PHOSPHORYLATION OF FILAMIN (ABP-280) REGULATES THE BINDING TO THE LIPID MEMBRANE, INTEGRIN, AND ACTIN

Authors

  • Wolfgang H. Goldmann

    Corresponding author
    1. Departments of Pathology and Surgery, Children's Hospital, Harvard Medical School, Boston, MA, 02115, U.S.A.
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Department of Medicine, Renal Unit, Massachusetts General Hospital, Harvard Medical School, Building 149, 13th Street, Charlestown MA 02129. U.S.A. Fax: +1 (617) 726 5671. E-mail: wgoldmann@partners.org.

Abstract

Actin-binding protein (ABP-280; filamin) is a phosphoprotein present in the periphery of the cytoplasm, where it can cross-link actin filaments, associate with lipid membranes, and bind to membrane surface receptors. Given its function and localization in the cell, the hypothesis that it serves as a substrate for p56lck, a lymphocyte-specific member of the src family of protein tyrosine kinases associated with cell surface glycoproteins is considered. The results suggest conformationally-induced regulation of filamin (ABP-280).

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