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Mechanisms of the 14-3-3 protein function: regulation of protein function through conformational modulation
V. Obsilova, M. Kopecka, D. Kosek, M. Kacirova, S. Kylarova, L. Rezabkova, T. Obsil
Language English Country Czech Republic
Document type Journal Article, Research Support, Non-U.S. Gov't, Review
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- MeSH
- DNA Glycosylases chemistry ultrastructure MeSH
- DNA-(Apurinic or Apyrimidinic Site) Lyase chemistry ultrastructure MeSH
- Phosphoproteins chemistry ultrastructure MeSH
- Protein Conformation MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Multienzyme Complexes chemistry ultrastructure MeSH
- Eye Proteins chemistry ultrastructure MeSH
- 14-3-3 Proteins chemistry ultrastructure MeSH
- RGS Proteins chemistry ultrastructure MeSH
- GTP-Binding Protein Regulators chemistry ultrastructure MeSH
- Schizosaccharomyces pombe Proteins chemistry ultrastructure MeSH
- Amino Acid Sequence MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Structure-Activity Relationship MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Review MeSH
Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin.
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- $a Many aspects of protein function regulation require specific protein-protein interactions to carry out the exact biochemical and cellular functions. The highly conserved members of the 14-3-3 protein family mediate such interactions and through binding to hundreds of other proteins provide multitude of regulatory functions, thus playing key roles in many cellular processes. The 14-3-3 protein binding can affect the function of the target protein in many ways including the modulation of its enzyme activity, its subcellular localization, its structure and stability, or its molecular interactions. In this minireview, we focus on mechanisms of the 14-3-3 protein-dependent regulation of three important 14-3-3 binding partners: yeast neutral trehalase Nth1, regulator of G-protein signaling 3 (RGS3), and phosducin.
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