunits. When the pH is raised to 8.0, the decorated filaments are rapidly severed and depolymerized.
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Cites
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Cited by
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Reactivation of Phosphorylated Actin Depolymerizing Factor and Identification of the Regulatory Site
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Metadata
- Authors
- Hawkins, M., Pope, B., Maciver, S. K., & Weeds, A. G.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1993-09-28
- Volume
- 32
- Issue
- 38
- Pages
- 9985-9993
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W1999350913
- Cited by
- 277
- References
- 36
- FWCI
- 2.78
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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