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Binding of the WASP/N-WASP-Interacting Protein WIP to Actin Regulates Focal Adhesion Assembly and Adhesion

Narayanaswamy Ramesh, Michel J. Massaad, Lalit Kumar, Suresh Koduru, Yoji Sasahara, Ines Anton, Manoj Bhasin, Towia Libermann, Raif Geha
Narayanaswamy Ramesh
aDivision of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, USA
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Michel J. Massaad
aDivision of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, USA
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Lalit Kumar
aDivision of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, USA
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Suresh Koduru
aDivision of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, USA
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Yoji Sasahara
bDepartment of Pediatrics, Tohoku University Graduate School of Medicine, Miyagi, Japan
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Ines Anton
cCentro Nacional de Biotecnología (CNB-CSIC), Madrid, Spain
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Manoj Bhasin
dBIDMC Genomics and Proteomics Center and Division of Interdisciplinary Medicine and Biotechnology, Beth Israel Deaconess Medical Center, and Department of Medicine, Harvard Medical School, Boston, Massachusetts, USA
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Towia Libermann
dBIDMC Genomics and Proteomics Center and Division of Interdisciplinary Medicine and Biotechnology, Beth Israel Deaconess Medical Center, and Department of Medicine, Harvard Medical School, Boston, Massachusetts, USA
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Raif Geha
aDivision of Immunology, Children's Hospital, and Department of Pediatrics, Harvard Medical School, Boston, Massachusetts, USA
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DOI: 10.1128/MCB.00017-14
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ABSTRACT

The actin cytoskeleton is essential for cell adhesion and migration, functions important for tumor invasion. In addition to binding N-WASP/WASP, WIP binds and stabilizes F-actin. WIP−/− fibroblasts were used to test the role of WIP in F-actin function. WIP−/− cells had defective focal adhesion (FA), stress fiber assembly, and adherence to substrates, functions that were restored by transduction of wild-type WIP. Protein and mRNA levels of several FA constituents regulated by the myocardin-related transcription factor (MRTF)–serum response factor (SRF) transcription factor complex were reduced in WIP−/− fibroblasts. The level of G-actin, which sequesters MRTF in the cytoplasm, was increased, and nuclear localization of MRTF-A and SRF was reduced, in WIP−/− fibroblasts. Transfection of an MRTF-A mutant that constitutively translocates to the nucleus or transfection of constitutively active SRF restored FA and stress fiber assembly. Fibroblasts from knock-in mice expressing a WIP mutant that fails to bind actin phenocopied WIP−/− fibroblasts. Thus, WIP is a novel regulator of FA assembly and cell adhesion.

FOOTNOTES

    • Received 7 January 2014.
    • Returned for modification 14 February 2014.
    • Accepted 22 April 2014.
    • Accepted manuscript posted online 5 May 2014.
  • Supplemental material for this article may be found at http://dx.doi.org/10.1128/MCB.00017-14.

  • Copyright © 2014, American Society for Microbiology. All Rights Reserved.
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Binding of the WASP/N-WASP-Interacting Protein WIP to Actin Regulates Focal Adhesion Assembly and Adhesion
Narayanaswamy Ramesh, Michel J. Massaad, Lalit Kumar, Suresh Koduru, Yoji Sasahara, Ines Anton, Manoj Bhasin, Towia Libermann, Raif Geha
Molecular and Cellular Biology Jun 2014, 34 (14) 2600-2610; DOI: 10.1128/MCB.00017-14

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Binding of the WASP/N-WASP-Interacting Protein WIP to Actin Regulates Focal Adhesion Assembly and Adhesion
Narayanaswamy Ramesh, Michel J. Massaad, Lalit Kumar, Suresh Koduru, Yoji Sasahara, Ines Anton, Manoj Bhasin, Towia Libermann, Raif Geha
Molecular and Cellular Biology Jun 2014, 34 (14) 2600-2610; DOI: 10.1128/MCB.00017-14
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