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Control of actin reorganization by Slingshot, a family of phosphatases that dephosphorylate ADF/cofilin.

The ADF (actin-depolymerizing factor)/cofilin family is a stimulus-responsive mediator of actin dynamics. In contrast to the mechanisms of inactivation of ADF/cofilin by kinases such as LIM-kinase 1 (LIMK1), much less is known about its reactivation through dephosphorylation. Here we report Slingshot (SSH), a family of phosphatases that have the property of F actin binding. In Drosophila, loss of ssh function dramatically increased levels of both F actin and phospho-cofilin (P cofilin) and disorganized epidermal cell morphogenesis. In mammalian cells, human SSH homologs (hSSHs) suppressed LIMK1-induced actin reorganization. Furthermore, SSH and the hSSHs dephosphorylated P cofilin in cultured cells and in cell-free assays. Our results strongly suggest that the SSH family plays a pivotal role in actin dynamics by reactivating ADF/cofilin in vivo.

Pubmed ID: 11832213

Authors

  • Niwa R
  • Nagata-Ohashi K
  • Takeichi M
  • Mizuno K
  • Uemura T

Journal

Cell

Publication Data

January 25, 2002

Associated Grants

None

Mesh Terms

  • Actin Depolymerizing Factors
  • Actins
  • Amino Acid Sequence
  • Animals
  • Cell Line
  • Cell-Free System
  • Destrin
  • Drosophila
  • Drosophila Proteins
  • Embryonic Structures
  • Homeodomain Proteins
  • Humans
  • Immunohistochemistry
  • LIM-Homeodomain Proteins
  • Microfilament Proteins
  • Molecular Sequence Data
  • Phosphoprotein Phosphatases
  • Phosphoric Monoester Hydrolases
  • Phosphorylation
  • Protein Binding
  • Protein-Serine-Threonine Kinases
  • Sequence Alignment
  • Transcription Factors
  • Zyxin