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PMID: 16829561 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Conformational changes in actin filaments induced by formin binding to the barbed end.

Biophysical journal ·Vol. 91 ·No. 7 ·2006-10-01 ·Pages 2564-72

Papp G, Bugyi B, Ujfalusi Z, Barkó S, Hild G, Somogyi B, Nyitrai M

Abstract

Formins bind actin filaments and play an essential role in the regulation of the actin cytoskeleton. In this work we describe details of the formin-induced conformational changes in actin filaments by fluorescence-lifetime and anisotropy-decay experiments. The results show that the binding of the formin homology 2 domain of a mammalian formin (mouse mDia1) to actin filaments resulted in a less rigid protein structure in the microenvironment of the Cys374 of actin, weakening of the interactions between neighboring actin protomers, and greater overall flexibility of the actin filaments. The formin effect is smaller at greater ionic strength. The results show that formin binding to the barbed end of actin filaments is responsible for the increase of flexibility of actin filaments. One formin dimer can affect the dynamic properties of an entire filament. Analyses of the results obtained at various formin/actin concentration ratios indicate that at least 160 actin protomers are affected by the binding of a single formin dimer to the barbed end of a filament.

MeSH Terms
Actin Cytoskeleton/chemistry Allosteric Regulation Carrier Proteins/chemistry Dimerization Fluorescence Formins Models, Molecular Osmolar Concentration Protein Binding Protein Conformation Protein Structure, Tertiary
Chemicals
Carrier Proteins Diap1 protein, mouse Formins
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Papp Gábor
Department of Biophysics, Faculty of Medicine, Office for Academy Research Groups, University of Pécs, Pécs, Hungary.
Bugyi Beáta
Ujfalusi Zoltán
Barkó Szilvia
Hild Gábor
Somogyi Béla
Nyitrai Miklós
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Article Info
Journal
Biophysical journal
Abbr.
Biophys J
ISSN
0006-3495
DOI
10.1529/biophysj.106.087775
Published
2006-10-01
Epub
2006-00-07
Pages
2564-72
Language
English
Region
United States
NLM ID
0370626
PMCID
PMC1562385
Subset
IM
Grants
Wellcome Trust · 079003 · United Kingdom
External Links
PubMed source DOI: 10.1529/biophysj.106.087775 PMC Full Text View journal details
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