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Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling.

Lymphocyte activation is accompanied by visible changes in chromatin structure. We find that antigen receptor signaling induces the rapid association of the BAF complex with chromatin. PIP2, which is regulated by activation stimuli, is sufficient in vitro to target the BAF complex to chromatin, but it has no effect on related chromatin remodeling complexes containing SNF2L or hISWI. Purification and peptide sequencing of the subunits of the complex revealed beta-actin as well as a novel actin-related protein, BAF53. beta-actin and BAF53 are required for maximal ATPase activity of BRG1 and are also required with BRG1 for association of the complex with chromatin/matrix. This work indicates that membrane signals control the activity of the mammalian SWI/SNF or BAF complex and demonstrates a direct interface between signaling and chromatin regulation.

Pubmed ID: 9845365

Authors

  • Zhao K
  • Wang W
  • Rando OJ
  • Xue Y
  • Swiderek K
  • Kuo A
  • Crabtree GR

Journal

Cell

Publication Data

November 25, 1998

Associated Grants

None

Mesh Terms

  • Actins
  • Adenosine Triphosphatases
  • Animals
  • Cattle
  • Cell Nucleus
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • DNA Helicases
  • DNA-Binding Proteins
  • Humans
  • Jurkat Cells
  • Lymphocyte Activation
  • Macromolecular Substances
  • Mice
  • Molecular Sequence Data
  • Nuclear Proteins
  • Phosphatidylinositol 4,5-Diphosphate
  • Receptors, Antigen, T-Cell
  • Signal Transduction
  • Transcription Factors