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Phosphatidylinositol-dependent actin filament binding by the SWI/SNF-like BAF chromatin remodeling complex

By Oliver J. Rando, Keji Zhao, Paul Janmey and Gerald R. Crabtree


Recently, several chromatin remodeling complexes in yeast, Drosophila, and mammals have been shown to contain actin and actin-related proteins (arps). However, the function of actin in these complexes is unclear. Here, we show that the mammalian SWI/SNF-like BAF complex binds to phosphatidylinositol 4,5-bisphosphate (PIP2) micelles and PIP2-containing mixed lipid vesicles, and that PIP2 binding allows the complex to associate with actin pointed ends and branch points. Actin binds to at least two distinct domains in the C terminus of the Brg1 protein, and interaction with only one of these domains is sensitive to PIP2. Based on these findings, we propose a model for PIP2 activation of actin binding by relief of intramolecular capping of actin by Brg1

Topics: Biological Sciences
Publisher: The National Academy of Sciences
Year: 2002
DOI identifier: 10.1073/pnas.032662899
OAI identifier:
Provided by: PubMed Central
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