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Phosphorylation of filamin (ABP-280) regulates the binding to the lipid membrane, integrin, and actin

W H Goldmann1

  • 1Department of Pathology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA. wgoldmann@partners.org

Cell Biology International
|August 3, 2001
PubMed

Insights

Actin-binding protein (ABP-280), also known as filamin, is regulated by conformation changes. This protein interacts with actin filaments and cell surface receptors, suggesting a role in cellular signaling pathways.

Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Actin-binding protein (ABP-280), or filamin, is a cytoplasmic phosphoprotein.
  • It is localized at the cell periphery, cross-linking actin filaments and interacting with membranes and receptors.

Purpose of the Study:

  • To investigate if ABP-280 (filamin) is a substrate for p56lck, a lymphocyte-specific tyrosine kinase.
  • To explore the regulation of filamin's function.

Main Methods:

  • The study considered the hypothesis of filamin being a substrate for p56lck.
  • Experimental results were analyzed to understand filamin's regulation.

Main Results:

  • The findings suggest that filamin (ABP-280) undergoes conformationally-induced regulation.
  • This implies that changes in protein shape influence its activity.

Conclusions:

  • Filamin (ABP-280) is subject to regulation through conformational changes.
  • This regulation may be linked to its interactions with signaling molecules like p56lck.

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