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Cited by 329

The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.

Effects of cytochalasin, phalloidin and pH on the elongation of actin filaments

Sampath, Prakash, Pollard, Thomas D.·1991·Biochemistry
DOI 10.1021/bi00221a034
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Abstract

We used electron microscopy to measure the effects of cytochalasins, phalloidin, and pH on the rates of elongation at the barbed and pointed ends of actin filaments. In the case of the cytochalasins, we compared the effects on ATP- and ADP-actin monomers. Micromolar concentrations of either cytochalasin B (CB) or cytochalasin D (CD) inhibit elongation at both ends of the filament, about 95% at the barbed end and 50% at the pointed end, so that the two ends contribute about equally to the rate of growth. Half-maximal inhibition of elongation at the barbed end is at 0.1 microM CB and 0.02 microM CD for ATP-actin and at 0.1 microM CD for ADP-actin. At the pointed end, CD inhibits elongation by ATP-actin and ADP-actin about equally. At high (2 microM) concentrations, the cytochalasins reduce the association and dissociation rate constants in parallel for both ADP- and ATP-actin, so their effects on the critical concentrations are minimal. These observations confirm and extend those of Bonder and Mooseker [Bonder, E. M., & Mooseker, M. S. (1986) J. Cell Biol. 102, 282-288]. The dependence of the elongation rate on the concentration of both cytochalasin and actin can be explained quantitatively by a mechanism that includes the effects of cytochalasin binding to actin monomers [Godette, D. W., & Frieden, C. (1986) J. Biol. Chem. 261, 5974-5980] and a partial cap of the barbed end of the filament by the complex of ADP-actin and cytochalasin.(ABSTRACT TRUNCATED AT 250 WORDS)

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Metadata

Authors
Sampath, P., & Pollard, T. D.
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
1991-02-19
Volume
30
Issue
7
Pages
1973-1980
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi00221a034
OpenAlex
W2124754800
Cited by
329
References
26
FWCI
3.75
Type
journal article
Language
en
Open access
closed

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