Polycomb group protein Ezh2 controls actin polymerization and cell signaling Journal Article


Authors: Su, I. H.; Dobenecker, M. W.; Dickinson, E.; Oser, M.; Basavaraj, A.; Marqueron, R.; Viale, A.; Reinberg, D.; Wülfing, C.; Tarakhovsky, A.
Article Title: Polycomb group protein Ezh2 controls actin polymerization and cell signaling
Abstract: Polycomb group protein Ezh2, one of the key regulators of development in organisms from flies to mice, exerts its epigenetic function through regulation of histone methylation. Here, we report the existence of the cytosolic Ezh2-containing methyltransferase complex and tie the function of this complex to regulation of actin polymerization in various cell types. Genetic evidence supports the essential role of cytosolic Ezh2 in actin polymerization-dependent processes such as antigen receptor signaling in T cells and PDGF-induced dorsal circular ruffle formation in fibroblasts. Revealed function of Ezh2 points to a broader usage of lysine methylation in regulation of both nuclear and extra-nuclear signaling processes. Copyright ©2005 by Elsevier Inc.
Keywords: signal transduction; platelet derived growth factor; controlled study; unclassified drug; human cell; dna-binding proteins; proto-oncogene proteins; nonhuman; protein function; protein localization; cell proliferation; t-lymphocytes; proteins; animal cell; mouse; animals; cell cycle proteins; mice; complex formation; embryo; protein; cell differentiation; mice, inbred c57bl; cell type; mice, transgenic; transcription factors; antigen presentation; lymphocyte activation; methyltransferase; regulatory mechanism; receptors, antigen, t-cell; thymus gland; carrier proteins; platelet-derived growth factor; fibroblast; fibroblasts; cellular distribution; cytoplasm; actins; repressor proteins; actin polymerization; cytosol; protein methylation; protein cdc42; jurkat cells; protein methyltransferases; cdc42 gtp-binding protein; proto-oncogene proteins c-vav; polycomb group protein ezh2
Journal Title: Cell
Volume: 121
Issue: 3
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 2005-05-06
Start Page: 425
End Page: 436
Language: English
DOI: 10.1016/j.cell.2005.02.029
PUBMED: 15882624
PROVIDER: scopus
DOI/URL:
Notes: --- - "Cited By (since 1996): 107" - "Export Date: 24 October 2012" - "CODEN: CELLB" - "Source: Scopus"
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  1. Agnes Viale
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