TitleGlycine-rich region regulates cysteine-rich protein 1 binding to actin cytoskeleton.
Publication TypeJournal Article
Year of Publication2009
AuthorsJang HSang, Greenwood JA
JournalBiochem Biophys Res Commun
Volume380
Issue3
Pagination484-8
Date Published2009 Mar 13
ISSN1090-2104
KeywordsActins, Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, Avian Proteins, Carrier Proteins, Cytoskeleton, Glycine, LIM Domain Proteins, Molecular Sequence Data, Protein Structure, Tertiary
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.

DOI10.1016/j.bbrc.2009.01.125
Alternate JournalBiochem. Biophys. Res. Commun.
PubMed ID19284992
Grant ListGM 63711 / GM / NIGMS NIH HHS / United States
P30 ES00210 / ES / NIEHS NIH HHS / United States