Glycine-rich region regulates cysteine-rich protein 1 binding to actin cytoskeleton

Hyo Sang Jang, Jeffrey A. Greenwood

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

Cysteine-rich protein 1 (CRP1) has a unique structure with two well separated LIM domains, each followed by a glycine-rich region. Although CRP1 has been shown to interact with actin-binding proteins and actin filaments, the mechanism regulating localization to the actin cytoskeleton in cells is not clear. Experiments using truncated forms showed that the first LIM domain and glycine-rich region are necessary for CRP1 bundling of actin filaments and localization to the actin cytoskeleton. Furthermore, domain swapping experiments replacing the first glycine-rich region with the second resulted in the loss of CRP1 bundling activity and localization to the actin cytoskeleton, identifying seven critical amino acid residues. These results highlight the importance of the first glycine-rich region for CRP1 bundling activity and localization to the actin cytoskeleton. In addition, this work identifies the first LIM domain and glycine-rich region as a distinct actin filament bundling module.

Original languageEnglish (US)
Pages (from-to)484-488
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume380
Issue number3
DOIs
StatePublished - Mar 13 2009
Externally publishedYes

Keywords

  • Actin bundling
  • Cysteine-rich protein
  • Glycine-rich region
  • LIM domain

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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