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Cited by 287

The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.

Formins: signaling effectors for assembly and polarization of actin filaments

Evangelista, Marie, Zigmond, Sally, Boone, Charles·2003·Journal of Cell Science
DOI 10.1242/jcs.00611
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Abstract

Eukaryotic cells require filamentous actin to maintain their shape and for movement, growth and replication. New actin filaments are formed by the cutting of existing filaments or de novo through the action of specialized nucleators. The most highly characterized nucleator is the Arp2/3 complex,which nucleates the branched actin networks in the lamellae of migrating cells. Recently, Bni1p, which is a member of the formin family of proteins,has been shown to nucleate actin filaments in vitro. Formins are implicated in the formation of actin cables in yeast, stress fibers in tissue culture cells and cytokinesis in many cell types. Formins contain two highly conserved formin-homology domains, FH1 and FH2. The Bni1p FH2 domain is sufficient to mediate nucleation. The Bni1p FH1 domain binds profilin, an actin-monomer-binding protein that delivers actin to the growing barbed end of filaments. The Bni1p FH1-profilin interaction enhances nucleation. Formins participate in a number of signaling pathways that control the assembly of specific actin structures and bind the barbed end of actin filaments, thereby providing a cytoskeletal basis for the establishment of cell polarity.

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Metadata

Authors
Evangelista, M., Zigmond, S., & Boone, C.
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2003-07-01
Volume
116
Issue
13
Pages
2603-2611
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
DOI
10.1242/jcs.00611
OpenAlex
W2074622507
Cited by
287
References
90
FWCI
11.05
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).

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