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Article

The beta-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly.

Cell - 28 May 2004

Hertzog Maud, van Heijenoort Carine, Didry Dominique, Gaudier Martin, Coutant Jérôme, Gigant Benoît, Didelot Gérard, Préat Thomas, Knossow Marcel, Guittet Eric, Carlier Marie-France

Abstract excerpt

The widespread beta-thymosin/WH2 actin binding domain has versatile regulatory properties in actin dynamics and motility. beta-thymosins (isolated WH2 domain) maintain monomeric actin in a "sequestered" nonpolymerizable form. In contrast, when repeated in tandem or inserted in modular proteins, the beta-thymosin/WH2 domain promotes actin assembly at filament barbed ends, like profilin. The structural basis for...

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PMID: 15163409
DOI: 10.1016/s0092-8674(04)00403-9

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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