Localization and structure of the ankyrin-binding site on β 2-spectrin

Lydia Davis, Khadar Abdi, Mischa Machius, Chad A Brautigam, Diana R Tomchick, Vann Bennett, Peter A Michaely

Research output: Contribution to journalArticle

48 Scopus citations

Abstract

Spectrins are tetrameric actin-cross-linking proteins that form an elastic network, termed the membrane skeleton, on the cytoplasmic surface of cellular membranes. At the plasma membrane, the membrane skeleton provides essential support, preventing loss of membrane material to environmental shear stresses. The skeleton also controls the location, abundance, and activity of membrane proteins that are critical to cell and tissue function. The ability of the skeleton to modulate membrane stability and function requires adaptor proteins that bind the skeleton to membranes. The principal adaptors are the ankyrin proteins, which bind to the β-subunit of spectrin and to the cytoplasmic domains of numerous integral membrane proteins. Here, we present the crystal structure of the ankyrin-binding domain of human β 2-spectrin at 1.95 Å resolution together with mutagenesis data identifying the binding surface for ankyrins on β 2-spectrin.

Original languageEnglish (US)
Pages (from-to)6982-6987
Number of pages6
JournalJournal of Biological Chemistry
Volume284
Issue number11
DOIs
StatePublished - Mar 13 2009

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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