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Cited by 277

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

Hawkins, M., Pope, B., Maciver, S. K., Weeds, A. G.·1993·Biochemistry
DOI 10.1021/bi00089a014
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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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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
DOI
10.1021/bi00089a014
OpenAlex
W1999350913
Cited by
277
References
36
FWCI
2.78
Type
journal article
Language
en
Open access
closed

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.