Glycine-rich region regulates cysteine-rich protein 1 binding to actin cytoskeleton |
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Authors: | Hyo Sang Jang |
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Affiliation: | Department of Biochemistry and Biophysics, Oregon State University, 2011 ALS, Corvallis, OR 97331-7305, USA |
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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. |
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Keywords: | CRP, cysteine-rich protein GR, glycine-rich region Ni-NTA, nickel-nitrilotriacetic acid YFP, yellow fluorescence protein CFP, cyan fluorescence protein F-actin, filamentous actin TEV, tobacco etch virus |
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